C1D0N4 (FABH_DEIDV) 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:	Deide_05700

Organism

Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]

Taxonomic identifier

546414 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	350 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 By similarity 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 – 350	350	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000215997
Regions
	Region	257 – 261	5	ACP-binding By similarity
Sites
	Active site	120	1	By similarity
	Active site	256	1	By similarity
	Active site	286	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	C1D0N4 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: DF1EAE4E05400F47	FASTA	350	36,840
	10 20 30 40 50 60 MTAPSASRLS LGIVALGAYT PERIVRNEDF EARMDTNAAW IESRTGIRER RFAAEHEYTS 70 80 90 100 110 120 DMGVRAVQDM LRRDPQALTD VDAIICATVS PDALMPSTAA LIGMQVGLVG AAAFDLSTAC 130 140 150 160 170 180 SGFVYGLSVA SGLIHAGTAR RVLVVGAEVL SKIVDQDDRG TAILFGDGAG AAVVGPVPEG 190 200 210 220 230 240 YGFQDFVLGA DGNGGSSLYM RSVAKQLPGG FAMGDFTGMN GREVFKFAVR VLGDSGTQAL 250 260 270 280 290 300 EKSGLTTADV DWVIPHQANV RIIEAAMERF GLPMSKTIIN LDRYGNTSSA TVPLVLREGL 310 320 330 340 350 DDGRIRDGQQ LLLIAFGGGL SWVAGTMKWW GGAPSLQPDR AAEHSAGVQG

References

[1]

"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti." de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J. PLoS Genet. 5:E1000434-E1000434(2009) [PubMed: 19370165] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001114 Genomic DNA. Translation: ACO45408.1.
RefSeq	YP_002785162.1. NC_012526.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	C1D0N4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7738070.
GenomeReviews	Gene locus Deide_05700 in contig CP001114_GR.
KEGG	ddr:Deide_05700.
PATRIC	21614690. VBIDeiDes121019_0641.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	HTIFMEG.
ProtClustDB	PRK09352.
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_DEIDV

Accession

Primary (citable) accession number: C1D0N4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	May 26, 2009
Last modified:	January 25, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program