Reviewed, UniProtKB/Swiss-Prot A4YW84 (FABH_BRASO)

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:	BRADO4417

Organism

Bradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP]

Taxonomic identifier

114615 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

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: 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
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_1000056331
Regions
	Region	252 – 256	5	ACP-binding By similarity
Sites
	Active site	114	1	By similarity
	Active site	251	1	By similarity
	Active site	281	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4YW84-1 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: EEEB229F6A48C7E7	FASTA	324	34,471
	10 20 30 40 50 60 MTIRSVVLGC GSYLPQRVVT NAELASRIET SDEWIVQRTG IRERHVAADG EFTSHLAINA 70 80 90 100 110 120 ARAALANADV DPQSIDLIVL GTSTPDNTFP ATAVAVQNGL GIHHGAAFDL QAVCSGFVYA 130 140 150 160 170 180 LATADNFLRS GSFKRALVIG AETFSRILDW NDRTTCVLFG DGAGALVLDA QQQGGTAADR 190 200 210 220 230 240 GVLSTHLRSD GRHKAKLYVD GGPSSTQTVG HLRMEGREVF KHAVGMITDV IVDAFEATGL 250 260 270 280 290 300 SAETIDWFVP HQANKRIIDA SAHKLHIAPE KVVLTVDRHG NTSAASIPLA LDVAVKDGRI 310 320 KKGDVVLLEA MGGGFTWGSA LVRW

References

[1]

"Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia." Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C., Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z. , Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A., Medigue C., Sadowsky M. Science 316:1307-1312(2007) [PubMed: 17540897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU234118 Genomic DNA. Translation: CAL78160.1.
RefSeq	YP_001206381.1.
3D structure databases
SMR	A4YW84. Positions 5-324.
ModBase	Search...
Protein-protein interaction databases
STRING	A4YW84.
Genome annotation databases
GeneID	5119232.
GenomeReviews	Gene locus BRADO4417 in contig CU234118_GR.
KEGG	bra:BRADO4417.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	TSADRGI.
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.
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_BRASO

Accession

Primary (citable) accession number: A4YW84

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 29, 2007
Last modified:	February 9, 2010
This is version 21 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)