UniProtKB - P80457 (XDH_BOVIN)
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>sp|P80457|XDH_BOVIN Xanthine dehydrogenase/oxidase OS=Bos taurus OX=9913 GN=XDH PE=1 SV=4 MTADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKLGCGEGGCGACTVMLSKYDR LQDKIIHFSANACLAPICTLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGI VMSMYTLLRNQPEPTVEEIEDAFQGNLCRCTGYRPILQGFRTFAKNGGCCGGNGNNPNCC MNQKKDHTVTLSPSLFNPEEFMPLDPTQEPIFPPELLRLKDVPPKQLRFEGERVTWIQAS TLKELLDLKAQHPEAKLVVGNTEIGIEMKFKNQLFPMIICPAWIPELNAVEHGPEGISFG AACALSSVEKTLLEAVAKLPTQKTEVFRGVLEQLRWFAGKQVKSVASLGGNIITASPISD LNPVFMASGTKLTIVSRGTRRTVPMDHTFFPSYRKTLLGPEEILLSIEIPYSREDEFFSA FKQASRREDDIAKVTCGMRVLFQPGSMQVKELALCYGGMADRTISALKTTQKQLSKFWNE KLLQDVCAGLAEELSLSPDAPGGMIEFRRTLTLSFFFKFYLTVLKKLGKDSKDKCGKLDP TYTSATLLFQKDPPANIQLFQEVPNGQSKEDTVGRPLPHLAAAMQASGEAVYCDDIPRYE NELFLRLVTSTRAHAKIKSIDVSEAQKVPGFVCFLSADDIPGSNETGLFNDETVFAKDTV TCVGHIIGAVVADTPEHAERAAHVVKVTYEDLPAIITIEDAIKNNSFYGSELKIEKGDLK KGFSEADNVVSGELYIGGQDHFYLETHCTIAIPKGEEGEMELFVSTQNAMKTQSFVAKML GVPVNRILVRVKRMGGGFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNEDMLITGGRH PFLARYKVGFMKTGTIVALEVDHYSNAGNSRDLSHSIMERALFHMDNCYKIPNIRGTGRL CKTNLSSNTAFRGFGGPQALFIAENWMSEVAVTCGLPAEEVRWKNMYKEGDLTHFNQRLE GFSVPRCWDECLKSSQYYARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGAL IHVYTDGSVLVSHGGTEMGQGLHTKMVQVASKALKIPISKIYISETSTNTVPNSSPTAAS VSTDIYGQAVYEACQTILKRLEPFKKKNPDGSWEDWVMAAYQDRVSLSTTGFYRTPNLGY SFETNSGNAFHYFTYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFV QGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPTEFRVSLLRDCPNKKAIYASKAVG EPPLFLGASVFFAIKDAIRAARAQHTNNNTKELFRLDSPATPEKIRNACVDKFTTLCVTG APGNCKPWSLRVCommunity curation ()Add a publicationFeedback
Xanthine dehydrogenase/oxidase
XDH
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species.
By similarity<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- H2OEC:1.17.1.4
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<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
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+xanthine- Search proteins in UniProtKB for this molecule.
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+urate- Search proteins in UniProtKB for this molecule.
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- H2OEC:1.17.1.4
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Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
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+NADH- Search proteins in UniProtKB for this molecule.
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+xanthine- Search proteins in UniProtKB for this molecule.
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- H2OEC:1.17.3.2
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Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
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Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
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<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Protein has several cofactor binding sites:- [2Fe-2S] cluster
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Manual assertion based on experiment ini
- Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.9"Substrate orientation and catalysis at the molybdenum site in xanthine oxidase: crystal structures in complex with xanthine and lumazine."
Pauff J.M., Cao H., Hille R.
J. Biol. Chem. 284:8760-8767(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS; CALCIUM IONS; XANTHINE AND LUMAZINE, COFACTOR, SUBUNIT.
Manual assertion based on experiment ini
- Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.9"Substrate orientation and catalysis at the molybdenum site in xanthine oxidase: crystal structures in complex with xanthine and lumazine."
Pauff J.M., Cao H., Hille R.
J. Biol. Chem. 284:8760-8767(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS; CALCIUM IONS; XANTHINE AND LUMAZINE, COFACTOR, SUBUNIT.
- FAD
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.9"Substrate orientation and catalysis at the molybdenum site in xanthine oxidase: crystal structures in complex with xanthine and lumazine."
Pauff J.M., Cao H., Hille R.
J. Biol. Chem. 284:8760-8767(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS; CALCIUM IONS; XANTHINE AND LUMAZINE, COFACTOR, SUBUNIT.
- Mo-molybdopterin
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.9"Substrate orientation and catalysis at the molybdenum site in xanthine oxidase: crystal structures in complex with xanthine and lumazine."
Pauff J.M., Cao H., Hille R.
J. Biol. Chem. 284:8760-8767(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS; CALCIUM IONS; XANTHINE AND LUMAZINE, COFACTOR, SUBUNIT.
Manual assertion based on experiment ini
- Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.9"Substrate orientation and catalysis at the molybdenum site in xanthine oxidase: crystal structures in complex with xanthine and lumazine."
Pauff J.M., Cao H., Hille R.
J. Biol. Chem. 284:8760-8767(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS; CALCIUM IONS; XANTHINE AND LUMAZINE, COFACTOR, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.5"Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductase."
Kuwabara Y., Nishino T., Okamoto K., Matsumura T., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 100:8170-8175(2003) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-335; TRP-336 AND ARG-427. - Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=111 µM for molecular oxygen in dehydrogenase form2 Publications
Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.5"Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductase."
Kuwabara Y., Nishino T., Okamoto K., Matsumura T., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 100:8170-8175(2003) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-335; TRP-336 AND ARG-427.
- KM=37.7 µM for molecular oxygen in oxygenase form2 Publications
Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.5"Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductase."
Kuwabara Y., Nishino T., Okamoto K., Matsumura T., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 100:8170-8175(2003) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-335; TRP-336 AND ARG-427.
- KM=20.8 µM for NAD2 Publications
Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.5"Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductase."
Kuwabara Y., Nishino T., Okamoto K., Matsumura T., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 100:8170-8175(2003) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-335; TRP-336 AND ARG-427.
- KM=5 µM for xanthine2 Publications
Manual assertion based on experiment ini
- Ref.4"Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties."
Battelli M.G., Lorenzoni E., Stripe F.
Biochem. J. 131:191-198(1973) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, CONVERSION BY PARTIAL PROTEOLYSIS AND BY REDUCING AGENTS. - Ref.5"Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductase."
Kuwabara Y., Nishino T., Okamoto K., Matsumura T., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 100:8170-8175(2003) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-335; TRP-336 AND ARG-427.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 43 | Iron-sulfur (2Fe-2S) 13 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 48 | Iron-sulfur (2Fe-2S) 13 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 51 | Iron-sulfur (2Fe-2S) 13 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 73 | Iron-sulfur (2Fe-2S) 13 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 113 | Iron-sulfur (2Fe-2S) 23 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 116 | Iron-sulfur (2Fe-2S) 23 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 148 | Iron-sulfur (2Fe-2S) 23 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 150 | Iron-sulfur (2Fe-2S) 23 Publications Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 337 | FAD2 Publications Manual assertion based on experiment ini
| 1 | |
Binding sitei | 360 | FAD2 Publications Manual assertion based on experiment ini
| 1 | |
Binding sitei | 404 | FAD; via amide nitrogen and carbonyl oxygen2 Publications Manual assertion based on experiment ini
| 1 | |
Binding sitei | 422 | FAD2 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 767 | Molybdenum (Mo-molybdopterin metal ligand)3 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 798 | Molybdenum (Mo-molybdopterin metal ligand); via carbonyl oxygen3 Publications Manual assertion based on experiment ini
| 1 | |
Binding sitei | 802 | Substrate | 1 | |
Binding sitei | 880 | Substrate | 1 | |
Metal bindingi | 912 | Molybdenum (Mo-molybdopterin metal ligand); via amide nitrogen3 Publications Manual assertion based on experiment ini
| 1 | |
Binding sitei | 914 | Substrate | 1 | |
Binding sitei | 1010 | Substrate; via amide nitrogen | 1 | |
Metal bindingi | 1079 | Molybdenum (Mo-molybdopterin metal ligand); via amide nitrogen3 Publications Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 1261 | Proton acceptor1 Publication Manual assertion based on experiment ini
| 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 257 – 264 | FAD2 Publications Manual assertion based on experiment ini
| 8 | |
Nucleotide bindingi | 347 – 351 | FAD2 Publications Manual assertion based on experiment ini
| 5 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 2 iron, 2 sulfur cluster binding Source: CAFA
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- FAD binding Source: CAFAInferred from direct assayi
- Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- flavin adenine dinucleotide binding Source: UniProtKB
- iron ion binding Source: InterPro
- molybdenum ion binding Source: CAFAInferred from direct assayi
- Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- molybdopterin cofactor binding Source: CAFAInferred from direct assayi
- Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- oxidoreductase activity Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- protein homodimerization activity Source: CAFAInferred from direct assayi
- Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- xanthine dehydrogenase activity Source: UniProtKB
- xanthine oxidase activity Source: UniProtKB
GO - Biological processi
- xanthine catabolic process Source: UniProtKB
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | Oxidoreductase |
Ligand | 2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.17.1.4, 908 1.17.3.2, 908 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P80457 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Xanthine dehydrogenase/oxidaseIncluding the following 2 domains: Xanthine dehydrogenase (EC:1.17.1.4
Manual assertion based on experiment ini
Short name: XD Xanthine oxidase (EC:1.17.3.2
Manual assertion based on experiment ini
Short name: XO Alternative name(s): Xanthine oxidoreductase Short name: XOR |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:XDH |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Bos taurus (Bovine) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9913 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Extracellular region or secreted
Peroxisome
Cytoplasm and Cytosol
- Cytoplasm By similarity
Extracellular region or secreted
- extracellular space Source: CAFAInferred from direct assayi
- Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- extracellular space Source: CAFAInferred from direct assayi
Peroxisome
- peroxisome Source: UniProtKB-SubCell
Other locations
- xanthine dehydrogenase complex Source: CAFAInferred from direct assayi
- Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- xanthine dehydrogenase complex Source: CAFAInferred from direct assayi
Keywords - Cellular componenti
Cytoplasm, Peroxisome, Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 335 | R → A: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 336 | W → A: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 427 | R → Q: Promotes conversion to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents. 1 Publication Manual assertion based on experiment ini
| 1 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3649 |
DrugCentral More...DrugCentrali | P80457 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication Manual assertion based on experiment ini
| |||
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000166082 | 2 – 1332 | Xanthine dehydrogenase/oxidaseAdd BLAST | 1331 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 535 ↔ 992 | In oxidase formBy similarity |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Keywords - PTMi
Disulfide bondProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P80457 |
PeptideAtlas More...PeptideAtlasi | P80457 |
PRoteomics IDEntifications database More...PRIDEi | P80457 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Manual assertion based on experiment ini
- Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.7"An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition."
Okamoto K., Eger B.T., Nishino T., Kondo S., Pai E.F., Nishino T.
J. Biol. Chem. 278:1848-1855(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND SYNTHETIC INHIBITOR TEI-6720, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.8"The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition."
Okamoto K., Matsumoto K., Hille R., Eger B.T., Pai E.F., Nishino T.
Proc. Natl. Acad. Sci. U.S.A. 101:7931-7936(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH FAD; MOLYBDOPTERIN; IRON-SULFUR CENTERS AND INHIBITOR FYX-051, ACTIVE SITE, COFACTOR, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.
Interacts with BTN1A1 (By similarity).
By similarityGO - Molecular functioni
- protein homodimerization activity Source: CAFAInferred from direct assayi
- Ref.6"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion."
Enroth C., Eger B.T., Okamoto K., Nishino T., Nishino T., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 97:10723-10728(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH FAD; IRON-SULFUR CENTERS; SALICYLATE, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Protein-protein interaction databases
Protein interaction database and analysis system More...IntActi | P80457, 1 interactor |
STRING: functional protein association networks More...STRINGi | 9913.ENSBTAP00000016620 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P80457 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 6 – 10 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 13 – 17 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 26 – 32 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 44 – 48 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 52 – 59 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 60 – 63 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 64 – 71 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Turni | 72 – 74 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 77 – 79 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 84 – 86 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 88 – 90 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 94 – 96 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 100 – 107 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 117 – 130 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
Helixi | 136 – 140 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 142 – 145 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 149 – 151 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 154 – 161 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 198 – 200 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 206 – 208 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 214 – 218 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 219 – 221 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 227 – 230 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 235 – 238 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 242 – 251 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 264 – 270 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 276 – 280 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 285 – 287 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 290 – 292 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 294 – 300 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 305 – 318 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
Helixi | 321 – 323 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 325 – 334 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 336 – 338 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 340 – 343 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 348 – 354 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 362 – 367 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 371 – 376 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 379 – 384 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 387 – 389 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 403 – 410 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 416 – 422 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 428 – 431 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 435 – 443 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 446 – 462 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 | |
Helixi | 467 – 471 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 472 – 475 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 477 – 479 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 480 – 493 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
Helixi | 505 – 527 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 23 | |
Turni | 540 – 542 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 543 – 546 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 555 – 559 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 582 – 586 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 593 – 595 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 603 – 609 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 611 – 621 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 625 – 627 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 631 – 635 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 637 – 639 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 644 – 647 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 652 – 655 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 658 – 660 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 666 – 674 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 675 – 683 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 686 – 691 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 698 – 703 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 707 – 717 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 719 – 725 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 727 – 736 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 748 – 753 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 760 – 764 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 769 – 780 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
Helixi | 784 – 786 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 787 – 791 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 798 – 801 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 806 – 819 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
Beta strandi | 823 – 826 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 829 – 835 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 842 – 850 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 856 – 866 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 874 – 883 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Turni | 884 – 888 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 892 – 901 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Turni | 912 – 915 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 916 – 934 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 19 | |
Helixi | 938 – 945 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 964 – 974 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 977 – 990 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
Beta strandi | 992 – 1008 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 | |
Helixi | 1012 – 1014 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 1016 – 1023 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 1029 – 1034 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 1038 – 1040 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 1042 – 1054 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
Helixi | 1058 – 1060 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 1061 – 1063 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 1068 – 1070 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 1079 – 1081 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 1082 – 1107 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 26 | |
Helixi | 1113 – 1122 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 1128 – 1134 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 1142 – 1145 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 1151 – 1165 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
Turni | 1166 – 1168 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 1171 – 1181 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 1188 – 1207 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 20 | |
Turni | 1224 – 1226 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 1232 – 1234 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 1237 – 1243 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 1253 – 1255 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 1264 – 1267 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 1268 – 1285 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 18 | |
Helixi | 1302 – 1308 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 1312 – 1314 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 1317 – 1319 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P80457 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P80457 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 4 – 91 | 2Fe-2S ferredoxin-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 88 | |
Domaini | 229 – 414 | FAD-binding PCMH-typePROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 186 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0430, Eukaryota |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P80457 |
Database of Orthologous Groups More...OrthoDBi | 48717at2759 |
Family and domain databases
Database of protein disorder More...DisProti | DP00450 |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.10.20.30, 1 hit 3.30.43.10, 1 hit 3.30.465.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002888, 2Fe-2S-bd IPR036884, 2Fe-2S-bd_dom_sf IPR036010, 2Fe-2S_ferredoxin-like_sf IPR001041, 2Fe-2S_ferredoxin-type IPR006058, 2Fe2S_fd_BS IPR000674, Ald_Oxase/Xan_DH_a/b IPR036856, Ald_Oxase/Xan_DH_a/b_sf IPR016208, Ald_Oxase/xanthine_DH IPR008274, AldOxase/xan_DH_Mopterin-bd IPR037165, AldOxase/xan_DH_Mopterin-bd_sf IPR012675, Beta-grasp_dom_sf IPR005107, CO_DH_flav_C IPR036683, CO_DH_flav_C_dom_sf IPR016166, FAD-bd_PCMH IPR036318, FAD-bd_PCMH-like_sf IPR016167, FAD-bd_PCMH_sub1 IPR016169, FAD-bd_PCMH_sub2 IPR002346, Mopterin_DH_FAD-bd IPR022407, OxRdtase_Mopterin_BS IPR014307, Xanthine_DH_ssu |
The PANTHER Classification System More...PANTHERi | PTHR11908, PTHR11908, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01315, Ald_Xan_dh_C, 1 hit PF02738, Ald_Xan_dh_C2, 1 hit PF03450, CO_deh_flav_C, 1 hit PF00941, FAD_binding_5, 1 hit PF00111, Fer2, 1 hit PF01799, Fer2_2, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000127, Xanthine_DH, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01008, Ald_Xan_dh_C, 1 hit SM01092, CO_deh_flav_C, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47741, SSF47741, 1 hit SSF54292, SSF54292, 1 hit SSF54665, SSF54665, 1 hit SSF55447, SSF55447, 1 hit SSF56003, SSF56003, 1 hit SSF56176, SSF56176, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR02963, xanthine_xdhA, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00197, 2FE2S_FER_1, 1 hit PS51085, 2FE2S_FER_2, 1 hit PS51387, FAD_PCMH, 1 hit PS00559, MOLYBDOPTERIN_EUK, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA
60 70 80 90 100
CTVMLSKYDR LQDKIIHFSA NACLAPICTL HHVAVTTVEG IGSTKTRLHP
110 120 130 140 150
VQERIAKSHG SQCGFCTPGI VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC
160 170 180 190 200
TGYRPILQGF RTFAKNGGCC GGNGNNPNCC MNQKKDHTVT LSPSLFNPEE
210 220 230 240 250
FMPLDPTQEP IFPPELLRLK DVPPKQLRFE GERVTWIQAS TLKELLDLKA
260 270 280 290 300
QHPEAKLVVG NTEIGIEMKF KNQLFPMIIC PAWIPELNAV EHGPEGISFG
310 320 330 340 350
AACALSSVEK TLLEAVAKLP TQKTEVFRGV LEQLRWFAGK QVKSVASLGG
360 370 380 390 400
NIITASPISD LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PSYRKTLLGP
410 420 430 440 450
EEILLSIEIP YSREDEFFSA FKQASRREDD IAKVTCGMRV LFQPGSMQVK
460 470 480 490 500
ELALCYGGMA DRTISALKTT QKQLSKFWNE KLLQDVCAGL AEELSLSPDA
510 520 530 540 550
PGGMIEFRRT LTLSFFFKFY LTVLKKLGKD SKDKCGKLDP TYTSATLLFQ
560 570 580 590 600
KDPPANIQLF QEVPNGQSKE DTVGRPLPHL AAAMQASGEA VYCDDIPRYE
610 620 630 640 650
NELFLRLVTS TRAHAKIKSI DVSEAQKVPG FVCFLSADDI PGSNETGLFN
660 670 680 690 700
DETVFAKDTV TCVGHIIGAV VADTPEHAER AAHVVKVTYE DLPAIITIED
710 720 730 740 750
AIKNNSFYGS ELKIEKGDLK KGFSEADNVV SGELYIGGQD HFYLETHCTI
760 770 780 790 800
AIPKGEEGEM ELFVSTQNAM KTQSFVAKML GVPVNRILVR VKRMGGGFGG
810 820 830 840 850
KETRSTLVSV AVALAAYKTG HPVRCMLDRN EDMLITGGRH PFLARYKVGF
860 870 880 890 900
MKTGTIVALE VDHYSNAGNS RDLSHSIMER ALFHMDNCYK IPNIRGTGRL
910 920 930 940 950
CKTNLSSNTA FRGFGGPQAL FIAENWMSEV AVTCGLPAEE VRWKNMYKEG
960 970 980 990 1000
DLTHFNQRLE GFSVPRCWDE CLKSSQYYAR KSEVDKFNKE NCWKKRGLCI
1010 1020 1030 1040 1050
IPTKFGISFT VPFLNQAGAL IHVYTDGSVL VSHGGTEMGQ GLHTKMVQVA
1060 1070 1080 1090 1100
SKALKIPISK IYISETSTNT VPNSSPTAAS VSTDIYGQAV YEACQTILKR
1110 1120 1130 1140 1150
LEPFKKKNPD GSWEDWVMAA YQDRVSLSTT GFYRTPNLGY SFETNSGNAF
1160 1170 1180 1190 1200
HYFTYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
1210 1220 1230 1240 1250
QGLGLFTLEE LHYSPEGSLH TRGPSTYKIP AFGSIPTEFR VSLLRDCPNK
1260 1270 1280 1290 1300
KAIYASKAVG EPPLFLGASV FFAIKDAIRA ARAQHTNNNT KELFRLDSPA
1310 1320 1330
TPEKIRNACV DKFTTLCVTG APGNCKPWSL RV
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 188 | T → TQ in CAA67117 (PubMed:9388547).Curated | 1 | |
Sequence conflicti | 199 | E → K in CAA67117 (PubMed:9388547).Curated | 1 | |
Sequence conflicti | 366 | M → V in CAA67117 (PubMed:9388547).Curated | 1 | |
Sequence conflicti | 552 | D → H in CAA58497 (PubMed:8708081).Curated | 1 | |
Sequence conflicti | 958 | R → K in CAA67117 (PubMed:9388547).Curated | 1 | |
Sequence conflicti | 976 | Q → E in CAA67117 (PubMed:9388547).Curated | 1 | |
Sequence conflicti | 1039 – 1040 | GQ → E in CAA67117 (PubMed:9388547).Curated | 2 | |
Sequence conflicti | 1244 | L → V in CAA67117 (PubMed:9388547).Curated | 1 | |
Sequence conflicti | 1268 | A → P in CAA67117 (PubMed:9388547).Curated | 1 | |
Sequence conflicti | 1279 – 1281 | RAA → ARG in CAA67117 (PubMed:9388547).Curated | 3 |
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X83508 mRNA Translation: CAA58497.1 X98491 mRNA Translation: CAA67117.1 |
Protein sequence database of the Protein Information Resource More...PIRi | S65135 |
NCBI Reference Sequences More...RefSeqi | NP_776397.1, NM_173972.2 |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 280960 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | bta:280960 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P80457 | Xanthine dehydrogenase/oxidase | 1332 | UniRef100_P80457 | |||
+5 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P80457 | Xanthine dehydrogenase/oxidase | 1332 | UniRef90_P80457 | |||
Xanthine dehydrogenase | 1377 | |||||
Xanthine dehydrogenase/oxidase | 1350 | |||||
Xanthine dehydrogenase/oxidase | 1339 | |||||
Xanthine dehydrogenase/oxidase | 1334 | |||||
+50 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P80457 | Xanthine dehydrogenase/oxidase | 1358 | UniRef50_P80457 | |||
Xanthine dehydrogenase/oxidase | 1332 | |||||
Xanthine dehydrogenase | 1377 | |||||
Xanthine dehydrogenase/oxidase | 1350 | |||||
Xanthine dehydrogenase/oxidase | 1339 | |||||
+461 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
Worthington enzyme manual |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X83508 mRNA Translation: CAA58497.1 X98491 mRNA Translation: CAA67117.1 |
PIRi | S65135 |
RefSeqi | NP_776397.1, NM_173972.2 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1FIQ | X-ray | 2.50 | A | 1-219 | [»] | |
B | 220-569 | [»] | ||||
C | 570-1332 | [»] | ||||
1FO4 | X-ray | 2.10 | A/B | 1-1332 | [»] | |
1N5X | X-ray | 2.80 | A/B | 2-1332 | [»] | |
1V97 | X-ray | 1.94 | A/B | 1-1332 | [»] | |
1VDV | X-ray | 1.98 | A/B | 1-1332 | [»] | |
3AM9 | X-ray | 2.17 | A/B | 1-1332 | [»] | |
3AMZ | X-ray | 2.10 | A/B | 1-1332 | [»] | |
3AX7 | X-ray | 2.34 | A/B | 1-1332 | [»] | |
3AX9 | X-ray | 2.30 | A/B | 1-1332 | [»] | |
3B9J | X-ray | 2.30 | A/I | 1-219 | [»] | |
B/J | 220-569 | [»] | ||||
C/K | 570-1332 | [»] | ||||
3BDJ | X-ray | 2.00 | A/B | 1-1332 | [»] | |
3ETR | X-ray | 2.20 | A/L | 2-165 | [»] | |
B/M | 224-528 | [»] | ||||
C/N | 571-1325 | [»] | ||||
3EUB | X-ray | 2.60 | 2/A/J/S | 1-165 | [»] | |
3/B/K/T | 224-528 | [»] | ||||
4/C/L/U | 571-1332 | [»] | ||||
3NRZ | X-ray | 1.80 | A/J | 2-165 | [»] | |
B/K | 224-528 | [»] | ||||
C/L | 571-1326 | [»] | ||||
3NS1 | X-ray | 2.60 | A/J | 2-165 | [»] | |
B/K | 224-528 | [»] | ||||
C/L | 571-1325 | [»] | ||||
3NVV | X-ray | 1.82 | A/J | 2-165 | [»] | |
B/K | 195-528 | [»] | ||||
C/L | 571-1325 | [»] | ||||
3NVW | X-ray | 1.60 | A/J | 2-165 | [»] | |
B/K | 195-528 | [»] | ||||
C/L | 571-1326 | [»] | ||||
3NVY | X-ray | 2.00 | A/J | 2-165 | [»] | |
B/K | 195-528 | [»] | ||||
C/L | 571-1326 | [»] | ||||
3NVZ | X-ray | 1.60 | A/J | 2-165 | [»] | |
B/K | 224-528 | [»] | ||||
C/L | 571-1325 | [»] | ||||
3SR6 | X-ray | 2.10 | A/J | 2-165 | [»] | |
B/K | 224-528 | [»] | ||||
C/L | 571-1315 | [»] | ||||
3UNA | X-ray | 1.90 | A/B | 1-1332 | [»] | |
3UNC | X-ray | 1.65 | A/B | 1-1332 | [»] | |
3UNI | X-ray | 2.20 | A/B | 1-1332 | [»] | |
7D6O | X-ray | 1.99 | A/B | 1-1332 | [»] | |
SMRi | P80457 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P80457, 1 interactor |
STRINGi | 9913.ENSBTAP00000016620 |
Chemistry databases
BindingDBi | P80457 |
ChEMBLi | CHEMBL3649 |
DrugCentrali | P80457 |
Proteomic databases
PaxDbi | P80457 |
PeptideAtlasi | P80457 |
PRIDEi | P80457 |
Genome annotation databases
GeneIDi | 280960 |
KEGGi | bta:280960 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 7498 |
Phylogenomic databases
eggNOGi | KOG0430, Eukaryota |
InParanoidi | P80457 |
OrthoDBi | 48717at2759 |
Enzyme and pathway databases
BRENDAi | 1.17.1.4, 908 1.17.3.2, 908 |
SABIO-RKi | P80457 |
Miscellaneous databases
EvolutionaryTracei | P80457 |
Protein Ontology More...PROi | PR:P80457 |
Family and domain databases
DisProti | DP00450 |
Gene3Di | 3.10.20.30, 1 hit 3.30.43.10, 1 hit 3.30.465.10, 1 hit |
InterProi | View protein in InterPro IPR002888, 2Fe-2S-bd IPR036884, 2Fe-2S-bd_dom_sf IPR036010, 2Fe-2S_ferredoxin-like_sf IPR001041, 2Fe-2S_ferredoxin-type IPR006058, 2Fe2S_fd_BS IPR000674, Ald_Oxase/Xan_DH_a/b IPR036856, Ald_Oxase/Xan_DH_a/b_sf IPR016208, Ald_Oxase/xanthine_DH IPR008274, AldOxase/xan_DH_Mopterin-bd IPR037165, AldOxase/xan_DH_Mopterin-bd_sf IPR012675, Beta-grasp_dom_sf IPR005107, CO_DH_flav_C IPR036683, CO_DH_flav_C_dom_sf IPR016166, FAD-bd_PCMH IPR036318, FAD-bd_PCMH-like_sf IPR016167, FAD-bd_PCMH_sub1 IPR016169, FAD-bd_PCMH_sub2 IPR002346, Mopterin_DH_FAD-bd IPR022407, OxRdtase_Mopterin_BS IPR014307, Xanthine_DH_ssu |
PANTHERi | PTHR11908, PTHR11908, 1 hit |
Pfami | View protein in Pfam PF01315, Ald_Xan_dh_C, 1 hit PF02738, Ald_Xan_dh_C2, 1 hit PF03450, CO_deh_flav_C, 1 hit PF00941, FAD_binding_5, 1 hit PF00111, Fer2, 1 hit PF01799, Fer2_2, 1 hit |
PIRSFi | PIRSF000127, Xanthine_DH, 1 hit |
SMARTi | View protein in SMART SM01008, Ald_Xan_dh_C, 1 hit SM01092, CO_deh_flav_C, 1 hit |
SUPFAMi | SSF47741, SSF47741, 1 hit SSF54292, SSF54292, 1 hit SSF54665, SSF54665, 1 hit SSF55447, SSF55447, 1 hit SSF56003, SSF56003, 1 hit SSF56176, SSF56176, 1 hit |
TIGRFAMsi | TIGR02963, xanthine_xdhA, 1 hit |
PROSITEi | View protein in PROSITE PS00197, 2FE2S_FER_1, 1 hit PS51085, 2FE2S_FER_2, 1 hit PS51387, FAD_PCMH, 1 hit PS00559, MOLYBDOPTERIN_EUK, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | XDH_BOVIN | |
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P80457Primary (citable) accession number: P80457 Secondary accession number(s): Q95325 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1996 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 174 of the entry and version 4 of the sequence. See complete history. | ||
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families