Reviewed, UniProtKB/Swiss-Prot Q8KAP2 (FABH_CHLTE)

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:	CT2114

Organism

Chlorobium tepidum [Complete proteome] [HAMAP]

Taxonomic identifier

1097 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length	329 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 – 329	329	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110415
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)
	Q8KAP2-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 1D81E016AF798ACC	FASTA	329	36,140
	10 20 30 40 50 60 MKAAITTTAK YLPEEIMSNQ DLERILDTND EWITTRTGIK ERRILRDPKK ATSYMCTEVA 70 80 90 100 110 120 RQLLEKRGIS ADEIDLIIVA TMSPDMLFPS TACLVQGNIQ AKNAWGFDLS AACSGFVYGL 130 140 150 160 170 180 YTGAQFIESG NCKKVMVIGA DKMSSILDYE DRTTAILFGD GAGGVILEAA NEEGYGVLDA 190 200 210 220 230 240 RLYSDGLNGR EHLLMPGGGS LHPASHETVD QHMHFIQQDG KQVFKAAVIA MADVAEEIMQ 250 260 270 280 290 300 RNNLTAETID WLVPHQANQR IIHATAERMG ITEEKVMMNI ARYGNTTAGT VPICLAELDE 310 320 QGKLHKGSNL VLVSFGAGYT WGGVYVRWQ

References

[1]

"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE006470 Genomic DNA. Translation: AAM73330.1.
RefSeq	NP_662988.1.
3D structure databases
HSSP	HSSP built from PDB template 1HNK based on UniProtKB P24249.
ModBase	Search...
Genome annotation databases
GeneID	1007447.
GenomeReviews	Gene locus CT2114 in contig AE006470_GR.
KEGG	cte:CT2114.
NMPDR	fig|194439.1.peg.2082.
TIGR	CT2114.
Phylogenomic databases
HOGENOM	Q8KAP2.
OMA	YIVPHQA.
Enzyme and pathway databases
BioCyc	CTEP194439:CT_2114-MON.
BRENDA	2.3.1.180. 189605.
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. 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_CHLTE

Accession

Primary (citable) accession number: Q8KAP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	October 1, 2002
Last modified:	November 3, 2009
This is version 47 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)