A5VK78 (FABH_LACRD) 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:	Lreu_0991

Organism

Lactobacillus reuteri (strain DSM 20016) [Complete proteome] [HAMAP]

Taxonomic identifier

557436 [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_1000187874
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)
	A5VK78 [UniParc]. Last modified July 10, 2007. 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]

"The evolution of host specialization in the vertebrate gut symbiont Lactobacillus reuteri." Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M., Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M., Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L. , Ivanova N., Kyrpides N.C., Walter J. PLoS Genet. 7:E1001314-E1001314(2011) [PubMed: 21379339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 20016.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000705 Genomic DNA. Translation: ABQ83252.1.
RefSeq	YP_001271589.1. NC_009513.1.
3D structure databases
ProteinModelPortal	A5VK78.
ModBase	Search...
Protein-protein interaction databases
STRING	A5VK78.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5189070.
GenomeReviews	Gene locus Lreu_0991 in contig CP000705_GR.
KEGG	lre:Lreu_0991.
PATRIC	22255162. VBILacReu87937_0998.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG649927.
OMA	DYFILHQ.
ProtClustDB	CLSK845716.
Enzyme and pathway databases
BioCyc	LREU557436:LREU_0991-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_LACRD

Accession

Primary (citable) accession number: A5VK78

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	July 10, 2007
Last modified:	December 14, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program