Reviewed, UniProtKB/Swiss-Prot Q9RT22 (FABH2_DEIRA)

Names and origin

Protein names

Recommended name:
    3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2
    EC=2.3.1.180
Alternative name(s):
    3-oxoacyl-[acyl-carrier-protein] synthase III protein 2
    Beta-ketoacyl-ACP synthase III 2
      Short name=KAS III 2

Gene names

Name:	fabH2
Ordered Locus Names:	DR_1947

Organism

Deinococcus radiodurans [Complete proteome] [HAMAP]

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	338 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 – 338	338	3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 HAMAP MF_01815		PRO_0000110423
Regions
	Region	256 – 260	5	ACP-binding By similarity
Sites
	Active site	119	1	By similarity
	Active site	255	1	By similarity
	Active site	285	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RT22-1 [UniParc]. Last modified August 15, 2003. Version 2. Checksum: DF38A5DA32D12FF0	FASTA	338	34,926
	10 20 30 40 50 60 MTASLSAPAI GILAVGAYAP AAVITNAHYA TRLDTSDDWI TSRTGIRERR HAAPDESSSV 70 80 90 100 110 120 LGIRATQDLA GRFPGALDGV NLVICATSSP DAMFPSTAAL IAGGTGLRGA AAFDVSVACS 130 140 150 160 170 180 GFLYALSVGY GMIRAGLAKK ALIVGSEVMS GAVDQNDRNT AILFGDGAGC VVIGEVPQGY 190 200 210 220 230 240 GFQSFVLGAD SAGGPHLYLR GAALRLPEGT EMGPHLTQNG REVFKFAVRT LGDSAEQAMR 250 260 270 280 290 300 QAGKTTADID WLVPHQANIR IIEAACERFG LPIERAVTNL DRYGNTSAAS IPLALAEAQA 310 320 330 QGRFKDGDQL LLAGFGGGLS WGAAALKWWS GPTGKQSS

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000513 Genomic DNA. Translation: AAF11499.1. Different initiation.
PIR	C75334.
RefSeq	NP_295670.1.
3D structure databases
HSSP	HSSP built from PDB template 1HNK based on UniProtKB P24249.
ModBase	Search...
Genome annotation databases
GeneID	1797849.
GenomeReviews	Gene locus DR_1947 in contig AE000513_GR.
KEGG	dra:DR_1947.
NMPDR	fig|243230.1.peg.2129.
TIGR	DR_1947.
Phylogenomic databases
HOGENOM	Q9RT22.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_1947-MON.
BRENDA	2.3.1.180. 96172.
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

FABH2_DEIRA

Accession

Primary (citable) accession number: Q9RT22

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	August 15, 2003
Last modified:	June 16, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)