Q7N384 (FABH_PHOLL) 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:	plu2835

Organism

Photorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]

Taxonomic identifier

243265 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus

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: 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 – 317	317	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110450
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)
	Q7N384 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: DD0C81AADE0F6A27	FASTA	317	34,211
	10 20 30 40 50 60 MYTKILGTGS YLPAQVRTNA DLEKMVDTSD EWIVTRTGVR ERRLATDDET VAVMGFRAAK 70 80 90 100 110 120 KAIEMSGIDK EQIDLIIVAT ASSTHAFPSS ACQIQHMLGT QNSAAFDISA ACSGFVYALS 130 140 150 160 170 180 IADKFIKTGV AKHALVIGSD SITRTLDPED RGTLVLFGDG AGAMVVGASD EPGILSTHLH 190 200 210 220 230 240 ANGSYGELLV LPYQERQNLK EPAYASMIGN EVFKIAVREL ANIVDETLEA NNLPYSELDW 250 260 270 280 290 300 LVPHQANLRI IAATAKKLNM TMDKVVVTLD RYGNTSAASV PTAFDEAVRD GRIKRGQLIL 310 IEAFGGGLTW GSALIRF

References

[1]

"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens." Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K. , Siguier P., Vincent R., Wingate V., Zouine M., Glaser P., Boemare N., Danchin A., Kunst F. Nat. Biotechnol. 21:1307-1313(2003) [PubMed: 14528314] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TT01.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571868 Genomic DNA. Translation: CAE15209.1.
RefSeq	NP_930069.1. NC_005126.1.
3D structure databases
ProteinModelPortal	Q7N384.
SMR	Q7N384. Positions 1-317.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2802843.
GenomeReviews	Gene locus plu2835 in contig BX470251_GR.
KEGG	plu:plu2835.
NMPDR	fig|243265.1.peg.2693.
PATRIC	20509965. VBIPhoLum48522_3222.
Organism-specific databases
GenoList	plu2835.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG649927.
OMA	RILNFLA.
PhylomeDB	Q7N384.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	PLUM243265:PLU2835-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_PHOLL

Accession

Primary (citable) accession number: Q7N384

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	December 15, 2003
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program