A3N232 (FABH_ACTP2) 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:	APL_1384

Organism

Actinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]

Taxonomic identifier

416269 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	316 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 – 316	316	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000056320
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)
	A3N232 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 22E3C73976EDD647	FASTA	316	34,014
	10 20 30 40 50 60 MYSKILATGS YLPAQIRTNA DLEKMVDTSD EWIFTRSGMK ERRIAAADET VATMGAQAAK 70 80 90 100 110 120 NALEIANIDH NEIDLIVVGT TTNSHAYPSA ACQIQGMLDI QDAIAFDVAA ACTGFVYALS 130 140 150 160 170 180 VADQFIRSGK IKKALVIGSD LNSRALDETD RSTVVLFGDG AGAVILEASE EQGIISTHLH 190 200 210 220 230 240 SSSDTEYMLA LPAQKRGDEK SGFIQMQGNA TFKLAVGQLS SVVEETLEAN NLQKSDLDWL 250 260 270 280 290 300 VPHQANIRII AATAKKLEMD MSQVVLTVEK YGNNSAATVP VALDEAVRDG RIQRGQLLLL 310 EAFGGGWTWG SALVRF

References

[1]	"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)." Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E. J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L20.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000569 Genomic DNA. Translation: ABN74468.1.
RefSeq	YP_001054073.1. NC_009053.1.
3D structure databases
ProteinModelPortal	A3N232.
SMR	A3N232. Positions 1-316.
ModBase	Search...
Protein-protein interaction databases
STRING	A3N232.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4848572.
GenomeReviews	Gene locus APL_1384 in contig CP000569_GR.
KEGG	apl:APL_1384.
PATRIC	20747753. VBIActPle94089_1442.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	RILNFLA.
PhylomeDB	A3N232.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	APLE416269:APL_1384-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_ACTP2

Accession

Primary (citable) accession number: A3N232

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	April 3, 2007
Last modified:	December 14, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program