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Protein

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

Gene

fabH

Organism
Helicobacter acinonychis (strain Sheeba)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.UniRule annotation

Catalytic activityi

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

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 sitei115 – 1151UniRule annotation
Active sitei255 – 2551UniRule annotation
Active sitei285 – 2851UniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciHACI382638:GJAU-366-MONOMER.
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
Gene namesi
Name:fabHUniRule annotation
Ordered Locus Names:Hac_0387
OrganismiHelicobacter acinonychis (strain Sheeba)
Taxonomic identifieri382638 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000000775 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3313313-oxoacyl-[acyl-carrier-protein] synthase 3PRO_1000056366Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi382638.Hac_0387.

Structurei

3D structure databases

ProteinModelPortaliQ17YQ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni256 – 2605ACP-bindingUniRule annotation

Domaini

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

Sequence similaritiesi

Belongs to the FabH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
KOiK00648.
OMAiESGMYEN.
OrthoDBiEOG6J74XN.

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.

Q17YQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFYASLKSI AMHAPSECIK NVAFQEFLDT SDEWIEKRTG IKERRFASVG
60 70 80 90 100
EKSSDLGVIA AKQAIERAHL TPQDIDLVVV ATLSPDFLAM PSTACVLSAK
110 120 130 140 150
LGIENKPAFD ISAACTGFIY LLSVAKAYVE SGMYENVLIV GAEKTSSVLD
160 170 180 190 200
FKDRGTCILF GDGAGACVIG RTKHLKESIL DVQISANGNF SNYLYTPRTL
210 220 230 240 250
KPTPFNAKEE TSDPFLCMKG NEVFKLAVKT LLKDVEMILE KNALKPEDVR
260 270 280 290 300
LFIPHQANLR IIQAVREHLD FKDEQVVLTV HKYGNTSAAS IPMAMGEAYE
310 320 330
EGRLKKGDLM LLDAFGGGLT WGSALVYFGG S
Length:331
Mass (Da):36,221
Last modified:July 25, 2006 - v1
Checksum:i2413A726C94531B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260522 Genomic DNA. Translation: CAJ99224.1.
RefSeqiWP_011577338.1. NC_008229.1.

Genome annotation databases

EnsemblBacteriaiCAJ99224; CAJ99224; Hac_0387.
KEGGihac:Hac_0387.
PATRICi20584707. VBIHelAci71660_0379.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260522 Genomic DNA. Translation: CAJ99224.1.
RefSeqiWP_011577338.1. NC_008229.1.

3D structure databases

ProteinModelPortaliQ17YQ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi382638.Hac_0387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ99224; CAJ99224; Hac_0387.
KEGGihac:Hac_0387.
PATRICi20584707. VBIHelAci71660_0379.

Phylogenomic databases

eggNOGiENOG4105CCZ. Bacteria.
COG0332. LUCA.
HOGENOMiHOG000246674.
KOiK00648.
OMAiESGMYEN.
OrthoDBiEOG6J74XN.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciHACI382638:GJAU-366-MONOMER.

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

  1. "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
    Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
    PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sheeba.

Entry informationi

Entry nameiFABH_HELAH
AccessioniPrimary (citable) accession number: Q17YQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: November 11, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.