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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

Enzyme 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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei37NADPCombined sources1 Publication1
Metal bindingi50Calcium 1; via carbonyl oxygen; shared with dimeric partner1
Metal bindingi53Calcium 1; via carbonyl oxygen; shared with dimeric partner1
Binding sitei86NADP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei138SubstrateBy similarity1
Metal bindingi145Calcium 21
Active sitei151Proton acceptorPROSITE-ProRule annotation1
Binding sitei184NADP; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi233Calcium 3; shared with dimeric partner1
Metal bindingi234Calcium 3; via carbonyl oxygen; shared with dimeric partner1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 15NADPCombined sources1 Publication4
Nucleotide bindingi59 – 60NADPCombined sources1 Publication2
Nucleotide bindingi151 – 155NADPCombined sources1 Publication5

GO - Molecular functioni

GO - Biological processi

  • biotin biosynthetic process Source: EcoCyc
  • fatty acid biosynthetic process Source: EcoCyc
  • fatty acid elongation Source: UniProtKB
  • lipid biosynthetic process Source: EcoCyc

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandCalcium, Metal-binding, NADP

Enzyme and pathway databases

BioCyciEcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER
MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER
BRENDAi1.1.1.100 2026
UniPathwayiUPA00094

Chemistry databases

SwissLipidsiSLP: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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11318 fabG

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi151Y → F: Defect in the affinity for NADPH. 1 Publication1
Mutagenesisi154A → T: Decreases in the thermolability of the reductase; when associated with K-233. 1 Publication1
Mutagenesisi155K → A: Defect in the affinity for NADPH. 1 Publication1
Mutagenesisi233E → K: Decreases in the thermolability of the reductase; when associated with T-154. 1 Publication1

Chemistry databases

DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000546721 – 2443-oxoacyl-[acyl-carrier-protein] reductase FabGAdd BLAST244

Proteomic databases

EPDiP0AEK2
PaxDbiP0AEK2
PRIDEiP0AEK2

Interactioni

Subunit structurei

Homotetramer.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260080, 228 interactors
DIPiDIP-31869N
IntActiP0AEK2, 6 interactors
STRINGi316385.ECDH10B_1165

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 12Combined sources6
Helixi16 – 27Combined sources12
Beta strandi31 – 38Combined sources8
Helixi39 – 49Combined sources11
Helixi50 – 52Combined sources3
Beta strandi53 – 57Combined sources5
Helixi63 – 76Combined sources14
Beta strandi81 – 85Combined sources5
Helixi95 – 97Combined sources3
Helixi100 – 110Combined sources11
Helixi112 – 128Combined sources17
Beta strandi131 – 136Combined sources6
Helixi139 – 143Combined sources5
Helixi149 – 169Combined sources21
Helixi170 – 172Combined sources3
Beta strandi174 – 181Combined sources8
Helixi187 – 190Combined sources4
Helixi194 – 201Combined sources8
Helixi212 – 223Combined sources12
Helixi225 – 227Combined sources3
Beta strandi234 – 238Combined sources5

3D structure databases

ProteinModelPortaliP0AEK2
SMRiP0AEK2
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEK2

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CHR Bacteria
ENOG410XNW1 LUCA
InParanoidiP0AEK2
KOiK00059
OMAiGSRNIRC
PhylomeDBiP0AEK2

Family and domain databases

InterProiView protein in InterPro
IPR011284 3oxo_ACP_reduc
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01830 3oxo_ACP_reduc, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

Sequencei

Sequence statusi: Complete.

P0AEK2-1 [UniParc]FASTAAdd 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
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30A → G in AAA23739 (PubMed:1556094).Curated1
Sequence conflicti43Q → R in AAA23739 (PubMed:1556094).Curated1

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
PIRiB64853 B42147
RefSeqiNP_415611.1, NC_000913.3
WP_001008535.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74177; AAC74177; b1093
BAA35901; BAA35901; BAA35901
GeneIDi945645
KEGGiecj:JW1079
eco:b1093
PATRICifig|1411691.4.peg.1175

Similar proteinsi

Entry informationi

Entry nameiFABG_ECOLI
AccessioniPrimary (citable) accession number: P0AEK2
Secondary accession number(s): P25716, P78221, Q47202
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 28, 2018
This is version 113 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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