Q17YQ2 (FABH_HELAH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3
EC=2.3.1.41

Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III
Beta-ketoacyl-ACP synthase III
Short name=KAS III

Gene names

Name:	fabH
Ordered Locus Names:	Hac_0387

Organism

Helicobacter acinonychis (strain Sheeba) [Complete proteome] [HAMAP]

Taxonomic identifier

382638 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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 By similarity. HAMAP MF_01815
Catalytic activity	Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. HAMAP MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815
Subunit structure	Homodimer By similarity. HAMAP MF_01815
Subcellular location	Cytoplasm Probable HAMAP MF_01815.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP MF_01815
Sequence similarities	Belongs to the FabH family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 331	331	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000056366
Regions
	Region	256 – 260	5	ACP-binding By similarity
Sites
	Active site	115	1	By similarity
	Active site	255	1	By similarity
	Active site	285	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q17YQ2 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: 2413A726C94531B3	FASTA	331	36,221
	10 20 30 40 50 60 MEFYASLKSI AMHAPSECIK NVAFQEFLDT SDEWIEKRTG IKERRFASVG EKSSDLGVIA 70 80 90 100 110 120 AKQAIERAHL TPQDIDLVVV ATLSPDFLAM PSTACVLSAK LGIENKPAFD ISAACTGFIY 130 140 150 160 170 180 LLSVAKAYVE SGMYENVLIV GAEKTSSVLD FKDRGTCILF GDGAGACVIG RTKHLKESIL 190 200 210 220 230 240 DVQISANGNF SNYLYTPRTL KPTPFNAKEE TSDPFLCMKG NEVFKLAVKT LLKDVEMILE 250 260 270 280 290 300 KNALKPEDVR LFIPHQANLR IIQAVREHLD FKDEQVVLTV HKYGNTSAAS IPMAMGEAYE 310 320 330 EGRLKKGDLM LLDAFGGGLT WGSALVYFGG S

References

[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: 16789826] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sheeba.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM260522 Genomic DNA. Translation: CAJ99224.1.
RefSeq	YP_664223.1. NC_008229.1.
3D structure databases
ProteinModelPortal	Q17YQ2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q17YQ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4177410.
GenomeReviews	Gene locus Hac_0387 in contig AM260522_GR.
KEGG	hac:Hac_0387.
NMPDR	fig|382638.8.peg.376.
PATRIC	20584707. VBIHelAci71660_0379.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	RILNFLA.
PhylomeDB	Q17YQ2.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	HACI382638:HAC_0387-MONOMER.
Family and domain databases
HAMAP	MF_01815. FabH. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KO	K00648.
Pfam	PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view]
SUPFAM	SSF53901. Thiolase-like. 1 hit.
TIGRFAMs	TIGR00747. FabH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABH_HELAH

Accession

Primary (citable) accession number: Q17YQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 25, 2006
Last modified:	January 25, 2012
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program