Reviewed, UniProtKB/Swiss-Prot Q9ZMN0 (FABH_HELPJ)

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:	jhp_0188

Organism

Helicobacter pylori J99 (Campylobacter pylori J99) [Complete proteome] [HAMAP]

Taxonomic identifier

85963 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	331 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 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 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 – 331	331	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110435
Regions
	Region	256 – 260	5	ACP-binding By similarity
Sites
	Active site	115	1	By similarity
	Active site	255	1	By similarity
	Active site	285	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZMN0-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: DBD1D3259405B279	FASTA	331	36,576
	10 20 30 40 50 60 MEFYASLKSI AMHVPSERVK NAEFQQFLDT SDEWIEKRTG IKERRFANDE EKSSDLGVIA 70 80 90 100 110 120 AKQAIERAHL TPQDIDLVVV ATLSPDFLAM PSTACVLSAK LGIENKPAFD ISAACTGFIY 130 140 150 160 170 180 LLSVAKAYVE SGMYENVLIV GAEKTSSVLD FKDRGTCILF GDGAGACVIG RTKRLKESVL 190 200 210 220 230 240 DVQISANGNF SNYLYTPRTL KPTPFNAKEE ALEPFLRMKG NEVFKLAVKT LLKDVETILE 250 260 270 280 290 300 KNALKPEDVR LFIPHQANFR IIQAVREHLD FKDEQVVLTV HKYGNTSAAS IPMAMCEAYE 310 320 330 EGRLKKGDLM LLDAFGGGLT WGSALVYFGG I

References

[1]

"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J. Nature 397:176-180(1999) [PubMed: 9923682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001439 Genomic DNA. Translation: AAD05771.1.
PIR	C71962.
RefSeq	NP_222909.1.
3D structure databases
SMR	Q9ZMN0. Positions 6-328.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9ZMN0.
Genome annotation databases
GeneID	889248.
GenomeReviews	Gene locus jhp_0188 in contig AE001439_GR.
KEGG	hpj:jhp0188.
NMPDR	fig|85963.1.peg.187.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	CEAYEEG.
Enzyme and pathway databases
BioCyc	HPYL85963:JHP0188-MONOMER.
BRENDA	2.3.1.180. 295085.
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. [Graphical view]
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_HELPJ

Accession

Primary (citable) accession number: Q9ZMN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	February 9, 2010
This is version 61 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)