P59813 (FABH_HELHP) 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:	HH_0681

Organism

Helicobacter hepaticus (strain ATCC 51449 / 3B1) [Complete proteome] [HAMAP]

Taxonomic identifier

235279 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	332 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: 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 – 332	332	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_0000110433
Regions
	Region	256 – 260	5	ACP-binding By similarity
Sites
	Active site	116	1	By similarity
	Active site	255	1	By similarity
	Active site	285	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P59813 [UniParc]. Last modified August 15, 2003. Version 1. Checksum: 6C9F97E930998428	FASTA	332	35,943
	10 20 30 40 50 60 MGKIYASLKS IASYIPPTCI SNVDFEKTLD TNDEWITKRT GIKTRYFALP SQQTSDLAYE 70 80 90 100 110 120 AGKKAIERAG IEPKDIDAVI VATLSPDYLT MPSTACITSF KLGIENKAAF DISAACSGFV 130 140 150 160 170 180 YLLSLAKSFI ESGTYKQILI IGAEKTSSVL DFSDRSTCVL FGDGAGACVI GSTNDEKAAI 190 200 210 220 230 240 LGVNVSANGR YQDFLCTPRV HATFGATQAQ EKQSFIQMKG NETFKVAVKT LVSEVKEILN 250 260 270 280 290 300 THHINPQDVS FFIPHQANLR IINAVGENLN FTPEQIVVSI QKYGNTSAAS IPMAMNDLYE 310 320 330 EKKLKYGDLM LLDALGGGLT WGSALVHFGG TN

References

[1]

"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus." Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B. , Shen Z., Weber J., Frosch M., Fox J.G. Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed: 12810954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017125 Genomic DNA. Translation: AAP77278.1.
RefSeq	NP_860212.1. NC_004917.1.
3D structure databases
ProteinModelPortal	P59813.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1493735.
GenomeReviews	Gene locus HH_0681 in contig AE017125_GR.
KEGG	hhe:HH0681.
NMPDR	fig|235279.1.peg.681.
PATRIC	20588816. VBIHelHep90276_0682.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG649927.
OMA	RADETIF.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	HHEP235279:HH_0681-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_HELHP

Accession

Primary (citable) accession number: P59813

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	August 15, 2003
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program