UniProtKB - P0AF18 (NAGA_ECOLI)
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>sp|P0AF18|NAGA_ECOLI N-acetylglucosamine-6-phosphate deacetylase OS=Escherichia coli (strain K12) OX=83333 GN=nagA PE=1 SV=1 MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQL NGCGGVQFNDTAEAVSVETLEIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLAK HPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLCENADVITKVTLAPEMVPAEV ISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEAD IYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCV DENGTLSGSSLTMIEGVRNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANL TAFTPDFKITKTIVNGNEVVTQCommunity curation ()Add a publicationFeedback
N-acetylglucosamine-6-phosphate deacetylase
nagA
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
<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.2"Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli."
Peri K.G., Goldie H., Waygood E.B.
Biochem. Cell Biol. 68:123-137(1990) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. - Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
<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:3.5.1.25
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Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
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Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
Source: Rhea- Search for this reaction in UniProtKB.
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+N-acetyl-D-glucosamine 6-phosphate- Search proteins in UniProtKB for this molecule.
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=acetate- Search proteins in UniProtKB for this molecule.
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+D-glucosamine 6-phosphate- Search proteins in UniProtKB for this molecule.
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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
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Manual assertion based on experiment ini
- Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
- 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.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
- 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.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
- 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.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
Manual assertion based on experiment ini
- Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
<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.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT.
<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
Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM.
- KM=0.3 mM for N-acetyl-glucosamine 6-phosphate (at 30 degrees Celsius and pH 7.5)3 Publications
Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM.
- KM=0.8 mM for N-acetyl-glucosamine 6-phosphate (at 37 degrees Celsius and pH 8.0)3 Publications
Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM.
- KM=20 mM for glucosamine 6-phosphate (at 30 degrees Celsius and pH 7.5)3 Publications
Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM.
- KM=20 mM for acetate (at 30 degrees Celsius and pH 7.5)3 Publications
Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM.
- KM=0.08 mM for N-acetyl-D-glucosamine-6-phosphate (at 30 degrees Celsius and pH 7.5 using Zn-reconstituted form of the enzyme)3 Publications
Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM.
- KM=1.24 mM for N-acetyl-D-galactosamine-6-phosphate (at 30 degrees Celsius and pH 7.5 using Zn-reconstituted form of the enzyme)3 Publications
Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM.
pH dependencei
Manual assertion based on experiment ini
- Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: N-acetylneuraminate degradation
This protein is involved in step 4 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.1 Publication<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.2"Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli."
Peri K.G., Goldie H., Waygood E.B.
Biochem. Cell Biol. 68:123-137(1990) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
- N-acetylneuraminate lyase (nanA), N-acetylneuraminate lyase (nanA)
- N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK)
- Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE), Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
- N-acetylglucosamine-6-phosphate deacetylase (nagA)
- Glucosamine-6-phosphate deaminase (nagB), Glucosamine-6-phosphate deaminase (nagB)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate, the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.
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 | 131 | Zinc1 Publication Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 195 | Zinc; via tele nitrogen1 Publication Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 216 | Zinc; via tele nitrogen1 Publication 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 | 227 | Substrate1 Publication 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 | 273 | Proton donor/acceptor1 Publication Manual assertion based on experiment ini
| 1 |
<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
- N-acetylgalactosamine-6-phosphate deacetylase activity Source: UniProtKB-EC
- N-acetylglucosamine-6-phosphate deacetylase activity Source: UniProtKB
<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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE. - Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- zinc ion binding Source: UniProtKBInferred from direct assayi
- Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
GO - Biological processi
- carbohydrate metabolic process Source: UniProtKB-KW
- N-acetylglucosamine catabolic process Source: UniProtKBInferred from direct assayi
- Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE. - Ref.6"The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli."
White R.J., Pasternak C.A.
Biochem. J. 105:121-125(1967) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM.
- N-acetylneuraminate catabolic process Source: EcoCyc
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "Transport and catabolism of the sialic acids N-glycolylneuraminic acid and 3-keto-3-deoxy-D-glycero-D-galactonononic acid by Escherichia coli K-12."
Hopkins A.P., Hawkhead J.A., Thomas G.H.
FEMS Microbiol. Lett. 347:14-22(2013) [PubMed] [Europe PMC] [Abstract]
- protein homotetramerization Source: UniProtKBInferred from direct assayi
- Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE. - Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM.
<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 | Hydrolase |
Biological process | Carbohydrate metabolism |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:NAG6PDEACET-MONOMER MetaCyc:NAG6PDEACET-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.5.1.25, 2026 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P0AF18 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00629;UER00683 |
<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: N-acetylglucosamine-6-phosphate deacetylase1 Publication<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: GlcNAc 6-P deacetylase1 Publication Manual assertion based on opinion ini
|
<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:nagA Ordered Locus Names:b0677, JW0663 |
<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 | Escherichia coli (strain K12) |
<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 | 83333 [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 › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
<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 disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
Manual assertion based on experiment ini
- Ref.7"Coordinated regulation of amino sugar-synthesizing and -degrading enzymes in Escherichia coli K-12."
Plumbridge J.A., Cochet O., Souza J.M., Altamirano M.M., Calcagno M.L., Badet B.
J. Bacteriol. 175:4951-4956(1993) [PubMed] [Europe PMC] [Abstract]Cited for: DISRUPTION PHENOTYPE.
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 | 59 | Q → H: Large decrease in catalytic activity and substrate affinity, and increase in the average amount of Zn bound to the protein, suggesting that an additional metal ion can bind to this mutant; when associated with H-61. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 61 | N → H: Large decrease in catalytic activity and substrate affinity, and increase in the average amount of Zn bound to the protein, suggesting that an additional metal ion can bind to this mutant; when associated with H-59. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 131 | E → Q or A: Large reduction in the amount of the metal cofactor bound to the enzyme. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 143 | H → N: Dramatic decrease in catalytic activity and moderate decrease in substrate affinity, producing a 6000-fold decrease in catalytic efficiency. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 143 | H → Q: 180-fold decrease in catalytic efficiency. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 251 | H → N: 500-fold decrease in catalytic efficiency. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 273 | D → N or A: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 |
<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 '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_0000170915 | 1 – 382 | N-acetylglucosamine-6-phosphate deacetylaseAdd BLAST | 382 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P0AF18 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0AF18 |
PRoteomics IDEntifications database More...PRIDEi | P0AF18 |
<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Manual assertion based on experiment ini
- Ref.10"Identification and molecular characterization of the Mg2+ stimulon of Escherichia coli."
Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T., Mori H., Ishihama A., Utsumi R.
J. Bacteriol. 185:3696-3702(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION.
<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
Homotetramer.
4 PublicationsManual assertion based on experiment ini
- Ref.8"N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization."
Souza J.M., Plumbridge J.A., Calcagno M.L.
Arch. Biochem. Biophys. 340:338-346(1997) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, REACTION MECHANISM. - Ref.11"N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion."
Hall R.S., Xiang D.F., Xu C., Raushel F.M.
Biochemistry 46:7942-7952(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, REACTION MECHANISM. - Ref.12"Structural analysis of N-acetylglucosamine-6-phosphate deacetylase apoenzyme from Escherichia coli."
Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R., Fischer H., Calcagno M.L., Oliva G.
J. Mol. Biol. 359:308-321(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT. - Ref.13"Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase."
Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C., Almo S.C., Raushel F.M.
Biochemistry 46:7953-7962(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-273, COFACTOR, SUBUNIT, ACTIVE SITE.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4261208, 26 interactors |
Database of interacting proteins More...DIPi | DIP-10297N |
Protein interaction database and analysis system More...IntActi | P0AF18, 5 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b0677 |
<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 | 2 – 10 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 15 – 24 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 27 – 33 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
<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 | 34 – 36 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 43 – 45 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 50 – 53 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 55 – 63 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 66 – 71 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
<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 | 72 – 74 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 77 – 89 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Beta strandi | 92 – 100 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 104 – 120 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
Beta strandi | 123 – 125 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 128 – 131 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 137 – 139 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 145 – 147 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 150 – 161 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Turni | 162 – 165 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 166 – 171 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 173 – 175 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 178 – 186 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 190 – 193 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 200 – 209 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 213 – 216 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 217 – 220 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 230 – 237 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 242 – 246 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 248 – 252 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 254 – 264 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 265 – 267 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 268 – 271 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 276 – 279 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 283 – 287 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 290 – 294 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 298 – 301 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 306 – 309 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 313 – 324 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Helixi | 328 – 335 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 337 – 342 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Turni | 346 – 348 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 349 – 351 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 360 – 363 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 369 – 374 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 377 – 381 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0AF18 |
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 | P0AF18 |
<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
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 142 – 143 | Substrate binding1 Publication Manual assertion based on experiment ini
| 2 | |
Regioni | 219 – 220 | Substrate binding1 Publication Manual assertion based on experiment ini
| 2 | |
Regioni | 248 – 251 | Substrate binding1 Publication Manual assertion based on experiment ini
| 4 | |
Regioni | 306 – 308 | Substrate binding1 Publication Manual assertion based on experiment ini
| 3 |
<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 | COG1820, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_032482_2_2_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0AF18 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0AF18 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00854, NagA, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.30.40.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR003764, GlcNAc_6-P_deAcase IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase |
The PANTHER Classification System More...PANTHERi | PTHR11113:SF14, PTHR11113:SF14, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF038994, NagA, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51338, SSF51338, 1 hit SSF51556, SSF51556, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00221, nagA, 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.
10 20 30 40 50
MYALTQGRIF TGHEFLDDHA VVIADGLIKS VCPVAELPPE IEQRSLNGAI
60 70 80 90 100
LSPGFIDVQL NGCGGVQFND TAEAVSVETL EIMQKANEKS GCTNYLPTLI
110 120 130 140 150
TTSDELMKQG VRVMREYLAK HPNQALGLHL EGPWLNLVKK GTHNPNFVRK
160 170 180 190 200
PDAALVDFLC ENADVITKVT LAPEMVPAEV ISKLANAGIV VSAGHSNATL
210 220 230 240 250
KEAKAGFRAG ITFATHLYNA MPYITGREPG LAGAILDEAD IYCGIIADGL
260 270 280 290 300
HVDYANIRNA KRLKGDKLCL VTDATAPAGA NIEQFIFAGK TIYYRNGLCV
310 320 330 340 350
DENGTLSGSS LTMIEGVRNL VEHCGIALDE VLRMATLYPA RAIGVEKRLG
360 370 380
TLAAGKVANL TAFTPDFKIT KTIVNGNEVV TQ
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 | X14135 Genomic DNA Translation: CAA32353.1 AF052007 Genomic DNA Translation: AAC09325.1 U00096 Genomic DNA Translation: AAC73771.1 AP009048 Genomic DNA Translation: BAA35320.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A37018 |
NCBI Reference Sequences More...RefSeqi | NP_415203.1, NC_000913.3 WP_000271153.1, NZ_STEB01000044.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC73771; AAC73771; b0677 BAA35320; BAA35320; BAA35320 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 57728780 945289 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW0663 eco:b0677 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.1601 |
<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 | |
---|---|---|---|---|---|---|
P0AF18 | N-acetylglucosamine-6-phosphate deacetylase | 382 | UniRef100_P0AF19 | |||
N-acetylglucosamine-6-phosphate deacetylase | 397 | |||||
N-acetylglucosamine-6-phosphate deacetylase | 382 | |||||
N-acetylglucosamine-6-phosphate deacetylase | 382 | |||||
N-acetylglucosamine-6-phosphate deacetylase | 382 | |||||
+66 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P0AF18 | N-acetylglucosamine-6-phosphate deacetylase | 382 | UniRef90_P0AF19 | |||
N-acetylglucosamine-6-phosphate deacetylase | 397 | |||||
N-acetylglucosamine-6-phosphate deacetylase | 382 | |||||
N-acetylglucosamine-6-phosphate deacetylase | 382 | |||||
N-acetylglucosamine-6-phosphate deacetylase | 382 | |||||
+756 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P0AF18 | N-acetylglucosamine-6-phosphate deacetylase | 382 | UniRef50_P0AF19 | |||
N-acetylglucosamine-6-phosphate deacetylase | 381 | |||||
N-acetylglucosamine-6-phosphate deacetylase | 397 | |||||
N-acetylglucosamine-6-phosphate deacetylase | 382 | |||||
N-acetylglucosamine-6-phosphate deacetylase | 382 | |||||
+3666 |
<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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X14135 Genomic DNA Translation: CAA32353.1 AF052007 Genomic DNA Translation: AAC09325.1 U00096 Genomic DNA Translation: AAC73771.1 AP009048 Genomic DNA Translation: BAA35320.1 |
PIRi | A37018 |
RefSeqi | NP_415203.1, NC_000913.3 WP_000271153.1, NZ_STEB01000044.1 |
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 |
1YMY | X-ray | 2.60 | A/B | 1-382 | [»] | |
1YRR | X-ray | 2.00 | A/B | 1-382 | [»] | |
2P50 | X-ray | 2.20 | A/B/C/D | 1-382 | [»] | |
2P53 | X-ray | 2.10 | A/B | 1-382 | [»] | |
SMRi | P0AF18 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261208, 26 interactors |
DIPi | DIP-10297N |
IntActi | P0AF18, 5 interactors |
STRINGi | 511145.b0677 |
Proteomic databases
jPOSTi | P0AF18 |
PaxDbi | P0AF18 |
PRIDEi | P0AF18 |
Genome annotation databases
EnsemblBacteriai | AAC73771; AAC73771; b0677 BAA35320; BAA35320; BAA35320 |
GeneIDi | 57728780 945289 |
KEGGi | ecj:JW0663 eco:b0677 |
PATRICi | fig|1411691.4.peg.1601 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0626 |
Phylogenomic databases
eggNOGi | COG1820, Bacteria |
HOGENOMi | CLU_032482_2_2_6 |
InParanoidi | P0AF18 |
PhylomeDBi | P0AF18 |
Enzyme and pathway databases
UniPathwayi | UPA00629;UER00683 |
BioCyci | EcoCyc:NAG6PDEACET-MONOMER MetaCyc:NAG6PDEACET-MONOMER |
BRENDAi | 3.5.1.25, 2026 |
SABIO-RKi | P0AF18 |
Miscellaneous databases
EvolutionaryTracei | P0AF18 |
Protein Ontology More...PROi | PR:P0AF18 |
Family and domain databases
CDDi | cd00854, NagA, 1 hit |
Gene3Di | 2.30.40.10, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR003764, GlcNAc_6-P_deAcase IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase |
PANTHERi | PTHR11113:SF14, PTHR11113:SF14, 1 hit |
Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit |
PIRSFi | PIRSF038994, NagA, 1 hit |
SUPFAMi | SSF51338, SSF51338, 1 hit SSF51556, SSF51556, 1 hit |
TIGRFAMsi | TIGR00221, nagA, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
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 | NAGA_ECOLI | |
<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 | P0AF18Primary (citable) accession number: P0AF18 Secondary accession number(s): P15300 | |
<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: | December 20, 2005 |
Last sequence update: | December 20, 2005 | |
Last modified: | April 7, 2021 | |
This is version 118 of the entry and version 1 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 | Prokaryotic 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, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families