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UniProtKB - P62617 (ISPF_ECOLI)
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>sp|P62617|ISPF_ECOLI 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase OS=Escherichia coli (strain K12) OX=83333 GN=ispF PE=1 SV=1 MRIGHGFDVHAFGGEGPIIIGGVRIPYEKGLLAHSDGDVALHALTDALLGAAALGDIGKL FPDTDPAFKGADSRELLREAWRRIQAKGYTLGNVDVTIIAQAPKMLPHIPQMRVFIAEDL GCHMDDVNVKATTTEKLGFTGRGEGIACEAVALLIKATKCommunity curation ()Add a publicationFeedback
Protein
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Gene
ispF
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
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). Also converts 4-diphosphocytidyl-2-C-methyl-D-erythritol into 2-C-methyl-D-erythritol 3,4-cyclophosphate and CMP.
2 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.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.8"2C-Methyl-d-erythritol 4-phosphate enhances and sustains cyclodiphosphate synthase IspF activity."
Bitok J.K., Meyers C.F.
ACS Chem. Biol. 7:1702-1710(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
<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
- 4-CDP-2-C-methyl-D-erythritol 2-phosphateEC:4.6.1.12
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- See the description of this molecule in ChEBI.
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- Search proteins in UniProtKB for this molecule.
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<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
2 PublicationsManual assertion based on experiment ini
- Ref.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.8"2C-Methyl-d-erythritol 4-phosphate enhances and sustains cyclodiphosphate synthase IspF activity."
Bitok J.K., Meyers C.F.
ACS Chem. Biol. 7:1702-1710(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
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Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.8"2C-Methyl-d-erythritol 4-phosphate enhances and sustains cyclodiphosphate synthase IspF activity."
Bitok J.K., Meyers C.F.
ACS Chem. Biol. 7:1702-1710(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
Source: Rhea- Search for this reaction in UniProtKB.
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4-CDP-2-C-methyl-D-erythritol 2-phosphate- Search proteins in UniProtKB for this molecule.
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=2-C-methyl-D-erythritol 2,4-cyclic diphosphate- Search proteins in UniProtKB for this molecule.
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+CMP- Search proteins in UniProtKB for this molecule.
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- 4-CDP-2-C-methyl-D-erythritol
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- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- 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.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
4-CDP-2-C-methyl-D-erythritol- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
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=2-C-methyl-D-erythritol 3,4-cyclophosphate- Search proteins in UniProtKB for this molecule.
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+CMP- Search proteins in UniProtKB for this molecule.
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+H+- 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
a divalent metal cation
- 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 according to rulesi
8 PublicationsManual assertion based on experiment ini
- Ref.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.9"Structure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic pathway."
Richard S.B., Ferrer J.-L., Bowman M.E., Lillo A.M., Tetzlaff C.N., Cane D.E., Noel J.P.
J. Biol. Chem. 277:8667-8672(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, COFACTOR, SUBUNIT. - Ref.10"Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids."
Steinbacher S., Kaiser J., Wungsintaweekul J., Hecht S., Eisenreich W., Gerhardt S., Bacher A., Rohdich F.
J. Mol. Biol. 316:79-88(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ASP-8; HIS-42 AND ASP-56, COFACTOR, SUBUNIT. - Ref.11"Structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase: an essential enzyme for isoprenoid biosynthesis and target for antimicrobial drug development."
Kemp L.E., Bond C.S., Hunter W.N.
Proc. Natl. Acad. Sci. U.S.A. 99:6591-6596(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, COFACTOR, SUBUNIT. - Ref.12"The identification of isoprenoids that bind in the intersubunit cavity of Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase by complementary biophysical methods."
Kemp L.E., Alphey M.S., Bond C.S., Ferguson M.A., Hecht S., Bacher A., Eisenreich W., Rohdich F., Hunter W.N.
Acta Crystallogr. D 61:45-52(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, COFACTOR, SUBUNIT. - Ref.13"A double mutation of Escherichia coli2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate."
Sgraja T., Kemp L.E., Ramsden N., Hunter W.N.
Acta Crystallogr. F 61:625-629(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF DOUBLE MUTANT MET-142/LEU-144 IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ARG-142 AND GLU-144, COFACTOR. - Ref.14"Fluorescent inhibitors for IspF, an enzyme in the non-mevalonate pathway for isoprenoid biosynthesis and a potential target for antimalarial therapy."
Crane C.M., Kaiser J., Ramsden N.L., Lauw S., Rohdich F., Eisenreich W., Hunter W.N., Bacher A., Diederich F.
Angew. Chem. Int. Ed. 45:1069-1074(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND ZINC IONS, COFACTOR, SUBUNIT. - Ref.15"A structure-based approach to ligand discovery for 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase: a target for antimicrobial therapy."
Ramsden N.L., Buetow L., Dawson A., Kemp L.A., Ulaganathan V., Brenk R., Klebe G., Hunter W.N.
J. Med. Chem. 52:2531-2542(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND ZINC IONS, COFACTOR, SUBUNIT.
Manual assertion according to rulesi
8 PublicationsManual assertion based on experiment ini
- Ref.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR. - Ref.9"Structure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic pathway."
Richard S.B., Ferrer J.-L., Bowman M.E., Lillo A.M., Tetzlaff C.N., Cane D.E., Noel J.P.
J. Biol. Chem. 277:8667-8672(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, COFACTOR, SUBUNIT. - Ref.10"Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids."
Steinbacher S., Kaiser J., Wungsintaweekul J., Hecht S., Eisenreich W., Gerhardt S., Bacher A., Rohdich F.
J. Mol. Biol. 316:79-88(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ASP-8; HIS-42 AND ASP-56, COFACTOR, SUBUNIT. - Ref.11"Structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase: an essential enzyme for isoprenoid biosynthesis and target for antimicrobial drug development."
Kemp L.E., Bond C.S., Hunter W.N.
Proc. Natl. Acad. Sci. U.S.A. 99:6591-6596(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, COFACTOR, SUBUNIT. - Ref.12"The identification of isoprenoids that bind in the intersubunit cavity of Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase by complementary biophysical methods."
Kemp L.E., Alphey M.S., Bond C.S., Ferguson M.A., Hecht S., Bacher A., Eisenreich W., Rohdich F., Hunter W.N.
Acta Crystallogr. D 61:45-52(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, COFACTOR, SUBUNIT. - Ref.13"A double mutation of Escherichia coli2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate."
Sgraja T., Kemp L.E., Ramsden N., Hunter W.N.
Acta Crystallogr. F 61:625-629(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF DOUBLE MUTANT MET-142/LEU-144 IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ARG-142 AND GLU-144, COFACTOR. - Ref.14"Fluorescent inhibitors for IspF, an enzyme in the non-mevalonate pathway for isoprenoid biosynthesis and a potential target for antimalarial therapy."
Crane C.M., Kaiser J., Ramsden N.L., Lauw S., Rohdich F., Eisenreich W., Hunter W.N., Bacher A., Diederich F.
Angew. Chem. Int. Ed. 45:1069-1074(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND ZINC IONS, COFACTOR, SUBUNIT. - Ref.15"A structure-based approach to ligand discovery for 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase: a target for antimicrobial therapy."
Ramsden N.L., Buetow L., Dawson A., Kemp L.A., Ulaganathan V., Brenk R., Klebe G., Hunter W.N.
J. Med. Chem. 52:2531-2542(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND ZINC IONS, COFACTOR, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Activated by 2C-methyl-D-erythritol 4-phosphate (MEP).1 Publication
Manual assertion based on experiment ini
- Ref.8"2C-Methyl-d-erythritol 4-phosphate enhances and sustains cyclodiphosphate synthase IspF activity."
Bitok J.K., Meyers C.F.
ACS Chem. Biol. 7:1702-1710(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
<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
kcat is 61 min(-1) for CDP-ME2P (at pH 7.4).
- KM=339 µM for CDP-ME2P (at pH 7.4)1 Publication
Manual assertion based on experiment ini
- Ref.8"2C-Methyl-d-erythritol 4-phosphate enhances and sustains cyclodiphosphate synthase IspF activity."
Bitok J.K., Meyers C.F.
ACS Chem. Biol. 7:1702-1710(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
<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: isopentenyl diphosphate biosynthesis via DXP pathway
This protein is involved in step 4 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.UniRule annotationManual assertion according to rulesi
This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.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 | 8 | Divalent metal cationCombined 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 7 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 10 | Divalent metal cation; via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 7 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 34 | Transition state stabilizerUniRule annotation Manual assertion according to rulesi 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
| 1 | |
| Metal bindingi | 42 | Divalent metal cation; via pros nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 7 PublicationsManual assertion based on experiment ini
| 1 | |
| Sitei | 133 | Transition state stabilizerUniRule annotation Manual assertion according to rulesi 1 PublicationManual assertion inferred by curator fromi
| 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 | 139 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate; via amide nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Binding sitei | 142 | 4-CDP-2-C-methyl-D-erythritol 2-phosphateCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi | 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
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity 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.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR.
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.10"Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids."
Steinbacher S., Kaiser J., Wungsintaweekul J., Hecht S., Eisenreich W., Gerhardt S., Bacher A., Rohdich F.
J. Mol. Biol. 316:79-88(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ASP-8; HIS-42 AND ASP-56, COFACTOR, SUBUNIT.
- manganese ion binding Source: EcoCycInferred from direct assayi
- Ref.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR.
- metal ion binding Source: EcoCycInferred from direct assayi
- Ref.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR.
- zinc ion binding Source: EcoCycInferred from direct assayi
- Ref.10"Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids."
Steinbacher S., Kaiser J., Wungsintaweekul J., Hecht S., Eisenreich W., Gerhardt S., Bacher A., Rohdich F.
J. Mol. Biol. 316:79-88(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ASP-8; HIS-42 AND ASP-56, COFACTOR, SUBUNIT.
GO - Biological processi
- isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway Source: UniProtKB-UniPathway
- terpenoid biosynthetic process Source: UniProtKB-UniRule
- ubiquinone biosynthetic process Source: EcoCycInferred from direct assayi
- Ref.2"Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate to 2C-methyl-D-erythritol 2,4-cyclodiphosphate."
Herz S., Wungsintaweekul J., Schuhr C.A., Hecht S., Luettgen H., Sagner S., Fellermeier M., Eisenreich W., Zenk M.H., Bacher A., Rohdich F.
Proc. Natl. Acad. Sci. U.S.A. 97:2486-2490(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS AN MECDP-SYNTHASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR.
<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 | Lyase |
| Biological process | Isoprene biosynthesis |
| Ligand | Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG11816-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 4.6.1.12, 2026 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P62617 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00056;UER00095 |
<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: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthaseUniRule annotationManual assertion according to rulesi (EC:4.6.1.12
Manual assertion according to rulesi 2 PublicationsManual assertion based on experiment ini
Short name: MECDP-synthaseUniRule annotation Manual assertion according to rulesi Short name: MECPP-synthaseUniRule annotation Manual assertion according to rulesi Short name: MECPSUniRule annotation Manual assertion according to rulesi |
| <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:ispFUniRule annotation Manual assertion according to rulesi Synonyms:mecS, ygbB Ordered Locus Names:b2746, JW2716 |
| <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
Cells lacking this gene reveal a filamentous phenotype.1 Publication
Manual assertion based on experiment ini
- Ref.7"Characterization of the depletion of 2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase in Escherichia coli and Bacillus subtilis."
Campbell T.L., Brown E.D.
J. Bacteriol. 184:5609-5618(2002) [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 | 8 | D → S: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 42 | H → S: Loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 56 | D → S: 35% decrease of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 142 | R → M: Little effect on the overall structure; when associated with L-144. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 144 | E → L: Little effect on the overall structure; when associated with M-142. 1 Publication Manual assertion based on experiment ini
| 1 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3217375 |
Drug and drug target database More...DrugBanki | DB02552, Geranyl Diphosphate |
<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_0000189464 | 1 – 159 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthaseAdd BLAST | 159 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P62617 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P62617 |
PRoteomics IDEntifications database More...PRIDEi | P62617 |
<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
Homotrimer.
UniRule annotationManual assertion according to rulesi
7 PublicationsManual assertion based on experiment ini
- Ref.9"Structure and mechanism of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase. An enzyme in the mevalonate-independent isoprenoid biosynthetic pathway."
Richard S.B., Ferrer J.-L., Bowman M.E., Lillo A.M., Tetzlaff C.N., Cane D.E., Noel J.P.
J. Biol. Chem. 277:8667-8672(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, COFACTOR, SUBUNIT. - Ref.10"Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids."
Steinbacher S., Kaiser J., Wungsintaweekul J., Hecht S., Eisenreich W., Gerhardt S., Bacher A., Rohdich F.
J. Mol. Biol. 316:79-88(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ASP-8; HIS-42 AND ASP-56, COFACTOR, SUBUNIT. - Ref.11"Structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase: an essential enzyme for isoprenoid biosynthesis and target for antimicrobial drug development."
Kemp L.E., Bond C.S., Hunter W.N.
Proc. Natl. Acad. Sci. U.S.A. 99:6591-6596(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, COFACTOR, SUBUNIT. - Ref.12"The identification of isoprenoids that bind in the intersubunit cavity of Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase by complementary biophysical methods."
Kemp L.E., Alphey M.S., Bond C.S., Ferguson M.A., Hecht S., Bacher A., Eisenreich W., Rohdich F., Hunter W.N.
Acta Crystallogr. D 61:45-52(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, COFACTOR, SUBUNIT. - Ref.13"A double mutation of Escherichia coli2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate."
Sgraja T., Kemp L.E., Ramsden N., Hunter W.N.
Acta Crystallogr. F 61:625-629(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF DOUBLE MUTANT MET-142/LEU-144 IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ARG-142 AND GLU-144, COFACTOR. - Ref.14"Fluorescent inhibitors for IspF, an enzyme in the non-mevalonate pathway for isoprenoid biosynthesis and a potential target for antimalarial therapy."
Crane C.M., Kaiser J., Ramsden N.L., Lauw S., Rohdich F., Eisenreich W., Hunter W.N., Bacher A., Diederich F.
Angew. Chem. Int. Ed. 45:1069-1074(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND ZINC IONS, COFACTOR, SUBUNIT. - Ref.15"A structure-based approach to ligand discovery for 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase: a target for antimicrobial therapy."
Ramsden N.L., Buetow L., Dawson A., Kemp L.A., Ulaganathan V., Brenk R., Klebe G., Hunter W.N.
J. Med. Chem. 52:2531-2542(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND ZINC IONS, COFACTOR, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
P62617
| With | #Exp. | IntAct |
|---|---|---|
| hldD [P67910] | 2 | EBI-562321,EBI-543760 |
GO - Molecular functioni
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.10"Structure of 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase involved in mevalonate-independent biosynthesis of isoprenoids."
Steinbacher S., Kaiser J., Wungsintaweekul J., Hecht S., Eisenreich W., Gerhardt S., Bacher A., Rohdich F.
J. Mol. Biol. 316:79-88(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND DIVALENT CATIONS, MUTAGENESIS OF ASP-8; HIS-42 AND ASP-56, COFACTOR, SUBUNIT.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4262279, 277 interactors |
Database of interacting proteins More...DIPi | DIP-48029N |
Protein interaction database and analysis system More...IntActi | P62617, 7 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b2746 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P62617 |
<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 | 1 – 16 | 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 | 16 | |
| Beta strandi | 18 – 20 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 23 – 25 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 28 – 31 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 33 – 35 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 39 – 51 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 57 – 60 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 63 – 65 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 66 – 68 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 69 – 71 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 73 – 86 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
| Beta strandi | 90 – 99 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 101 – 103 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 106 – 108 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 109 – 119 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 124 – 126 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 127 – 132 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 138 – 141 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 144 – 155 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P62617 |
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 | P62617 |
<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 | 8 – 10 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
Manual assertion inferred from database entriesi | 3 | |
| Regioni | 34 – 35 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 2 | |
| Regioni | 56 – 58 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 6 PublicationsManual assertion based on experiment ini
Manual assertion inferred from database entriesi | 3 | |
| Regioni | 61 – 65 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
Manual assertion inferred from database entriesi | 5 | |
| Regioni | 100 – 106 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| 7 | |
| Regioni | 132 – 135 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 4 |
<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 | COG0245, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_084630_2_0_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P62617 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P62617 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00554, MECDP_synthase, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.30.1330.50, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_00107, IspF, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR003526, MECDP_synthase IPR020555, MECDP_synthase_CS IPR036571, MECDP_synthase_sf |
The PANTHER Classification System More...PANTHERi | PTHR43181, PTHR43181, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF02542, YgbB, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF69765, SSF69765, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00151, ispF, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01350, ISPF, 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.
P62617-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MRIGHGFDVH AFGGEGPIII GGVRIPYEKG LLAHSDGDVA LHALTDALLG
60 70 80 90 100
AAALGDIGKL FPDTDPAFKG ADSRELLREA WRRIQAKGYT LGNVDVTIIA
110 120 130 140 150
QAPKMLPHIP QMRVFIAEDL GCHMDDVNVK ATTTEKLGFT GRGEGIACEA
VALLIKATK
Length:159
Mass (Da):16,898
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:i9FC5563623A62939
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 | L07942 Genomic DNA Translation: AAA79837.1 AF230738 Genomic DNA Translation: AAF44656.1 AB038256 Genomic DNA Translation: BAA95145.1 U29579 Genomic DNA Translation: AAA69256.1 U00096 Genomic DNA Translation: AAC75788.1 AP009048 Genomic DNA Translation: BAE76823.1 |
Protein sequence database of the Protein Information Resource More...PIRi | I55083 |
NCBI Reference Sequences More...RefSeqi | NP_417226.1, NC_000913.3 WP_001219242.1, NZ_SSUR01000024.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC75788; AAC75788; b2746 BAE76823; BAE76823; BAE76823 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 67413962 945057 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW2716 eco:b2746 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3994 |
<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
<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 | L07942 Genomic DNA Translation: AAA79837.1 AF230738 Genomic DNA Translation: AAF44656.1 AB038256 Genomic DNA Translation: BAA95145.1 U29579 Genomic DNA Translation: AAA69256.1 U00096 Genomic DNA Translation: AAC75788.1 AP009048 Genomic DNA Translation: BAE76823.1 |
| PIRi | I55083 |
| RefSeqi | NP_417226.1, NC_000913.3 WP_001219242.1, NZ_SSUR01000024.1 |
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 |
| 1GX1 | X-ray | 1.80 | A/B/C | 1-159 | [»] | |
| 1H47 | X-ray | 2.00 | A/B/C/D/E/F | 1-159 | [»] | |
| 1H48 | X-ray | 2.30 | A/B/C/D/E/F | 1-159 | [»] | |
| 1JY8 | X-ray | 2.50 | A | 1-159 | [»] | |
| 1KNJ | X-ray | 2.80 | A | 1-159 | [»] | |
| 1KNK | X-ray | 2.80 | A | 1-159 | [»] | |
| 1U3L | X-ray | 2.50 | A | 1-159 | [»] | |
| 1U3P | X-ray | 2.85 | A | 1-159 | [»] | |
| 1U40 | X-ray | 2.80 | A | 1-159 | [»] | |
| 1U43 | X-ray | 3.20 | A | 1-159 | [»] | |
| 1YQN | X-ray | 3.11 | A | 1-159 | [»] | |
| 2AMT | X-ray | 2.30 | A/B/C/D/E/F | 1-159 | [»] | |
| 2GZL | X-ray | 2.50 | A | 1-157 | [»] | |
| 3ELC | X-ray | 2.50 | A/B/C | 1-159 | [»] | |
| 3EOR | X-ray | 2.90 | A | 1-159 | [»] | |
| 3ERN | X-ray | 2.10 | A/B/C/D/E/F | 1-159 | [»] | |
| 3ESJ | X-ray | 2.70 | A | 1-159 | [»] | |
| 3FBA | X-ray | 3.10 | A | 1-159 | [»] | |
| SMRi | P62617 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 4262279, 277 interactors |
| DIPi | DIP-48029N |
| IntActi | P62617, 7 interactors |
| STRINGi | 511145.b2746 |
Chemistry databases
| BindingDBi | P62617 |
| ChEMBLi | CHEMBL3217375 |
| DrugBanki | DB02552, Geranyl Diphosphate |
Proteomic databases
| jPOSTi | P62617 |
| PaxDbi | P62617 |
| PRIDEi | P62617 |
Genome annotation databases
| EnsemblBacteriai | AAC75788; AAC75788; b2746 BAE76823; BAE76823; BAE76823 |
| GeneIDi | 67413962 945057 |
| KEGGi | ecj:JW2716 eco:b2746 |
| PATRICi | fig|1411691.4.peg.3994 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1763 |
Phylogenomic databases
| eggNOGi | COG0245, Bacteria |
| HOGENOMi | CLU_084630_2_0_6 |
| InParanoidi | P62617 |
| PhylomeDBi | P62617 |
Enzyme and pathway databases
| UniPathwayi | UPA00056;UER00095 |
| BioCyci | EcoCyc:EG11816-MONOMER |
| BRENDAi | 4.6.1.12, 2026 |
| SABIO-RKi | P62617 |
Miscellaneous databases
| EvolutionaryTracei | P62617 |
Protein Ontology More...PROi | PR:P62617 |
Family and domain databases
| CDDi | cd00554, MECDP_synthase, 1 hit |
| Gene3Di | 3.30.1330.50, 1 hit |
| HAMAPi | MF_00107, IspF, 1 hit |
| InterProi | View protein in InterPro IPR003526, MECDP_synthase IPR020555, MECDP_synthase_CS IPR036571, MECDP_synthase_sf |
| PANTHERi | PTHR43181, PTHR43181, 1 hit |
| Pfami | View protein in Pfam PF02542, YgbB, 1 hit |
| SUPFAMi | SSF69765, SSF69765, 1 hit |
| TIGRFAMsi | TIGR00151, ispF, 1 hit |
| PROSITEi | View protein in PROSITE PS01350, ISPF, 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 | ISPF_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 | P62617Primary (citable) accession number: P62617 Secondary accession number(s): P36663, Q2MA83 | |
| <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: | February 23, 2022 | |
| This is version 151 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, Direct protein sequencing, 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
