UniProtKB - P0AEK2 (FABG_ECOLI)

BLAST

>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
MYMV

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History
Entry version 115 (07 Nov 2018)
Sequence version 1 (20 Dec 2005)
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Protein

3-oxoacyl-[acyl-carrier-protein] reductase FabG

Gene

fabG

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.2 Publications

Miscellaneous

Calcium ions stabilize the structure, and may inhibit FabG activity by obstructing access to the active site.

Catalytic activityⁱ

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP⁺ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.1 Publication

Activity regulationⁱ

Inhibited by cinnamic acid derivatives.1 Publication

pH dependenceⁱ

Optimum pH is between 6.0 and 7.0.1 Publication

Pathwayⁱ: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
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	Length
Binding siteⁱ	37	NADPCombined sources1 Publication	1
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 sources1 Publication	1
Binding siteⁱ	138	SubstrateBy similarity	1
Metal bindingⁱ	145	Calcium 2	1
Active siteⁱ	151	Proton acceptorPROSITE-ProRule annotation	1
Binding siteⁱ	184	NADP; via amide nitrogen and carbonyl oxygen1 Publication	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	Length
Nucleotide bindingⁱ	12 – 15	NADPCombined sources1 Publication	4
Nucleotide bindingⁱ	59 – 60	NADPCombined sources1 Publication	2
Nucleotide bindingⁱ	151 – 155	NADPCombined sources1 Publication	5

GO - Molecular functionⁱ

3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
Source: EcoCyc
Inferred from direct assayⁱ
- 14527946
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: EcoCyc
Inferred from direct assayⁱ
- 11669613
metal ion binding Source: UniProtKB-KW
NAD binding Source: InterPro
NADP binding
Source: UniProtKB
Inferred from direct assayⁱ
- 15016358

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

biotin biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 20693992
fatty acid biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 14996818
fatty acid elongation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 14996818
lipid biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 14996818

View the complete GO annotation on QuickGO ...

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

BioCycⁱ	EcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER
BRENDAⁱ	1.1.1.100 2026
UniPathwayⁱ	UPA00094

Chemistry databases

SwissLipidsⁱ	SLP:000000853

SwissLipidsⁱ

SLP:000000853

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC:1.1.1.100) Alternative name(s): 3-ketoacyl-acyl carrier protein reductase Beta-Ketoacyl-acyl carrier protein reductase Beta-ketoacyl-ACP reductase
Gene namesⁱ	Name:fabG Ordered Locus Names:b1093, JW1079
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG11318 fabG

EcoGeneⁱ

EG11318 fabG

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 18304323

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	151	Y → F: Defect in the affinity for NADPH. 1 Publication	1
Mutagenesisⁱ	154	A → T: Decreases in the thermolability of the reductase; when associated with K-233. 1 Publication	1
Mutagenesisⁱ	155	K → A: Defect in the affinity for NADPH. 1 Publication	1
Mutagenesisⁱ	233	E → K: Decreases in the thermolability of the reductase; when associated with T-154. 1 Publication	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose

DrugBankⁱ

DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000054672	1 – 244	3-oxoacyl-[acyl-carrier-protein] reductase FabGAdd BLAST		244

Proteomic databases

EPDⁱ	P0AEK2
PaxDbⁱ	P0AEK2
PRIDEⁱ	P0AEK2

Interactionⁱ

Subunit structureⁱ

Homotetramer.2 Publications

GO - Molecular functionⁱ

identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 11669613

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4260080, 228 interactors
Database of interacting proteins More...DIPⁱ	DIP-31869N
IntActⁱ	P0AEK2, 6 interactors
STRINGⁱ	316385.ECDH10B_1165

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	7 – 12	Combined sources	6
Helixⁱ	16 – 27	Combined sources	12
Beta strandⁱ	31 – 38	Combined sources	8
Helixⁱ	39 – 49	Combined sources	11
Helixⁱ	50 – 52	Combined sources	3
Beta strandⁱ	53 – 57	Combined sources	5
Helixⁱ	63 – 76	Combined sources	14
Beta strandⁱ	81 – 85	Combined sources	5
Helixⁱ	95 – 97	Combined sources	3
Helixⁱ	100 – 110	Combined sources	11
Helixⁱ	112 – 128	Combined sources	17
Beta strandⁱ	131 – 136	Combined sources	6
Helixⁱ	139 – 143	Combined sources	5
Helixⁱ	149 – 169	Combined sources	21
Helixⁱ	170 – 172	Combined sources	3
Beta strandⁱ	174 – 181	Combined sources	8
Helixⁱ	187 – 190	Combined sources	4
Helixⁱ	194 – 201	Combined sources	8
Helixⁱ	212 – 223	Combined sources	12
Helixⁱ	225 – 227	Combined sources	3
Beta strandⁱ	234 – 238	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	P0AEK2
SMRⁱ	P0AEK2
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0AEK2

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the short-chain dehydrogenases/reductases (SDR) family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105CHR Bacteria ENOG410XNW1 LUCA
InParanoidⁱ	P0AEK2
KEGG Orthology (KO) More...KOⁱ	K00059
PhylomeDBⁱ	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

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AEK2-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:244

Mass (Da):25,560

Last modified:December 20, 2005 - v1

Checksum:ⁱ48EC1F2A7F7EEFD9

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
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: 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
NCBI Reference Sequences More...RefSeqⁱ	NP_415611.1, NC_000913.3 WP_001008535.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC74177; AAC74177; b1093 BAA35901; BAA35901; BAA35901
GeneIDⁱ	945645
KEGGⁱ	ecj:JW1079 eco:b1093
PATRICⁱ	fig\|1411691.4.peg.1175

Protein	Similar proteins		Species	Score	Length	Source
P0AEK2	3-oxoacyl-[acyl-carrier-protein] reductase FabG		SHIFL		244	UniRef100_P0AEK2
3-oxoacyl-[acyl-carrier-] reductase domain protein (Fragment)		Shigella flexneri 1235-66		30
Beta-ketoacyl-ACP reductase		Shigella sp.		244
Beta-ketoacyl-ACP reductase		Escherichia coli O145 str. RM9872		244
3-oxoacyl-[acyl-carrier protein] reductase		Klebsiella pneumoniae IS22		244
+160

Protein	Similar proteins		Species	Score	Length	Source
P0AEK2	3-oxoacyl-[acyl-carrier-protein] reductase FabG		SHIFL		244	UniRef90_P0AEK2
3-oxoacyl-[acyl-carrier-protein] reductase FabG		SALTI		244
3-oxoacyl-[acyl-carrier-protein] reductase FabG		SALTY		244
3-oxoacyl-[acyl-carrier-] reductase domain protein (Fragment)		Shigella flexneri 1235-66		30
Beta-ketoacyl-ACP reductase		Shigella sp.		244
+873

Protein	Similar proteins		Species	Score	Length	Source
P0AEK2	3-oxoacyl-[acyl-carrier-protein] reductase FabG		SHIFL		244	UniRef50_P0AEK2
3-oxoacyl-[acyl-carrier-protein] reductase FabG		SALTI		244
3-oxoacyl-[acyl-carrier-protein] reductase FabG		SALTY		244
3-oxoacyl-[acyl-carrier-protein] reductase FabG	)	PSEAE		247
3-oxoacyl-[acyl-carrier-protein] reductase FabG		VIBHA		244
+7062

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_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links 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	[»]
ProteinModelPortalⁱ	P0AEK2
SMRⁱ	P0AEK2
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4260080, 228 interactors
DIPⁱ	DIP-31869N
IntActⁱ	P0AEK2, 6 interactors
STRINGⁱ	316385.ECDH10B_1165

Chemistry databases

DrugBankⁱ	DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
SwissLipidsⁱ	SLP:000000853

Proteomic databases

EPDⁱ	P0AEK2
PaxDbⁱ	P0AEK2
PRIDEⁱ	P0AEK2

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC74177; AAC74177; b1093 BAA35901; BAA35901; BAA35901
GeneIDⁱ	945645
KEGGⁱ	ecj:JW1079 eco:b1093
PATRICⁱ	fig\|1411691.4.peg.1175

Organism-specific databases

EchoBASEⁱ	EB1294
EcoGeneⁱ	EG11318 fabG

Phylogenomic databases

eggNOGⁱ	ENOG4105CHR Bacteria ENOG410XNW1 LUCA
InParanoidⁱ	P0AEK2
KOⁱ	K00059
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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FABG_ECOLI
Accessionⁱ	P0AEK2Primary (citable) accession number: P0AEK2 Secondary accession number(s): P25716, P78221, Q47202
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
	Last sequence update:	December 20, 2005
	Last modified:	November 7, 2018
	This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

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UniRef

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Annotation systems

Supporting data

UniProtKB - P0AEK2 (FABG_ECOLI)

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3-oxoacyl-[acyl-carrier-protein] reductase FabG

fabG

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

Miscellaneous

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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

Sites

Regions

<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

GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<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

Organism-specific databases

<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

GO - Cellular componenti

<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

Chemistry databases

<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

Proteomic databases

<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

GO - Molecular functioni

Protein-protein interaction databases

<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

3D structure databases

Miscellaneous databases

<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

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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Functionⁱ

pH dependenceⁱ

Pathwayⁱ: fatty acid biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ