Reviewed, UniProtKB/Swiss-Prot Q6D690 (FABH_ERWCT)

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:	ECA1795

Organism

Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum) [Complete proteome] [HAMAP]

Taxonomic identifier

29471 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium

Protein attributes

Sequence length	317 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: 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 – 317	317	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110428
Regions
	Region	245 – 249	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	244	1	By similarity
	Active site	274	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6D690-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: D6B1C5619CB9F070	FASTA	317	34,015
	10 20 30 40 50 60 MYTKIIGTGS YLPEEIRTNA DLEKMVETTD EWIVTRTGIR ERRIAAPDEN VATMGYRAAQ 70 80 90 100 110 120 KALEMANVDA SEVGLLIVAT TSSSHAFPSS ACQVQQLLGI KDTIAFDLAA ACAGFTYALS 130 140 150 160 170 180 VADQYVKSGA VKYALVIGSD TLSRTLDPED RGTLILFGDG AGAVLLTTSE QPGILSTHLH 190 200 210 220 230 240 ADGRYGELLT LPHQDRNHTD KPAYLTMAGN EVFKVAVTEL AHIVEETLQA AQLDKSELDW 250 260 270 280 290 300 LVPHQANLRI ISATAKKLGM GMDKVVVTLD RHGNTSAASV PSALDEAVRD GRIKPGQLVL 310 LEAFGGGFTW GSALVRF

References

[1]

"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors." Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z. , Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K. Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004) [PubMed: 15263089] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SCRI 1043 / ATCC BAA-672.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX950851 Genomic DNA. Translation: CAG74700.1.
RefSeq	YP_049895.1.
3D structure databases
SMR	Q6D690. Positions 1-317.
ModBase	Search...
Genome annotation databases
GeneID	2883888.
GenomeReviews	Gene locus ECA1795 in contig BX950851_GR.
KEGG	eca:ECA1795.
NMPDR	fig|218491.3.peg.265.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG649927.
OMA	TSADRGI.
Enzyme and pathway databases
BioCyc	ECAR218491:ECA1795-MONOMER.
BRENDA	2.3.1.180. 281579.
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.
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

FABH_ERWCT

Accession

Primary (citable) accession number: Q6D690

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	August 16, 2004
Last modified:	February 9, 2010
This is version 41 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)