Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei112 – 11213 Publications
Active sitei244 – 24413 Publications
Active sitei274 – 27413 Publications

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121C → S: Loss of activity.
Mutagenesisi214 – 2141K → E or A: Strongly reduces the binding to malonyl-ACP but not that of the substrate. 1 Publication
Mutagenesisi244 – 2441H → A: Loss of activity.
Mutagenesisi249 – 2491R → E or A: Abolishes the binding to malonyl-ACP but not that of the substrate. 1 Publication
Mutagenesisi253 – 2531A → Y: Abolishes both binding to malonyl-ACP and binding to substrate. 1 Publication
Mutagenesisi256 – 2572KK → AA: Strongly reduces both binding to malonyl-ACP and binding to substrate. 1 Publication
Mutagenesisi256 – 2572KK → EE: Abolishes the binding to malonyl-ACP but not that of the substrate. 1 Publication
Mutagenesisi274 – 2741N → A: Loss of activity.

Chemistry

ChEMBLiCHEMBL4914.
DrugBankiDB01034. Cerulenin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3173173-oxoacyl-[acyl-carrier-protein] synthase 3PRO_0000110424Add
BLAST

Proteomic databases

EPDiP0A6R0.
PaxDbiP0A6R0.
PRIDEiP0A6R0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

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

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1110Combined sources
Beta strandi14 – 185Combined sources
Helixi19 – 235Combined sources
Helixi30 – 378Combined sources
Beta strandi41 – 444Combined sources
Helixi51 – 6616Combined sources
Helixi70 – 723Combined sources
Beta strandi75 – 795Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 989Combined sources
Beta strandi105 – 1084Combined sources
Helixi111 – 1133Combined sources
Helixi114 – 12714Combined sources
Beta strandi132 – 1409Combined sources
Helixi142 – 1454Combined sources
Helixi151 – 1544Combined sources
Beta strandi160 – 17112Combined sources
Beta strandi173 – 1819Combined sources
Helixi183 – 1886Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi196 – 1983Combined sources
Helixi209 – 23022Combined sources
Helixi235 – 2373Combined sources
Beta strandi240 – 2434Combined sources
Helixi248 – 25710Combined sources
Helixi262 – 2643Combined sources
Helixi269 – 2724Combined sources
Helixi276 – 2783Combined sources
Helixi279 – 28911Combined sources
Beta strandi298 – 3058Combined sources
Turni306 – 3083Combined sources
Beta strandi309 – 3168Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6R0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni245 – 2495ACP-binding

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.
OrthoDBiEOG6J74XN.
PhylomeDBiP0A6R0.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
HAMAPiMF_01815. FabH.
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
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. Positions 1-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

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.
OrthoDBiEOG6J74XN.
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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12."
    Tsay J.-T., Oh W., Larson T.J., Jackowski S., Rock C.O.
    J. Biol. Chem. 267:6807-6814(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Physical locations of genes in the rne (ams)-rpmF-plsX-fab region of the Escherichia coli K-12 chromosome."
    Oh W., Larson T.J.
    J. Bacteriol. 174:7873-7874(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
    Strain: K12.
  5. "Cloning, nucleotide sequence, and expression of the Escherichia coli fabD gene, encoding malonyl coenzyme A-acyl carrier protein transacylase."
    Verwoert I.I.G.S., Verbree E.C., van der Linden K.H., Nijkamp H.J., Stuitje A.R.
    J. Bacteriol. 174:2851-2857(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-317.
  6. "Cloning and nucleotide sequence of the fabD gene encoding malonyl coenzyme A-acyl carrier protein transacylase of Escherichia coli."
    Magnuson K., Oh W., Larson T.J., Cronan J.E. Jr.
    FEBS Lett. 299:262-266(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-317.
    Strain: K12.
  7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 201-317.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  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: ENZYME REGULATION.
  9. "Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III."
    Zhang Y.-M., Rao M.S., Heath R.J., Price A.C., Olson A.J., Rock C.O., White S.W.
    J. Biol. Chem. 276:8231-8238(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, MUTAGENESIS OF LYS-214; ARG-249; ALA-253 AND 256-LYS-LYS-257.
  10. "Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH)."
    Khandekar S.S., Gentry D.R., Van Aller G.S., Warren P., Xiang H., Silverman C., Doyle M.L., Chambers P.A., Konstantinidis A.K., Brandt M., Daines R.A., Lonsdale J.T.
    J. Biol. Chem. 276:30024-30030(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION BY ANTIBIOTICS.
  11. "Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis."
    Qiu X., Janson C.A., Konstantinidis A.K., Nwagwu S., Silverman C., Smith W.W., Khandekar S., Lonsdale J., Abdel-Meguid S.S.
    J. Biol. Chem. 274:36465-36471(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), ACTIVE SITE.
  12. "The 1.8-A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli."
    Davies C., Heath R.J., White S.W., Rock C.O.
    Structure 8:185-195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), ACTIVE SITE.
  13. "Refined structures of beta-ketoacyl-acyl carrier protein synthase III."
    Qiu X., Janson C.A., Smith W.W., Head M., Lonsdale J., Konstantinidis A.K.
    J. Mol. Biol. 307:341-356(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), ACTIVE SITE.

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: July 6, 2016
This is version 108 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.