UniProtKB - P0AEK2 (FABG_ECOLI)
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>sp|P0AEK2|FABG_ECOLI 3-oxoacyl-[acyl-carrier-protein] reductase FabG OS=Escherichia coli (strain K12) OX=83333 GN=fabG PE=1 SV=1 MNFEGKIALVTGASRGIGRAIAETLAARGAKVIGTATSENGAQAISDYLGANGKGLMLNV TDPASIESVLEKIRAEFGEVDILVNNAGITRDNLLMRMKDEEWNDIIETNLSSVFRLSKA VMRAMMKKRHGRIITIGSVVGTMGNGGQANYAAAKAGLIGFSKSLAREVASRGITVNVVA PGFIETDMTRALSDDQRAGILAQVPAGRLGGAQEIANAVAFLASDEAAYITGETLHVNGG MYMVCommunity curation ()Add a publicationFeedback
3-oxoacyl-[acyl-carrier-protein] reductase FabG
fabG
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 270:26538-26542(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.8"Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:10996-11000(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A BETA-KETOACYL-ACP REDUCTASE, CATALYTIC ACTIVITY. - Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.11"Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium."
Lai C.Y., Cronan J.E.
J. Bacteriol. 186:1869-1878(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS AND AS A BETA-KETOACYL-ACP REDUCTASE, MUTAGENESIS OF ALA-154 AND GLU-233.
Miscellaneous
<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
- a (3R)-hydroxyacyl-[ACP]EC:1.1.1.100
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Manual assertion based on experiment ini
- Ref.7"Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 270:26538-26542(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.8"Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:10996-11000(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A BETA-KETOACYL-ACP REDUCTASE, CATALYTIC ACTIVITY. - Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
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Manual assertion based on experiment ini
- Ref.7"Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 270:26538-26542(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.8"Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:10996-11000(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A BETA-KETOACYL-ACP REDUCTASE, CATALYTIC ACTIVITY. - Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the backward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.7"Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 270:26538-26542(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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a (3R)-hydroxyacyl-[ACP]- Search proteins in UniProtKB for this molecule.
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(3R)-hydroxyacyl-pantetheine-4-phosphorylserine residuezoom- Search proteins in UniProtKB for this molecule.
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=a 3-oxoacyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxoacylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxobutanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.7"Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 270:26538-26542(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.7"Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 270:26538-26542(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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3-oxobutanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxobutanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxybutanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxybutanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxopentanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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3-oxopentanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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3-oxopentanoyl-pantetheine-4-phosphorylserine residuezoom- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+NADPH- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxypentanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxypentanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxohexanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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3-oxohexanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxohexanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxyhexanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxyhexanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxoheptanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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3-oxoheptanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxoheptanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxyheptanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxyheptanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxooctanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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3-oxooctanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxooctanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxyoctanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxyoctanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxononanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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3-oxononanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxononanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxynonanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxynonanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxodecanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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3-oxodecanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxodecanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+NADPH- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxydecanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxydecanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxohexadecanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
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3-oxohexadecanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxohexadecanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxyhexadecanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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- 3-oxo-(9Z)-hexadecenoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion based on experiment ini
- Ref.9"Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
Heath R.J., Rock C.O.
J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
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3-oxo-(9Z)-hexadecenoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-[S-3-oxo-(9Z-hexadecenoylpantetheine)-4ʼ-phosphoryl]-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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O-[S-(3R)-hydroxy-(9Z)-hexadecenoylpantetheine-4ʼ-phosphoryl]-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxo-4-methylpentanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
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3-oxo-4-methylpentanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxo-4-methyl-pentanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxy-4-methylpentanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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- 3-oxo-5-methylhexanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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3-oxo-5-methylhexanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxo-5-methylhexanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+NADPH- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxy-5-methylhexanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxy-5-methylhexanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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+NADP+- Search proteins in UniProtKB for this molecule.
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- 3-oxo-4-methylhexanoyl-[ACP]
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Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.10"Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis."
Choi K.-H., Heath R.J., Rock C.O.
J. Bacteriol. 182:365-370(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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3-oxo-4-methylhexanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3-oxo-4-methylhexanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+NADPH- Search proteins in UniProtKB for this molecule.
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=(3R)-hydroxy-4-methylhexanoyl-[ACP]- Search proteins in UniProtKB for this molecule.
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O-(S-3R-hydroxy-4-methylhexanoylpantetheine-4ʼ-phosphoryl)-L-serine residuezoom- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Manual assertion based on experiment ini
- Ref.12"Novel inhibitors of beta-ketoacyl-ACP reductase from Escherichia coli."
Kristan K., Bratkovic T., Sova M., Gobec S., Prezelj A., Urleb U.
Chem. Biol. Interact. 178:310-316(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION.
<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>pH dependencei
Manual assertion based on experiment ini
- Ref.6"Studies on the mechanism of fatty acid synthesis. XV. Preparation and general properties of beta-ketoacyl acyl carrier protein reductase from Escherichia coli."
Toomey R.E., Wakil S.J.
Biochim. Biophys. Acta 116:189-197(1966) [PubMed] [Europe PMC] [Abstract]Cited for: 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: fatty acid biosynthesis
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.2 PublicationsManual assertion based on experiment ini
- Ref.7"Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli."
Heath R.J., Rock C.O.
J. Biol. Chem. 270:26538-26542(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. - Ref.11"Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium."
Lai C.Y., Cronan J.E.
J. Bacteriol. 186:1869-1878(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS AND AS A BETA-KETOACYL-ACP REDUCTASE, MUTAGENESIS OF ALA-154 AND GLU-233.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section 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 | 37 | NADPCombined 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 1 PublicationManual assertion based on experiment ini
| 1 | |
<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 | 50 | Calcium 1; via carbonyl oxygen; shared with dimeric partner | 1 | |
Metal bindingi | 53 | Calcium 1; via carbonyl oxygen; shared with dimeric partner | 1 | |
Binding sitei | 86 | NADP; via carbonyl oxygenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
Binding sitei | 138 | SubstrateBy similarity | 1 | |
Metal bindingi | 145 | Calcium 2 | 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 | 151 | Proton acceptorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
Binding sitei | 184 | NADP; via amide nitrogen and carbonyl oxygen1 Publication Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 233 | Calcium 3; shared with dimeric partner | 1 | |
Metal bindingi | 234 | Calcium 3; via carbonyl oxygen; shared with dimeric partner | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 12 – 15 | NADPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 4 | |
Nucleotide bindingi | 59 – 60 | NADPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 2 | |
Nucleotide bindingi | 151 – 155 | NADPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 5 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- "Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction."
Zhang Y.M., Wu B., Zheng J., Rock C.O.
J Biol Chem 278:52935-52943(2003) [PubMed] [Europe PMC] [Abstract]
- 3-oxo-glutaryl-[acp] methyl ester reductase activity Source: UniProtKB-EC
- 3-oxo-pimeloyl-[acp] methyl ester reductase activity Source: UniProtKB-EC
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.13"Structure of beta-ketoacyl-[acyl carrier-protein] reductase from Escherichia coli: negative cooperativity and its structural basis."
Price A.C., Zhang Y.-M., Rock C.O., White S.W.
Biochemistry 40:12772-12781(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
- metal ion binding Source: UniProtKB-KW
- NAD binding Source: InterPro
- NADP binding Source: UniProtKBInferred from direct assayi
- Ref.14"Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG."
Price A.C., Zhang Y.M., Rock C.O., White S.W.
Structure 12:417-428(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH NADP, MUTAGENESIS OF TYR-151 AND LYS-155, REACTION MECHANISM, SUBUNIT.
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
GO - Biological processi
- biotin biosynthetic process Source: EcoCyc
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "Biotin synthesis begins by hijacking the fatty acid synthetic pathway."
Lin S., Hanson R.E., Cronan J.E.
Nat. Chem. Biol. 6:682-688(2010) [PubMed] [Europe PMC] [Abstract]
- fatty acid biosynthetic process Source: EcoCycInferred from mutant phenotypei
- Ref.11"Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium."
Lai C.Y., Cronan J.E.
J. Bacteriol. 186:1869-1878(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS AND AS A BETA-KETOACYL-ACP REDUCTASE, MUTAGENESIS OF ALA-154 AND GLU-233.
- fatty acid elongation Source: UniProtKBInferred from mutant phenotypei
- Ref.11"Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium."
Lai C.Y., Cronan J.E.
J. Bacteriol. 186:1869-1878(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS AND AS A BETA-KETOACYL-ACP REDUCTASE, MUTAGENESIS OF ALA-154 AND GLU-233.
- lipid biosynthetic process Source: EcoCycInferred from mutant phenotypei
- Ref.11"Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium."
Lai C.Y., Cronan J.E.
J. Bacteriol. 186:1869-1878(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN FATTY ACID BIOSYNTHESIS AND AS A BETA-KETOACYL-ACP REDUCTASE, MUTAGENESIS OF ALA-154 AND GLU-233.
<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 | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Ligand | Calcium, Metal-binding, NADP |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.1.1.100, 2026 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00094 |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000000853 |
<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: 3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC:1.1.1.100
Manual assertion based on experiment ini
Alternative name(s): 3-ketoacyl-acyl carrier protein reductase Beta-Ketoacyl-acyl carrier protein reductase Beta-ketoacyl-ACP reductase |
<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:fabG Ordered Locus Names:b1093, JW1079 |
<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
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 | 151 | Y → F: Defect in the affinity for NADPH. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 154 | A → T: Decreases in the thermolability of the reductase; when associated with K-233. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 155 | K → A: Defect in the affinity for NADPH. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 233 | E → K: Decreases in the thermolability of the reductase; when associated with T-154. 1 Publication Manual assertion based on experiment ini
| 1 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB03461, Nicotinamide adenine dinucleotide phosphate |
<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_0000054672 | 1 – 244 | 3-oxoacyl-[acyl-carrier-protein] reductase FabGAdd BLAST | 244 |
Proteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P0AEK2 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0AEK2 |
PRoteomics IDEntifications database More...PRIDEi | P0AEK2 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homotetramer.
2 PublicationsManual assertion based on experiment ini
- Ref.13"Structure of beta-ketoacyl-[acyl carrier-protein] reductase from Escherichia coli: negative cooperativity and its structural basis."
Price A.C., Zhang Y.-M., Rock C.O., White S.W.
Biochemistry 40:12772-12781(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT. - Ref.14"Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG."
Price A.C., Zhang Y.M., Rock C.O., White S.W.
Structure 12:417-428(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH NADP, MUTAGENESIS OF TYR-151 AND LYS-155, REACTION MECHANISM, SUBUNIT.
GO - Molecular functioni
- identical protein binding Source: EcoCycInferred from direct assayi
- Ref.13"Structure of beta-ketoacyl-[acyl carrier-protein] reductase from Escherichia coli: negative cooperativity and its structural basis."
Price A.C., Zhang Y.-M., Rock C.O., White S.W.
Biochemistry 40:12772-12781(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 4260080, 228 interactors |
Database of interacting proteins More...DIPi | DIP-31869N |
Protein interaction database and analysis system More...IntActi | P0AEK2, 6 interactors |
STRING: functional protein association networks More...STRINGi | 511145.b1093 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 7 – 12 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 16 – 27 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 31 – 38 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 39 – 49 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 50 – 52 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 53 – 57 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 63 – 76 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
Beta strandi | 81 – 85 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 95 – 97 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 100 – 110 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 112 – 128 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
Beta strandi | 131 – 136 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 139 – 143 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 149 – 169 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
Helixi | 170 – 172 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 174 – 181 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 187 – 190 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 194 – 201 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 212 – 223 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Helixi | 225 – 227 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 234 – 238 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0AEK2 |
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 | P0AEK2 |
<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
<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 | COG1028, Bacteria |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_010194_1_3_6 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0AEK2 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0AEK2 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR011284, 3oxo_ACP_reduc IPR036291, NAD(P)-bd_dom_sf IPR020904, Sc_DH/Rdtase_CS IPR002347, SDR_fam |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00081, GDHRDH PR00080, SDRFAMILY |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51735, SSF51735, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR01830, 3oxo_ACP_reduc, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
10 20 30 40 50
MNFEGKIALV TGASRGIGRA IAETLAARGA KVIGTATSEN GAQAISDYLG
60 70 80 90 100
ANGKGLMLNV TDPASIESVL EKIRAEFGEV DILVNNAGIT RDNLLMRMKD
110 120 130 140 150
EEWNDIIETN LSSVFRLSKA VMRAMMKKRH GRIITIGSVV GTMGNGGQAN
160 170 180 190 200
YAAAKAGLIG FSKSLAREVA SRGITVNVVA PGFIETDMTR ALSDDQRAGI
210 220 230 240
LAQVPAGRLG GAQEIANAVA FLASDEAAYI TGETLHVNGG MYMV
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 30 | A → G in AAA23739 (PubMed:1556094).Curated | 1 | |
Sequence conflicti | 43 | Q → R in AAA23739 (PubMed:1556094).Curated | 1 |
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 | M84991 Genomic DNA Translation: AAA23739.1 U00096 Genomic DNA Translation: AAC74177.1 AP009048 Genomic DNA Translation: BAA35901.1 M87040 Genomic DNA Translation: AAA23743.1 |
Protein sequence database of the Protein Information Resource More...PIRi | B64853, B42147 |
NCBI Reference Sequences More...RefSeqi | NP_415611.1, NC_000913.3 WP_001008535.1, NZ_STEB01000016.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC74177; AAC74177; b1093 BAA35901; BAA35901; BAA35901 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 58461213 945645 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW1079 eco:b1093 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.1175 |
<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 | |
---|---|---|---|---|---|---|
P0AEK2 | 3-oxoacyl-[acyl-carrier-protein] reductase FabG | 244 | UniRef100_P0AEK2 | |||
3-oxoacyl-ACP reductase | 123 | |||||
3-oxoacyl-[acyl-carrier-protein] reductase | 244 | |||||
3-oxoacyl-[acyl-carrier-protein] reductase | 244 | |||||
3-oxoacyl-[acyl-carrier-protein] reductase | 244 | |||||
+203 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P0AEK2 | 3-oxoacyl-[acyl-carrier-protein] reductase FabG | 244 | UniRef90_P0AEK2 | |||
3-oxoacyl-ACP reductase | 123 | |||||
3-oxoacyl-[acyl-carrier-protein] reductase | 244 | |||||
3-oxoacyl-[acyl-carrier-protein] reductase | 244 | |||||
3-oxoacyl-[acyl-carrier-protein] reductase | 244 | |||||
+240 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P0AEK2 | 3-oxoacyl-[acyl-carrier-protein] reductase FabG | 244 | UniRef50_P0AEK2 | |||
3-oxoacyl-[acyl-carrier-protein] reductase FabG | ) | 244 | ||||
3-oxoacyl-[acyl-carrier-protein] reductase FabG | 244 | |||||
3-oxoacyl-ACP reductase | 123 | |||||
3-oxoacyl-[acyl-carrier-protein] reductase | 244 | |||||
+954 |
<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 | M84991 Genomic DNA Translation: AAA23739.1 U00096 Genomic DNA Translation: AAC74177.1 AP009048 Genomic DNA Translation: BAA35901.1 M87040 Genomic DNA Translation: AAA23743.1 |
PIRi | B64853, B42147 |
RefSeqi | NP_415611.1, NC_000913.3 WP_001008535.1, NZ_STEB01000016.1 |
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 |
1I01 | X-ray | 2.60 | A/B/C/D/E/F/G/H | 1-244 | [»] | |
1Q7B | X-ray | 2.05 | A/B/C/D | 1-244 | [»] | |
1Q7C | X-ray | 2.50 | A/B | 1-244 | [»] | |
SMRi | P0AEK2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260080, 228 interactors |
DIPi | DIP-31869N |
IntActi | P0AEK2, 6 interactors |
STRINGi | 511145.b1093 |
Chemistry databases
DrugBanki | DB03461, Nicotinamide adenine dinucleotide phosphate |
SwissLipidsi | SLP:000000853 |
Proteomic databases
jPOSTi | P0AEK2 |
PaxDbi | P0AEK2 |
PRIDEi | P0AEK2 |
Genome annotation databases
EnsemblBacteriai | AAC74177; AAC74177; b1093 BAA35901; BAA35901; BAA35901 |
GeneIDi | 58461213 945645 |
KEGGi | ecj:JW1079 eco:b1093 |
PATRICi | fig|1411691.4.peg.1175 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1294 |
Phylogenomic databases
eggNOGi | COG1028, Bacteria |
HOGENOMi | CLU_010194_1_3_6 |
InParanoidi | P0AEK2 |
PhylomeDBi | P0AEK2 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
BioCyci | EcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER |
BRENDAi | 1.1.1.100, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0AEK2 |
Protein Ontology More...PROi | PR:P0AEK2 |
Family and domain databases
InterProi | View protein in InterPro IPR011284, 3oxo_ACP_reduc IPR036291, NAD(P)-bd_dom_sf IPR020904, Sc_DH/Rdtase_CS IPR002347, SDR_fam |
PRINTSi | PR00081, GDHRDH PR00080, SDRFAMILY |
SUPFAMi | SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR01830, 3oxo_ACP_reduc, 1 hit |
PROSITEi | View protein in PROSITE PS00061, ADH_SHORT, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | FABG_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 | P0AEK2Primary (citable) accession number: P0AEK2 Secondary accession number(s): P25716, P78221, Q47202 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 20, 2005 |
Last sequence update: | December 20, 2005 | |
Last modified: | April 7, 2021 | |
This is version 133 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