Q9K8W9 (FABH1_BACHD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1
EC=2.3.1.180

Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III protein 1
Beta-ketoacyl-ACP synthase III 1
Short name=KAS III 1

Gene names

Name:	fabH1
Ordered Locus Names:	BH2883

Organism

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]

Taxonomic identifier

272558 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	312 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 – 312	312	3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1 HAMAP MF_01815		PRO_0000110397
Regions
	Region	238 – 242	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	237	1	By similarity
	Active site	267	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K8W9 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: D31A238A1EE5A864	FASTA	312	33,626
	10 20 30 40 50 60 MTRAGILGIG SYVGEHVVTN KDFEKRIDTS DEWIRTRTGI EERRFAPDNV DTSDMAYEAS 70 80 90 100 110 120 VKALKAAGVS AEEIDLILVA TVTPDMPFPT VSTLVQQRLG AKKAAAMDIS AACAGFIYGL 130 140 150 160 170 180 ATGQQFIENG GYKHVLVIGV EKLSKITDMT DRNTAVLFGD GAGAAVMGAV SEDRGILAYE 190 200 210 220 230 240 LGADGEGAMH INQKGEYIQM NGREVFKFAV RQMGESALSV LEKAGLSKED VDFLIPHQAN 250 260 270 280 290 300 IRIMEASRER LELPVEKMST TVKKYGNTSS ASIPMAMVDE LKDGKIKDGD LLVLVGFGAG 310 LVWGSLALRW GR

References

[1]

"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000004 Genomic DNA. Translation: BAB06602.1.
PIR	C84010.
RefSeq	NP_243749.1. NC_002570.2.
3D structure databases
ProteinModelPortal	Q9K8W9.
SMR	Q9K8W9. Positions 4-311.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000051028; EBBACP00000049667; EBBACG00000051019.
GeneID	893128.
GenomeReviews	Gene locus BH2883 in contig BA000004_GR.
KEGG	bha:BH2883.
NMPDR	fig|272558.1.peg.2883.
PATRIC	18943000. VBIBacHal18977_3001.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000001269.
HOGENOM	HBG649927.
OMA	TIWGSDG.
PhylomeDB	Q9K8W9.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	BHAL272558:BH2883-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

FABH1_BACHD

Accession

Primary (citable) accession number: Q9K8W9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program