Q5GS22 (FABH_WOLTR) 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:	Wbm0614

Organism

Wolbachia sp. subsp. Brugia malayi (strain TRS) [Complete proteome] [HAMAP]

Taxonomic identifier

292805 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Wolbachieae › Wolbachia

Protein attributes

Sequence length	326 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 – 326	326	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000056442
Regions
	Region	254 – 258	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	253	1	By similarity
	Active site	283	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5GS22 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: 6A3537E1BE6AD9F9	FASTA	326	35,397
	10 20 30 40 50 60 MNKSFILSTG SYLPKKKLGN DEIALMVETS DEWIRQRTGI TQRYIADEAE LTSDLAVNSA 70 80 90 100 110 120 KNAIEKAQIS VDEIGLIIVA TTTPDKTLPS CATIAQNKLK CKNAFSFDVQ AACSGFIYAV 130 140 150 160 170 180 TIADSLIKSN DRIKYALVIG AEIMSRIVDW KDRSTCVLFG DGAGAVIMKS TAHCNEMTEN 190 200 210 220 230 240 STRGIISTNL YSDGNVDVLC TKGGISSTGD SGKIYMNGRE VFKHAVDKLT ASIEETLRCN 250 260 270 280 290 300 NLKITDIDWL VPHQANIRII EAVVKKLNFL MEKVINTVDQ HANTSAASIP LALDYAIQKP 310 320 KIKPGSLGIL VAIGAGLTWG SVLLRY

References

[1]

"The Wolbachia genome of Brugia malayi: endosymbiont evolution within a human pathogenic nematode." Foster J., Ganatra M., Kamal I., Ware J., Makarova K., Ivanova N., Bhattacharyya A., Kapatral V., Kumar S., Posfai J., Vincze T., Ingram J., Moran L., Lapidus A., Omelchenko M., Kyrpides N., Ghedin E., Wang S. , Goltsman E., Joukov V., Ostrovskaya O., Tsukerman K., Mazur M., Comb D., Koonin E., Slatko B. PLoS Biol. 3:599-614(2005) [PubMed: 15780005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TRS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017321 Genomic DNA. Translation: AAW71202.1.
RefSeq	YP_198444.1. NC_006833.1.
3D structure databases
HSSP	HSSP built from PDB template 1HNK based on UniProtKB P0A6R0.
ProteinModelPortal	Q5GS22.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5GS22.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBWOLT00000002912; EBWOLP00000002607; EBWOLG00000002912.
GeneID	3266384.
GenomeReviews	Gene locus Wbm0614 in contig AE017321_GR.
KEGG	wbm:Wbm0614.
PATRIC	24033271. VBIWolEnd7741_0999.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
GeneTree	EBGT00050000031462.
HOGENOM	HBG649927.
OMA	DAYIRGG.
PhylomeDB	Q5GS22.
ProtClustDB	CLSK739999.
Enzyme and pathway databases
BioCyc	WPIP80849:WBM0614-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_WOLTR

Accession

Primary (citable) accession number: Q5GS22

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 1, 2005
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program