Reviewed, UniProtKB/Swiss-Prot Q71XG3 (FABH_LISMF)

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:	LMOf2365_2235

Organism

Listeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP]

Taxonomic identifier

265669 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.
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 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 – 312	312	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110440
Regions
	Region	238 – 242	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	237	1	By similarity
	Active site	267	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q71XG3-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: E87AE337231DE3DD	FASTA	312	33,971
	10 20 30 40 50 60 MNAGILGVGK YVPEKIVTNF DLEKIMDTSD EWIRTRTGIE ERRIARDDEY THDLAYEAAK 70 80 90 100 110 120 VAIKNAGLTP DDIDLFIVAT VTQEATFPSV ANIIQDRLGA KNAAGMDVEA ACAGFTFGVV 130 140 150 160 170 180 TAAQFIKTGA YKNIVVVGAD KLSKITNWDD RTTAVLFGDG AGAVVMGPVS DDHGLLSFDL 190 200 210 220 230 240 GSDGSGGKYL NLDENKKIYM NGREVFRFAV RQMGEASLRV LERAGLEKED LDLLIPHQAN 250 260 270 280 290 300 IRIMEASRER LNLPEEKLMK TVHKYGNTSS SSIALALVDA VEEGRIKDND NVLLVGFGGG 310 LTWGALIIRW GK

References

[1]

"Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species." Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. , Durkin A.S., Madupu R., Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., Luchansky J.B., Fraser C.M. Nucleic Acids Res. 32:2386-2395(2004) [PubMed: 15115801] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017262 Genomic DNA. Translation: AAT05002.1.
RefSeq	YP_014825.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q71XG3.
Genome annotation databases
GeneID	2798995.
GenomeReviews	Gene locus LMOf2365_2235 in contig AE017262_GR.
KEGG	lmf:LMOf2365_2235.
TIGR	LMOf2365_2235.
Phylogenomic databases
HOGENOM	Q71XG3.
OMA	YIVPHQA.
Enzyme and pathway databases
BioCyc	LMON265669:LMOF2365_2235-MON.
Family and domain databases
HAMAP	MF_01815. [Tree]
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. 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_LISMF

Accession

Primary (citable) accession number: Q71XG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 37 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)