B2G7L1 (FABH_LACRJ) 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:	LAR_0927

Organism

Lactobacillus reuteri (strain JCM 1112) [Complete proteome] [HAMAP]

Taxonomic identifier

557433 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

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	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 By similarity 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 – 324	324	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000187875
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)
	B2G7L1 [UniParc]. Last modified October 14, 2008. Version 1. Checksum: 0A64C2EF4D86B754	FASTA	324	34,911
	10 20 30 40 50 60 MQNLRITSTA SYHPPLNITN QQLSTIMDTS DEWIKTRTGI HQRYISNIEN TSDLALNVGN 70 80 90 100 110 120 QLLTNANLKT TELDLIIIAT MSPDAYTPST AAIVQGELGA KNAIAFDISA ACTGFIYAMN 130 140 150 160 170 180 TAELMLKSSN WQNAMVIGAE VLSKLIDWKD RSTAVLFGDG AGGVLLQKTT TATPLILGRD 190 200 210 220 230 240 LHTFGDLGDK IVAGKTTPKA GFPKQLTSLS PFAMAGRDVY RFATHEVPRS IASAVQQANL 250 260 270 280 290 300 KLDDIDYFLL HQANERIINQ IAKRLGQPIT KFPMNISEYG NTGAASEPIL LTQAVAHELV 310 320 KPGNIIAMSG FGGGLSTGTI ILNY

References

[1]

"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production." Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M. DNA Res. 15:151-161(2008) [PubMed: 18487258] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCM 1112.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007281 Genomic DNA. Translation: BAG25443.1.
RefSeq	YP_001841923.1. NC_010609.1.
3D structure databases
ProteinModelPortal	B2G7L1.
ModBase	Search...
Protein-protein interaction databases
STRING	B2G7L1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6230588.
GenomeReviews	Gene locus LAR_0927 in contig AP007281_GR.
KEGG	lrf:LAR_0927.
PATRIC	22259288. VBILacReu111271_1005.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG649927.
OMA	DYFILHQ.
ProtClustDB	CLSK845716.
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_LACRJ

Accession

Primary (citable) accession number: B2G7L1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	October 14, 2008
Last modified:	January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program