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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 3

Gene

fabH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.

Catalytic activityi

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2.UniRule annotation

Enzyme regulationi

Negatively regulated by acyl-ACP, possibly by binding to either the free enzyme or the acyl-enzyme intermediate.1 Publication

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation
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
Active sitei1123 Publications1
Active sitei2443 Publications1
Active sitei2743 Publications1

GO - Molecular functioni

GO - Biological processi

  • fatty acid biosynthetic process Source: UniProtKB-HAMAP
  • fatty acid metabolic process Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:FABH-MONOMER.
ECOL316407:JW1077-MONOMER.
MetaCyc:FABH-MONOMER.
BRENDAi2.3.1.180. 2026.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3UniRule annotation (EC:2.3.1.180UniRule annotation)
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase IIIUniRule annotation
Beta-ketoacyl-ACP synthase IIIUniRule annotation
Short name:
KAS IIIUniRule annotation
EcFabH
Gene namesi
Name:fabH
Ordered Locus Names:b1091, JW1077
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10277. fabH.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112C → S: Loss of activity. 1
Mutagenesisi214K → E or A: Strongly reduces the binding to malonyl-ACP but not that of the substrate. 1 Publication1
Mutagenesisi244H → A: Loss of activity. 1
Mutagenesisi249R → E or A: Abolishes the binding to malonyl-ACP but not that of the substrate. 1 Publication1
Mutagenesisi253A → Y: Abolishes both binding to malonyl-ACP and binding to substrate. 1 Publication1
Mutagenesisi256 – 257KK → AA: Strongly reduces both binding to malonyl-ACP and binding to substrate. 1 Publication2
Mutagenesisi256 – 257KK → EE: Abolishes the binding to malonyl-ACP but not that of the substrate. 1 Publication2
Mutagenesisi274N → A: Loss of activity. 1

Chemistry databases

ChEMBLiCHEMBL4914.
DrugBankiDB01034. Cerulenin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001104241 – 3173-oxoacyl-[acyl-carrier-protein] synthase 3Add BLAST317

Proteomic databases

EPDiP0A6R0.
PaxDbiP0A6R0.
PRIDEiP0A6R0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

BioGridi4261031. 458 interactors.
DIPiDIP-48255N.
IntActiP0A6R0. 5 interactors.
MINTiMINT-1263292.
STRINGi511145.b1091.

Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 11Combined sources10
Beta strandi14 – 18Combined sources5
Helixi19 – 23Combined sources5
Helixi30 – 37Combined sources8
Beta strandi41 – 44Combined sources4
Helixi51 – 66Combined sources16
Helixi70 – 72Combined sources3
Beta strandi75 – 79Combined sources5
Beta strandi86 – 88Combined sources3
Helixi90 – 98Combined sources9
Beta strandi105 – 108Combined sources4
Helixi111 – 113Combined sources3
Helixi114 – 127Combined sources14
Beta strandi132 – 140Combined sources9
Helixi142 – 145Combined sources4
Helixi151 – 154Combined sources4
Beta strandi160 – 171Combined sources12
Beta strandi173 – 181Combined sources9
Helixi183 – 188Combined sources6
Beta strandi189 – 192Combined sources4
Beta strandi196 – 198Combined sources3
Helixi209 – 230Combined sources22
Helixi235 – 237Combined sources3
Beta strandi240 – 243Combined sources4
Helixi248 – 257Combined sources10
Helixi262 – 264Combined sources3
Helixi269 – 272Combined sources4
Helixi276 – 278Combined sources3
Helixi279 – 289Combined sources11
Beta strandi298 – 305Combined sources8
Turni306 – 308Combined sources3
Beta strandi309 – 316Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EBLX-ray1.80A/B1-317[»]
1HN9X-ray2.00A/B1-317[»]
1HNDX-ray1.60A1-317[»]
1HNHX-ray1.90A1-317[»]
1HNJX-ray1.46A1-317[»]
1HNKX-ray1.90A1-317[»]
1MZSX-ray2.10A1-317[»]
2EFTX-ray2.00A/B1-317[»]
2GYOX-ray2.00A/B1-317[»]
3IL9X-ray1.85A/B1-317[»]
4Z8DX-ray2.00A/B1-317[»]
5BNMX-ray1.70A/B1-317[»]
5BNRX-ray1.89A1-317[»]
5BNSX-ray2.20A/B1-317[»]
ProteinModelPortaliP0A6R0.
SMRiP0A6R0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6R0.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni245 – 249ACP-binding5

Domaini

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the FabH family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
InParanoidiP0A6R0.
KOiK00648.
OMAiESGMYEN.
PhylomeDBiP0A6R0.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH. 1 hit.
InterProiIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 1 hit.
TIGRFAMsiTIGR00747. fabH. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6R0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYTKIIGTGS YLPEQVRTNA DLEKMVDTSD EWIVTRTGIR ERHIAAPNET
60 70 80 90 100
VSTMGFEAAT RAIEMAGIEK DQIGLIVVAT TSATHAFPSA ACQIQSMLGI
110 120 130 140 150
KGCPAFDVAA ACAGFTYALS VADQYVKSGA VKYALVVGSD VLARTCDPTD
160 170 180 190 200
RGTIIIFGDG AGAAVLAASE EPGIISTHLH ADGSYGELLT LPNADRVNPE
210 220 230 240 250
NSIHLTMAGN EVFKVAVTEL AHIVDETLAA NNLDRSQLDW LVPHQANLRI
260 270 280 290 300
ISATAKKLGM SMDNVVVTLD RHGNTSAASV PCALDEAVRD GRIKPGQLVL
310
LEAFGGGFTW GSALVRF
Length:317
Mass (Da):33,515
Last modified:May 10, 2005 - v1
Checksum:iBF3192CFF36023D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77744 Genomic DNA. Translation: AAA23749.1.
M96793 Genomic DNA. Translation: AAB59065.1.
U00096 Genomic DNA. Translation: AAC74175.1.
AP009048 Genomic DNA. Translation: BAA35899.2.
M87040 Genomic DNA. Translation: AAA23741.1.
Z11565 Genomic DNA. Translation: CAA77659.1.
PIRiA42431.
RefSeqiNP_415609.1. NC_000913.3.
WP_000288132.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74175; AAC74175; b1091.
BAA35899; BAA35899; BAA35899.
GeneIDi946003.
KEGGiecj:JW1077.
eco:b1091.
PATRICi32117423. VBIEscCol129921_1134.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77744 Genomic DNA. Translation: AAA23749.1.
M96793 Genomic DNA. Translation: AAB59065.1.
U00096 Genomic DNA. Translation: AAC74175.1.
AP009048 Genomic DNA. Translation: BAA35899.2.
M87040 Genomic DNA. Translation: AAA23741.1.
Z11565 Genomic DNA. Translation: CAA77659.1.
PIRiA42431.
RefSeqiNP_415609.1. NC_000913.3.
WP_000288132.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EBLX-ray1.80A/B1-317[»]
1HN9X-ray2.00A/B1-317[»]
1HNDX-ray1.60A1-317[»]
1HNHX-ray1.90A1-317[»]
1HNJX-ray1.46A1-317[»]
1HNKX-ray1.90A1-317[»]
1MZSX-ray2.10A1-317[»]
2EFTX-ray2.00A/B1-317[»]
2GYOX-ray2.00A/B1-317[»]
3IL9X-ray1.85A/B1-317[»]
4Z8DX-ray2.00A/B1-317[»]
5BNMX-ray1.70A/B1-317[»]
5BNRX-ray1.89A1-317[»]
5BNSX-ray2.20A/B1-317[»]
ProteinModelPortaliP0A6R0.
SMRiP0A6R0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261031. 458 interactors.
DIPiDIP-48255N.
IntActiP0A6R0. 5 interactors.
MINTiMINT-1263292.
STRINGi511145.b1091.

Chemistry databases

ChEMBLiCHEMBL4914.
DrugBankiDB01034. Cerulenin.

Proteomic databases

EPDiP0A6R0.
PaxDbiP0A6R0.
PRIDEiP0A6R0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74175; AAC74175; b1091.
BAA35899; BAA35899; BAA35899.
GeneIDi946003.
KEGGiecj:JW1077.
eco:b1091.
PATRICi32117423. VBIEscCol129921_1134.

Organism-specific databases

EchoBASEiEB0273.
EcoGeneiEG10277. fabH.

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
InParanoidiP0A6R0.
KOiK00648.
OMAiESGMYEN.
PhylomeDBiP0A6R0.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciEcoCyc:FABH-MONOMER.
ECOL316407:JW1077-MONOMER.
MetaCyc:FABH-MONOMER.
BRENDAi2.3.1.180. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A6R0.
PROiP0A6R0.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH. 1 hit.
InterProiIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 1 hit.
TIGRFAMsiTIGR00747. fabH. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFABH_ECOLI
AccessioniPrimary (citable) accession number: P0A6R0
Secondary accession number(s): P24249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: November 2, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Inhibited by the SB418011 antibiotic. Not inhibited by cerulenin and thiolactomycin.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.