A4SCL4 (FABH_PROVI) 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:	Cvib_0200

Organism

Prosthecochloris vibrioformis (strain DSM 265) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 265)) (Chlorobium phaeovibrioides (strain DSM 265)) [Complete proteome] [HAMAP]

Taxonomic identifier

290318 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Chlorobium

Protein attributes

Sequence length	329 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 – 329	329	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000088318
Regions
	Region	256 – 260	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	255	1	By similarity
	Active site	285	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4SCL4 [UniParc]. Last modified May 15, 2007. Version 1. Checksum: 08B5798AA5E42075	FASTA	329	35,708
	10 20 30 40 50 60 MNAAITATAK YLPDGILSNL DLERMLDTND EWIRTRTGIS ERRILRDPEK ATSYICGEVA 70 80 90 100 110 120 RQLLEKRGMK AEELDLIIVA TMTPDMLFPS TACLVQDIIG AGNAWAFDLN AACSGFLFAL 130 140 150 160 170 180 NTGSRFIESG AHKKVMVIGA DKMSSVIDYT DRSTAILFGD GGGGVILEPA TTEGCGVLDN 190 200 210 220 230 240 RMYCDGTSGK DHLLMKGGGS LHPATHQTVD DHLHYIYQDG RMVFKSAVTS MANVAVEIME 250 260 270 280 290 300 RNGLTAENVS WLVPHQANQR IISATAERMG ISSDKFISNV ARYGNTTAGT IPICLAELDE 310 320 ENKLHPGSNL VLCSFGAGYT WGGVYVKWQ

References

[1]

"Complete sequence of Prosthecochloris vibrioformis DSM 265." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 265.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000607 Genomic DNA. Translation: ABP36223.1.
RefSeq	YP_001129725.1. NC_009337.1.
3D structure databases
ProteinModelPortal	A4SCL4.
ModBase	Search...
Protein-protein interaction databases
STRING	A4SCL4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4970165.
GenomeReviews	Gene locus Cvib_0200 in contig CP000607_GR.
KEGG	pvi:Cvib_0200.
PATRIC	21394724. VBIChlPha132153_0218.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	TSHEWIS.
PhylomeDB	A4SCL4.
ProtClustDB	PRK09352.
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_PROVI

Accession

Primary (citable) accession number: A4SCL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 15, 2007
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program