Q1C6M8 (FABH_YERPA) 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:	YPA_1928

Organism

Yersinia pestis bv. Antiqua (strain Antiqua) [Complete proteome] [HAMAP]

Taxonomic identifier

360102 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › Yersinia pestis

Protein attributes

Sequence length	316 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-Rule MF_01815
Catalytic activity	Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP-Rule MF_01815
Pathway	Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP-Rule MF_01815
Sequence similarities	Belongs to the FabH family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
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: InterPro beta-ketoacyl-acyl-carrier-protein synthase III activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 316	316	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP-Rule MF_01815		PRO_1000056447
Regions
	Region	244 – 248	5	ACP-binding By similarity
Sites
	Active site	112	1	By similarity
	Active site	243	1	By similarity
	Active site	273	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1C6M8 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: 1BC70E25F7EFA3C8	FASTA	316	33,738
	10 20 30 40 50 60 MYTKILGTGS YLPVQVRSNA DLEKMVDTSD EWIVTRTGIR ERRIAGLDET VATMGFQAAE 70 80 90 100 110 120 KALEMAGIDK DDIGLIIVAT TSSSHAFPSS ACQVQRMLGI KDAASFDLAA ACAGFTYALS 130 140 150 160 170 180 VADQYVKSGA VKHAIVIGSD VLSRALDPED RGTIILFGDG AGAVVLGASE QPGIMSTHLH 190 200 210 220 230 240 ADGRYGELLA LPYPDRQQDQ PAYVTMAGNE VFKVAVTELA HIVDETLQAN NLDRTALDWL 250 260 270 280 290 300 VPHQANLRII SATAKKLGMG MDKVVITLDR HGNTSAASVP SAFDEAVRDG RIQRGQLVLL 310 EAFGGGFTWG SALVRF

References

[1]

"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen." Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L. J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Antiqua.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000308 Genomic DNA. Translation: ABG13894.1.
RefSeq	YP_651839.1. NC_008150.1.
3D structure databases
ProteinModelPortal	Q1C6M8.
SMR	Q1C6M8. Positions 1-316.
ModBase	Search...
Protein-protein interaction databases
STRING	360102.YPA_1928.
Proteomic databases
PRIDE	Q1C6M8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABG13894; ABG13894; YPA_1928.
GeneID	4121937.
KEGG	ypa:YPA_1928.
PATRIC	18583260. VBIYerPes1796_2446.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HOG000246674.
KO	K00648.
OMA	AHIVEET.
ProtClustDB	PRK09352.
Enzyme and pathway databases
UniPathway	UPA00094.
Family and domain databases
Gene3D	3.40.47.10. 2 hits.
HAMAP	MF_01815. FabH.
InterPro	IPR013751. ACP_syn_III. IPR013747. ACP_syn_III_C. IPR004655. FabH_synth. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
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_YERPA

Accession

Primary (citable) accession number: Q1C6M8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 11, 2006
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program