Q8YGH9 (FABH_BRUME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3
EC=2.3.1.180

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:	BMEI1180

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	323 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	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. 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: InterPro beta-ketoacyl-acyl-carrier-protein synthase III 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 – 323	323	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110407
Regions
	Region	251 – 255	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	250	1	By similarity
	Active site	280	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YGH9 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: B90A5420ADA296C7	FASTA	323	34,448
	10 20 30 40 50 60 MIRSVVRGIG SALPKRVMKN TDFEGIVETS DEWIVQRTGI RERHIAGEGE TTVSLGAAAA 70 80 90 100 110 120 RAAIENAGLQ PSDIDLVLLA TSTPNNTFPA SAVAIQRELG ITRGFAFDLQ AVCSGFIYAI 130 140 150 160 170 180 TTADLYIRGG MARRVLVIGA ETFSRILDWT DRTTCVLFGD GAGAIVLEAA EGHGLTSDRG 190 200 210 220 230 240 ILAANLRSDG NHKEKLYVDG GPSTTQTVGH LRMEGREVFK HAVGMITDVI EASFEATGLT 250 260 270 280 290 300 AEDIDWFVPH QANKRIIDAS AKKLHIAEEK VVITVDRHGN TSAASVPLAL ATAVADGRIK 310 320 KGDLVLLEAM GGGFTWGAVL VRW

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008917 Genomic DNA. Translation: AAL52361.1.
PIR	AF3399.
RefSeq	NP_540097.1. NC_003317.1.
3D structure databases
ProteinModelPortal	Q8YGH9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1196891.
GenomeReviews	Gene locus BMEI1180 in contig AE008917_GR.
KEGG	bme:BMEI1180.
PATRIC	17797648. VBIBruMel146950_0642.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG649927.
OMA	CSSDLGL.
PhylomeDB	Q8YGH9.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	BMEL224914:BMEI1180-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_BRUME

Accession

Primary (citable) accession number: Q8YGH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program