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UniProtKB - P62623 (ISPH_ECOLI)
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>sp|P62623|ISPH_ECOLI 4-hydroxy-3-methylbut-2-enyl diphosphate reductase OS=Escherichia coli (strain K12) OX=83333 GN=ispH PE=1 SV=1 MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQI SEVPDGAILIFSAHGVSQAVRNEAKSRDLTVFDATCPLVTKVHMEVARASRRGEESILIG HAGHPEVEGTMGQYSNPEGGMYLVESPDDVWKLTVKNEEKLSFMTQTTLSVDDTSDVIDA LRKRFPKIVGPRKDDICYATTNRQEAVRALAEQAEVVLVVGSKNSSNSNRLAELAQRMGK RAFLIDDAKDIQEEWVKEVKCVGVTAGASAPDILVQNVVARLQQLGGGEAIPLEGREENI VFEVPKELRVDIREVDCommunity curation ()Add a publicationFeedback
Protein
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Gene
ispH
Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:
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
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis (PubMed:11818558, PubMed:11418107, PubMed:12706830, PubMed:19569147, PubMed:22137895).
In vitro, can also hydrate acetylenes to aldehydes and ketones via anti-Markovnikov/Markovnikov addition (PubMed:22948824).
6 Publications<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.1"Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein."
Rohdich F., Hecht S., Gaertner K., Adam P., Krieger C., Amslinger S., Arigoni D., Bacher A., Eisenreich W.
Proc. Natl. Acad. Sci. U.S.A. 99:1158-1163(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY. - Ref.7"LytB, a novel gene of the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli."
Altincicek B., Kollas A.-K., Eberl M., Wiesner J., Sanderbrand S., Hintz M., Beck E., Jomaa H.
FEBS Lett. 499:37-40(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE. - Ref.10"Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein."
Wolff M., Seemann M., Tse Sum Bui B., Frapart Y., Tritsch D., Garcia Estrabot A., Rodriguez-Concepcion M., Boronat A., Marquet A., Rohmer M.
FEBS Lett. 541:115-120(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. - Ref.14"Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction."
Graewert T., Rohdich F., Span I., Bacher A., Eisenreich W., Eppinger J., Groll M.
Angew. Chem. Int. Ed. Engl. 48:5756-5759(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S), FUNCTION, COFACTOR, MUTAGENESIS OF HIS-41; HIS-74; VAL-99; HIS-124; GLU-126; THR-167; SER-225 AND ASN-227. - Ref.17"Crystal structures of mutant IspH proteins reveal a rotation of the substrate's hydroxymethyl group during catalysis."
Span I., Graewert T., Bacher A., Eisenreich W., Groll M.
J. Mol. Biol. 416:1-9(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF WILD-TYPE AND MUTANTS CYS-167; ASP-126 AND GLN-126 IN COMPLEXES WITH SUBSTRATE AND IRON-SULFUR (4FE-4S), FUNCTION, COFACTOR, MUTAGENESIS OF GLU-126 AND THR-167, REACTION MECHANISM, ACTIVE SITE. - Ref.18"Discovery of acetylene hydratase activity of the iron-sulphur protein IspH."
Span I., Wang K., Wang W., Zhang Y., Bacher A., Eisenreich W., Li K., Schulz C., Oldfield E., Groll M.
Nat. Commun. 3:1042-1042(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH VARIOUS COMPOUNDS; IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), FUNCTION, ACETYLENE HYDRATASE ACTIVITY.
<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:1.17.7.4
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Manual assertion based on experiment ini
- Ref.9"Biosynthesis of terpenes: studies on 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase."
Adam P., Hecht S., Eisenreich W., Kaiser J., Graewert T., Arigoni D., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 99:12108-12113(2002) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY. - Ref.10"Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein."
Wolff M., Seemann M., Tse Sum Bui B., Frapart Y., Tritsch D., Garcia Estrabot A., Rodriguez-Concepcion M., Boronat A., Marquet A., Rohmer M.
FEBS Lett. 541:115-120(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. - Ref.11"The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: studies on the mechanisms of the reactions catalyzed by IspG and IspH protein."
Rohdich F., Zepeck F., Adam P., Hecht S., Kaiser J., Laupitz R., Graewert T., Amslinger S., Eisenreich W., Bacher A., Arigoni D.
Proc. Natl. Acad. Sci. U.S.A. 100:1586-1591(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY.
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Manual assertion based on experiment ini
- Ref.9"Biosynthesis of terpenes: studies on 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase."
Adam P., Hecht S., Eisenreich W., Kaiser J., Graewert T., Arigoni D., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 99:12108-12113(2002) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY. - Ref.10"Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein."
Wolff M., Seemann M., Tse Sum Bui B., Frapart Y., Tritsch D., Garcia Estrabot A., Rodriguez-Concepcion M., Boronat A., Marquet A., Rohmer M.
FEBS Lett. 541:115-120(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. - Ref.11"The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: studies on the mechanisms of the reactions catalyzed by IspG and IspH protein."
Rohdich F., Zepeck F., Adam P., Hecht S., Kaiser J., Laupitz R., Graewert T., Amslinger S., Eisenreich W., Bacher A., Arigoni D.
Proc. Natl. Acad. Sci. U.S.A. 100:1586-1591(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY.
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H2O- Search proteins in UniProtKB for this molecule.
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+isopentenyl diphosphate- Search proteins in UniProtKB for this molecule.
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- dimethylallyl diphosphateEC:1.17.7.4
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Manual assertion based on experiment ini
- Ref.9"Biosynthesis of terpenes: studies on 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase."
Adam P., Hecht S., Eisenreich W., Kaiser J., Graewert T., Arigoni D., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 99:12108-12113(2002) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY. - Ref.10"Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein."
Wolff M., Seemann M., Tse Sum Bui B., Frapart Y., Tritsch D., Garcia Estrabot A., Rodriguez-Concepcion M., Boronat A., Marquet A., Rohmer M.
FEBS Lett. 541:115-120(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. - Ref.11"The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: studies on the mechanisms of the reactions catalyzed by IspG and IspH protein."
Rohdich F., Zepeck F., Adam P., Hecht S., Kaiser J., Laupitz R., Graewert T., Amslinger S., Eisenreich W., Bacher A., Arigoni D.
Proc. Natl. Acad. Sci. U.S.A. 100:1586-1591(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY.
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Manual assertion based on experiment ini
- Ref.9"Biosynthesis of terpenes: studies on 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase."
Adam P., Hecht S., Eisenreich W., Kaiser J., Graewert T., Arigoni D., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 99:12108-12113(2002) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY. - Ref.10"Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein."
Wolff M., Seemann M., Tse Sum Bui B., Frapart Y., Tritsch D., Garcia Estrabot A., Rodriguez-Concepcion M., Boronat A., Marquet A., Rohmer M.
FEBS Lett. 541:115-120(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. - Ref.11"The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: studies on the mechanisms of the reactions catalyzed by IspG and IspH protein."
Rohdich F., Zepeck F., Adam P., Hecht S., Kaiser J., Laupitz R., Graewert T., Amslinger S., Eisenreich W., Bacher A., Arigoni D.
Proc. Natl. Acad. Sci. U.S.A. 100:1586-1591(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY.
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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
[4Fe-4S] cluster
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Manual assertion based on experiment ini
- Ref.10"Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein."
Wolff M., Seemann M., Tse Sum Bui B., Frapart Y., Tritsch D., Garcia Estrabot A., Rodriguez-Concepcion M., Boronat A., Marquet A., Rohmer M.
FEBS Lett. 541:115-120(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. - Ref.13"Biosynthesis of isoprene units: Moessbauer spectroscopy of substrate and inhibitor binding to the [4Fe-4S] cluster of the LytB/IspH enzyme."
Ahrens-Botzong A., Janthawornpong K., Wolny J.A., Tambou E.N., Rohmer M., Krasutsky S., Poulter C.D., Schuenemann V., Seemann M.
Angew. Chem. Int. Ed. 50:11976-11979(2011) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, COFACTOR. - Ref.15"Probing the reaction mechanism of IspH protein by x-ray structure analysis."
Graewert T., Span I., Eisenreich W., Rohdich F., Eppinger J., Bacher A., Groll M.
Proc. Natl. Acad. Sci. U.S.A. 107:1077-1081(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; PRODUCTS; IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR, MUTAGENESIS OF CYS-12; CYS-96 AND CYS-197. - Ref.16"Are free radicals involved in IspH catalysis? An EPR and crystallographic investigation."
Wang W., Wang K., Span I., Jauch J., Bacher A., Groll M., Oldfield E.
J. Am. Chem. Soc. 134:11225-11234(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-315 IN COMPLEX WITH ISO-HMBPP AND IRON-SULFUR (4FE-4S), COFACTOR, REACTION MECHANISM, ACTIVE SITE. - Ref.17"Crystal structures of mutant IspH proteins reveal a rotation of the substrate's hydroxymethyl group during catalysis."
Span I., Graewert T., Bacher A., Eisenreich W., Groll M.
J. Mol. Biol. 416:1-9(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF WILD-TYPE AND MUTANTS CYS-167; ASP-126 AND GLN-126 IN COMPLEXES WITH SUBSTRATE AND IRON-SULFUR (4FE-4S), FUNCTION, COFACTOR, MUTAGENESIS OF GLU-126 AND THR-167, REACTION MECHANISM, ACTIVE SITE.
Manual assertion based on experiment ini
- Ref.10"Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein."
Wolff M., Seemann M., Tse Sum Bui B., Frapart Y., Tritsch D., Garcia Estrabot A., Rodriguez-Concepcion M., Boronat A., Marquet A., Rohmer M.
FEBS Lett. 541:115-120(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. - Ref.12"IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis."
Graewert T., Kaiser J., Zepeck F., Laupitz R., Hecht S., Amslinger S., Schramek N., Schleicher E., Weber S., Haslbeck M., Buchner J., Rieder C., Arigoni D., Bacher A., Eisenreich W., Rohdich F.
J. Am. Chem. Soc. 126:12847-12855(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PRESENCE OF A 3FE-4S IRON-SULFUR CLUSTER, ACTIVITY REGULATION, KINETIC PARAMETERS, MUTAGENESIS OF CYS-12; CYS-96 AND CYS-197. - Ref.14"Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction."
Graewert T., Rohdich F., Span I., Bacher A., Eisenreich W., Eppinger J., Groll M.
Angew. Chem. Int. Ed. Engl. 48:5756-5759(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S), FUNCTION, COFACTOR, MUTAGENESIS OF HIS-41; HIS-74; VAL-99; HIS-124; GLU-126; THR-167; SER-225 AND ASN-227. - Ref.15"Probing the reaction mechanism of IspH protein by x-ray structure analysis."
Graewert T., Span I., Eisenreich W., Rohdich F., Eppinger J., Bacher A., Groll M.
Proc. Natl. Acad. Sci. U.S.A. 107:1077-1081(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE; PRODUCTS; IRON-SULFUR (3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR, MUTAGENESIS OF CYS-12; CYS-96 AND CYS-197. - Ref.16"Are free radicals involved in IspH catalysis? An EPR and crystallographic investigation."
Wang W., Wang K., Span I., Jauch J., Bacher A., Groll M., Oldfield E.
J. Am. Chem. Soc. 134:11225-11234(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-315 IN COMPLEX WITH ISO-HMBPP AND IRON-SULFUR (4FE-4S), COFACTOR, REACTION MECHANISM, ACTIVE SITE. - Ref.17"Crystal structures of mutant IspH proteins reveal a rotation of the substrate's hydroxymethyl group during catalysis."
Span I., Graewert T., Bacher A., Eisenreich W., Groll M.
J. Mol. Biol. 416:1-9(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF WILD-TYPE AND MUTANTS CYS-167; ASP-126 AND GLN-126 IN COMPLEXES WITH SUBSTRATE AND IRON-SULFUR (4FE-4S), FUNCTION, COFACTOR, MUTAGENESIS OF GLU-126 AND THR-167, REACTION MECHANISM, 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
Addition of Ca2+, Mg2+, Mn2+, Ni2+, Co2+ or Fe2+ decreases the catalytic activity (PubMed:15469281). Addition of Zn2+ results in complete loss of activity (PubMed:15469281). Is potently inhibited by substrate analogs in which the hydroxy group in HMBPP is replaced by an amino or thiol group (PubMed:22012762).2 Publications
Manual assertion based on experiment ini
- Ref.12"IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis."
Graewert T., Kaiser J., Zepeck F., Laupitz R., Hecht S., Amslinger S., Schramek N., Schleicher E., Weber S., Haslbeck M., Buchner J., Rieder C., Arigoni D., Bacher A., Eisenreich W., Rohdich F.
J. Am. Chem. Soc. 126:12847-12855(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PRESENCE OF A 3FE-4S IRON-SULFUR CLUSTER, ACTIVITY REGULATION, KINETIC PARAMETERS, MUTAGENESIS OF CYS-12; CYS-96 AND CYS-197. - Ref.13"Biosynthesis of isoprene units: Moessbauer spectroscopy of substrate and inhibitor binding to the [4Fe-4S] cluster of the LytB/IspH enzyme."
Ahrens-Botzong A., Janthawornpong K., Wolny J.A., Tambou E.N., Rohmer M., Krasutsky S., Poulter C.D., Schuenemann V., Seemann M.
Angew. Chem. Int. Ed. 50:11976-11979(2011) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, COFACTOR.
<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=30 µM for 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate1 Publication
Manual assertion based on experiment ini
- Ref.12"IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis."
Graewert T., Kaiser J., Zepeck F., Laupitz R., Hecht S., Amslinger S., Schramek N., Schleicher E., Weber S., Haslbeck M., Buchner J., Rieder C., Arigoni D., Bacher A., Eisenreich W., Rohdich F.
J. Am. Chem. Soc. 126:12847-12855(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PRESENCE OF A 3FE-4S IRON-SULFUR CLUSTER, ACTIVITY REGULATION, KINETIC PARAMETERS, MUTAGENESIS OF CYS-12; CYS-96 AND CYS-197.
pH dependencei
Optimum pH is 7.0.
<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: dimethylallyl diphosphate biosynthesis
This protein is involved in step 1 of the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate.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.7"LytB, a novel gene of the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli."
Altincicek B., Kollas A.-K., Eberl M., Wiesner J., Sanderbrand S., Hintz M., Beck E., Jomaa H.
FEBS Lett. 499:37-40(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE.
Manual assertion based on experiment ini
- Ref.1"Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein."
Rohdich F., Hecht S., Gaertner K., Adam P., Krieger C., Amslinger S., Arigoni D., Bacher A., Eisenreich W.
Proc. Natl. Acad. Sci. U.S.A. 99:1158-1163(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate, the pathway dimethylallyl diphosphate biosynthesis and in Isoprenoid biosynthesis.
Pathwayi: isopentenyl diphosphate biosynthesis via DXP pathway
This protein is involved in step 6 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.1 PublicationManual assertion inferred by curator fromi
- Ref.7"LytB, a novel gene of the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli."
Altincicek B., Kollas A.-K., Eberl M., Wiesner J., Sanderbrand S., Hintz M., Beck E., Jomaa H.
FEBS Lett. 499:37-40(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE.
Manual assertion based on experiment ini
- Ref.1"Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein."
Rohdich F., Hecht S., Gaertner K., Adam P., Krieger C., Amslinger S., Arigoni D., Bacher A., Eisenreich W.
Proc. Natl. Acad. Sci. U.S.A. 99:1158-1163(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.
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 | 12 | Iron-sulfur (4Fe-4S)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 5 PublicationsManual 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 | 41 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 | |
| Binding sitei | 74 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 96 | Iron-sulfur (4Fe-4S)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 124 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion inferred by curator fromi
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 | 126 | Proton donor2 Publications Manual assertion inferred by curator fromi
| 1 | |
| Binding sitei | 167 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 | |
| Metal bindingi | 197 | Iron-sulfur (4Fe-4S)Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 269 | SubstrateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion inferred by curator fromi
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
- 3 iron, 4 sulfur cluster binding Source: EcoCyc
<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.14"Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction."
Graewert T., Rohdich F., Span I., Bacher A., Eisenreich W., Eppinger J., Groll M.
Angew. Chem. Int. Ed. Engl. 48:5756-5759(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S), FUNCTION, COFACTOR, MUTAGENESIS OF HIS-41; HIS-74; VAL-99; HIS-124; GLU-126; THR-167; SER-225 AND ASN-227.
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity Source: UniProtKB-UniRule
- 4 iron, 4 sulfur cluster binding Source: UniProtKB-UniRule
- hydroxymethylbutenyl pyrophosphate reductase activity Source: EcoCycInferred from direct assayi
- Ref.11"The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: studies on the mechanisms of the reactions catalyzed by IspG and IspH protein."
Rohdich F., Zepeck F., Adam P., Hecht S., Kaiser J., Laupitz R., Graewert T., Amslinger S., Eisenreich W., Bacher A., Arigoni D.
Proc. Natl. Acad. Sci. U.S.A. 100:1586-1591(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY.
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- dimethylallyl diphosphate biosynthetic process Source: UniProtKB-UniRule
- isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway 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-go-evidence-codes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.7"LytB, a novel gene of the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli."
Altincicek B., Kollas A.-K., Eberl M., Wiesner J., Sanderbrand S., Hintz M., Beck E., Jomaa H.
FEBS Lett. 499:37-40(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE.
- terpenoid biosynthetic process Source: UniProtKB-UniRule
<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 |
| Biological process | Isoprene biosynthesis |
| Ligand | 4Fe-4S, Iron, Iron-sulfur, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG11081-MONOMER |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00056;UER00097 UPA00059;UER00105 |
<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: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase1 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: HMBPP reductase1 Publication Manual assertion based on opinion ini
Alternative name(s): 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase1 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:ispH1 Publication Manual assertion based on opinion ini
Synonyms:lytB, yaaE Ordered Locus Names:b0029, JW0027 |
| <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 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
Cytosol
- cytosol Source: EcoCycInferred from direct assayi
- "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth."
Lopez-Campistrous A., Semchuk P., Burke L., Palmer-Stone T., Brokx S.J., Broderick G., Bottorff D., Bolch S., Weiner J.H., Ellison M.J.
Mol. Cell. Proteomics 4:1205-1209(2005) [PubMed] [Europe PMC] [Abstract] - "Protein abundance profiling of the Escherichia coli cytosol."
Ishihama Y., Schmidt T., Rappsilber J., Mann M., Hartl F.U., Kerner M.J., Frishman D.
BMC Genomics 9:102-102(2008) [PubMed] [Europe PMC] [Abstract]
- cytosol Source: EcoCycInferred from direct assayi
<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
Cells lacking this gene are viable only if the medium is supplemented with mevalonate or the cells are complemented with an episomal copy of ispH (PubMed:11418107). A conditional E.coli lytB mutant shows that LytB is essential for survival and that depletion of LytB results in cell lysis (PubMed:11717301).2 Publications
Manual assertion based on experiment ini
- Ref.7"LytB, a novel gene of the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli."
Altincicek B., Kollas A.-K., Eberl M., Wiesner J., Sanderbrand S., Hintz M., Beck E., Jomaa H.
FEBS Lett. 499:37-40(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE. - Ref.8"The lytB gene of Escherichia coli is essential and specifies a product needed for isoprenoid biosynthesis."
McAteer S., Coulson A., McLennan N., Masters M.
J. Bacteriol. 183:7403-7407(2001) [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 | 12 | C → S: Loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 41 | H → N: No effect on catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 74 | H → N: Reduces catalytic activity 2-fold. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 96 | C → S: Loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 99 | V → A: No effect on catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 124 | H → N: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 126 | E → D or Q: Loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 167 | T → C: Reduces catalytic activity 3-fold. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 167 | T → S: No effect on catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 197 | C → S: Loss of catalytic activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 225 | S → C: Loss of catalytic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 227 | N → Q: Reduces catalytic activity 20-fold. 1 Publication Manual assertion based on experiment ini
| 1 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB01785, Dimethylallyl Diphosphate DB04714, ISOPENTENYL PYROPHOSPHATE |
<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_0000128812 | 1 – 316 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductaseAdd BLAST | 316 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P62623 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P62623 |
PRoteomics IDEntifications database More...PRIDEi | P62623 |
<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.
1 PublicationManual assertion based on experiment ini
- Ref.10"Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein."
Wolff M., Seemann M., Tse Sum Bui B., Frapart Y., Tritsch D., Garcia Estrabot A., Rodriguez-Concepcion M., Boronat A., Marquet A., Rohmer M.
FEBS Lett. 541:115-120(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4262917, 331 interactors 849179, 2 interactors |
Database of interacting proteins More...DIPi | DIP-35808N |
Protein interaction database and analysis system More...IntActi | P62623, 7 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b0029 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P62623 |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| 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 – 5 | 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 | 4 | |
| <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 | 13 – 29 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 | |
| Beta strandi | 33 – 37 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 39 – 41 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 43 – 51 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 54 – 59 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 60 – 62 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 68 – 71 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 78 – 86 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 90 – 93 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 97 – 112 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 16 | |
| Beta strandi | 115 – 120 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 125 – 131 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 137 – 139 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 141 – 144 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 147 – 152 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 160 – 165 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 167 – 169 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 171 – 184 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
| Beta strandi | 191 – 193 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 198 – 213 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 16 | |
| Beta strandi | 215 – 220 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 226 – 237 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Beta strandi | 241 – 247 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 248 – 250 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 253 – 255 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| <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 | 256 – 258 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 260 – 266 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 272 – 284 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 289 – 292 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 300 – 302 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 306 – 308 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
AlphaFold Protein Structure Database More...AlphaFoldDBi | P62623 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P62623 |
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 | P62623 |
<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 | 225 – 227 | Substrate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion inferred by curator fromi
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
Belongs to the IspH family.UniRule 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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG0761, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_027486_1_0_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P62623 |
Identification of Orthologs from Complete Genome Data More...OMAi | HNKYVVD |
Database for complete collections of gene phylogenies More...PhylomeDBi | P62623 |
Family and domain databases
Conserved Domains Database More...CDDi | cd13944, lytB_ispH, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00191, IspH, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR003451, LytB/IspH |
The PANTHER Classification System More...PANTHERi | PTHR30426, PTHR30426, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF02401, LYTB, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00216, ispH_lytB, 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.
P62623-1 [UniParc]FASTAAdd to basketAdded to basket
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MQILLANPRG FCAGVDRAIS IVENALAIYG APIYVRHEVV HNRYVVDSLR
60 70 80 90 100
ERGAIFIEQI SEVPDGAILI FSAHGVSQAV RNEAKSRDLT VFDATCPLVT
110 120 130 140 150
KVHMEVARAS RRGEESILIG HAGHPEVEGT MGQYSNPEGG MYLVESPDDV
160 170 180 190 200
WKLTVKNEEK LSFMTQTTLS VDDTSDVIDA LRKRFPKIVG PRKDDICYAT
210 220 230 240 250
TNRQEAVRAL AEQAEVVLVV GSKNSSNSNR LAELAQRMGK RAFLIDDAKD
260 270 280 290 300
IQEEWVKEVK CVGVTAGASA PDILVQNVVA RLQQLGGGEA IPLEGREENI
310
VFEVPKELRV DIREVD
Length:316
Mass (Da):34,775
Last modified:July 19, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i0E7B378BD49AB771
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 | AY062212 Genomic DNA Translation: AAL38655.1 X54945 Genomic DNA Translation: CAA38707.1 U00096 Genomic DNA Translation: AAC73140.1 AP009048 Genomic DNA Translation: BAB96598.1 |
Protein sequence database of the Protein Information Resource More...PIRi | JE0403 |
NCBI Reference Sequences More...RefSeqi | NP_414570.1, NC_000913.3 WP_001166395.1, NZ_SSZK01000004.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC73140; AAC73140; b0029 BAB96598; BAB96598; BAB96598 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 58460832 944777 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW0027 eco:b0029 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.2256 |
<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 | |
|---|---|---|---|---|---|---|
| P62623 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | UniRef100_A7ZHB8 | |||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | |||||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | |||||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | |||||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | |||||
| +116 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P62623 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | UniRef90_A7MIM0 | |||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | |||||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | |||||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | |||||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | |||||
| +150 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P62623 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | UniRef50_Q6D0C6 | |||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 316 | |||||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 317 | |||||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 317 | |||||
| 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | 317 | |||||
| +3927 | ||||||
<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 | AY062212 Genomic DNA Translation: AAL38655.1 X54945 Genomic DNA Translation: CAA38707.1 U00096 Genomic DNA Translation: AAC73140.1 AP009048 Genomic DNA Translation: BAB96598.1 |
| PIRi | JE0403 |
| RefSeqi | NP_414570.1, NC_000913.3 WP_001166395.1, NZ_SSZK01000004.1 |
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 |
| 3F7T | X-ray | 1.80 | A/B | 1-316 | [»] | |
| 3KE8 | X-ray | 1.70 | A/B | 1-316 | [»] | |
| 3KE9 | X-ray | 1.90 | A/B | 1-316 | [»] | |
| 3KEF | X-ray | 1.70 | A/B | 1-316 | [»] | |
| 3KEL | X-ray | 1.80 | A/B | 1-316 | [»] | |
| 3KEM | X-ray | 2.00 | A/B | 1-316 | [»] | |
| 3SZL | X-ray | 1.60 | A/B | 1-316 | [»] | |
| 3SZO | X-ray | 1.60 | A/B | 1-316 | [»] | |
| 3SZU | X-ray | 1.40 | A/B | 1-316 | [»] | |
| 3T0F | X-ray | 1.90 | A/B | 1-316 | [»] | |
| 3T0G | X-ray | 2.10 | A/B | 1-316 | [»] | |
| 3URK | X-ray | 1.50 | A/B | 1-316 | [»] | |
| 3UTC | X-ray | 1.90 | A/B | 1-316 | [»] | |
| 3UTD | X-ray | 1.70 | A/B | 1-316 | [»] | |
| 3UV3 | X-ray | 1.60 | A/B | 1-316 | [»] | |
| 3UV6 | X-ray | 1.70 | A/B | 1-316 | [»] | |
| 3UV7 | X-ray | 1.60 | A/B | 1-316 | [»] | |
| 3UWM | X-ray | 1.80 | A/B | 1-316 | [»] | |
| 3ZGL | X-ray | 1.68 | A/B | 1-316 | [»] | |
| 3ZGN | X-ray | 1.95 | A/B | 1-316 | [»] | |
| 4EB3 | X-ray | 1.90 | A/B | 1-315 | [»] | |
| 4H4C | X-ray | 1.80 | A/B | 1-315 | [»] | |
| 4H4D | X-ray | 1.35 | A/B | 1-315 | [»] | |
| 4H4E | X-ray | 1.70 | A/B | 1-315 | [»] | |
| AlphaFoldDBi | P62623 | |||||
| SMRi | P62623 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 4262917, 331 interactors 849179, 2 interactors |
| DIPi | DIP-35808N |
| IntActi | P62623, 7 interactors |
| STRINGi | 511145.b0029 |
Chemistry databases
| BindingDBi | P62623 |
| DrugBanki | DB01785, Dimethylallyl Diphosphate DB04714, ISOPENTENYL PYROPHOSPHATE |
Proteomic databases
| jPOSTi | P62623 |
| PaxDbi | P62623 |
| PRIDEi | P62623 |
Genome annotation databases
| EnsemblBacteriai | AAC73140; AAC73140; b0029 BAB96598; BAB96598; BAB96598 |
| GeneIDi | 58460832 944777 |
| KEGGi | ecj:JW0027 eco:b0029 |
| PATRICi | fig|1411691.4.peg.2256 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1073 |
Phylogenomic databases
| eggNOGi | COG0761, Bacteria |
| HOGENOMi | CLU_027486_1_0_6 |
| InParanoidi | P62623 |
| OMAi | HNKYVVD |
| PhylomeDBi | P62623 |
Enzyme and pathway databases
| UniPathwayi | UPA00056;UER00097 UPA00059;UER00105 |
| BioCyci | EcoCyc:EG11081-MONOMER |
Miscellaneous databases
| EvolutionaryTracei | P62623 |
Protein Ontology More...PROi | PR:P62623 |
Family and domain databases
| CDDi | cd13944, lytB_ispH, 1 hit |
| HAMAPi | MF_00191, IspH, 1 hit |
| InterProi | View protein in InterPro IPR003451, LytB/IspH |
| PANTHERi | PTHR30426, PTHR30426, 1 hit |
| Pfami | View protein in Pfam PF02401, LYTB, 1 hit |
| TIGRFAMsi | TIGR00216, ispH_lytB, 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 | ISPH_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 | P62623Primary (citable) accession number: P62623 Secondary accession number(s): P22565 | |
| <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: | July 19, 2004 |
| Last sequence update: | July 19, 2004 | |
| Last modified: | May 25, 2022 | |
| This is version 141 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
