Q03RV2 (FABH_LACBA) 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:	LVIS_0935

Organism

Lactobacillus brevis (strain ATCC 367 / JCM 1170) [Complete proteome] [HAMAP]

Taxonomic identifier

387344 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	327 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 – 327	327	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000070234
Regions
	Region	255 – 259	5	ACP-binding By similarity
Sites
	Active site	114	1	By similarity
	Active site	254	1	By similarity
	Active site	284	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q03RV2 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 68FF630335EAD151	FASTA	327	35,281
	10 20 30 40 50 60 MKFENFNILA TAGYTPERVV PNSELTTMMT TSDEWIVQRT GIHQRHVVTA ERTSDLCTRV 70 80 90 100 110 120 AQQLLQRSGL QATDIDYIVV ATMSPDYQTP AVSAQVQGNI GATKAVALDV NAACSGFVYG 130 140 150 160 170 180 LQVVHRLLMG DSPKTALLIG GETLSRLVDW QDRSTAVLFG DGAGGVVLTS ALAQDGAFIA 190 200 210 220 230 240 ADYRTMGEQG RYLTAGANGV DSPFASDPQP VLPFFKMNGR RVYNFAIKQV PASLRRVLDQ 250 260 270 280 290 300 GHLAVTDVDY FILHQANQRI IERIAEDLTG SMAQFPVNIG QYGNTAAASE PLLLNQLVTS 310 320 HVIKRGDVLA LSGFGGGLTI GTMILRY

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 367 / JCM 1170.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000416 Genomic DNA. Translation: ABJ64070.1.
RefSeq	YP_795101.1. NC_008497.1.
3D structure databases
ProteinModelPortal	Q03RV2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q03RV2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4413824.
GenomeReviews	Gene locus LVIS_0935 in contig CP000416_GR.
KEGG	lbr:LVIS_0935.
NMPDR	fig|387344.8.peg.894.
PATRIC	22200829. VBILacBre134470_0910.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	DYFILHQ.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	LBRE387344:LVIS_0935-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_LACBA

Accession

Primary (citable) accession number: Q03RV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program