Reviewed, UniProtKB/Swiss-Prot Q87N20 (FABH1_VIBPA)

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:	VP2056

Organism

Vibrio parahaemolyticus [Complete proteome] [HAMAP]

Taxonomic identifier

670 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.
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: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: HAMAP 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 – 316	316	3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1 HAMAP MF_01815		PRO_0000110504
Regions
	Region	244 – 248	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	243	1	By similarity
	Active site	273	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q87N20-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 6621A043A1817BAF	FASTA	316	33,797
	10 20 30 40 50 60 MYSKILGTGS YLPSQVRTNA DLEKMVDTSD EWIVARTGIK ERRIAAEDET VADMAFYAAE 70 80 90 100 110 120 NAIDMAGIDK NDIDLIIVAT TSSSHTFPSS ACQVQAKLGI KGCPAFDLAA ACSGFVYALS 130 140 150 160 170 180 VADQHIKSGM CKNVLVIGAD ALSKTCDPTD RSTIILFGDG AGAVVVGASQ EPGIISTHIY 190 200 210 220 230 240 ADGQFGDLLS LPVPERGKDV DKWLHMAGNE VFKVAVTQLS KLVKDTLEAN DMHKSELDWL 250 260 270 280 290 300 VPHQANYRII SATAKKLSMS LDQVVVTLDR HGNTSAATVP TALDEAVRDG RIKRGQTLLL 310 EAFGGGFTWG SALVKF

References

[1]

"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633 / Serotype O3:K6.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000031 Genomic DNA. Translation: BAC60319.1.
RefSeq	NP_798435.1.
3D structure databases
HSSP	HSSP built from PDB template 1HNK based on UniProtKB P24249.
SMR	Q87N20. Positions 1-316.
ModBase	Search...
Genome annotation databases
GeneID	1189567.
GenomeReviews	Gene locus VP2056 in contig BA000031_GR.
KEGG	vpa:VP2056.
NMPDR	fig|223926.1.peg.2056.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q87N20.
OMA	FRIIKAT.
Enzyme and pathway databases
BioCyc	VPAR223926:VP2056-MON.
BRENDA	2.3.1.180. 3063.
Family and domain databases
HAMAP	MF_01815. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
Pfam	PF08545. ACP_syn_III. 1 hit. PF08541. ACP_syn_III_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00747. fabH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FABH1_VIBPA

Accession

Primary (citable) accession number: Q87N20

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)