Q0STU9 (FABH_CLOPS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3
EC=2.3.1.41

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:	CPR_1136

Organism

Clostridium perfringens (strain SM101 / Type A) [Complete proteome] [HAMAP]

Taxonomic identifier

289380 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	324 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	Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 324	324	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000056349
Regions
	Region	252 – 256	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	251	1	By similarity
	Active site	281	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0STU9 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 8AB1D759214FB4B6	FASTA	324	35,265
	10 20 30 40 50 60 MENAKIIGFG LYTPKNLVEN ERLQEFLETS DEWIRSRTGI ERRYISLDEN TSDLAVEASK 70 80 90 100 110 120 KALNQAGLSA EEIDLIIVAT VTPDNFTPST ACIVQDKLGA KNAWAFDINA ACTGFIYALK 130 140 150 160 170 180 LGRSLIRSGE AKNALIIGAE TLSKALNWED RGSCVLFGDG AGAIVLTSTE EDCGIKCVNV 190 200 210 220 230 240 KSDGSKGDSL VIQGLPLNSP FKDGREVSKN YINMNGREIF KFATKVMEES IVEILEKENI 250 260 270 280 290 300 KIEDISAIIP HQANLRIIDY VVKRLGIPRE KFVTNLQNYG NTSGASIPIA LCESINEGNL 310 320 KKGDNIIMVG FGGGLTWGAA LIKL

References

[1]

"Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens." Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Khouri H. , Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B., Paulsen I.T. Genome Res. 16:1031-1040(2006) [PubMed: 16825665] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SM101 / Type A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000312 Genomic DNA. Translation: ABG86514.1.
RefSeq	YP_698458.1. NC_008262.1.
3D structure databases
ProteinModelPortal	Q0STU9.
SMR	Q0STU9. Positions 3-323.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0STU9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4205520.
GenomeReviews	Gene locus CPR_1136 in contig CP000312_GR.
KEGG	cpr:CPR_1136.
PATRIC	19490563. VBICloPer122123_1112.
TIGR	CPR_1136.
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	KEIGAIN.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	CPER289380:CPR_1136-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

FABH_CLOPS

Accession

Primary (citable) accession number: Q0STU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program