Q1J198 (FABH_DEIGD) 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:	Dgeo_0433

Organism

Deinococcus geothermalis (strain DSM 11300) [Complete proteome] [HAMAP]

Taxonomic identifier

319795 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	346 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 – 346	346	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000187862
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)
	Q1J198 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 79850BC0D014325F	FASTA	346	36,203
	10 20 30 40 50 60 MTTPSGSRPS IGITALGTYV PPRVVTNKDF EAHMDTSDEW IVSRTGIRER RFAAENEFTS 70 80 90 100 110 120 DLGVRAVQDL LARDPDGLRD VDVVICATAT PDALFPSTAA LIAGQVGLSG AGAFDLSTAC 130 140 150 160 170 180 SGFVYALSMA QGLILGGTAR RVLVVGAETL SRLVDQHDRS TAILFGDGAG AAVVGPVPQG 190 200 210 220 230 240 HGFQEFVLGA DSAGGPSLYA RCMADRLPGG ILMGERVGMN GREVFKFAVR VLGDSGQQVL 250 260 270 280 290 300 DKSGLTSADV DWVIPHQANI RIIEAANERF GVPMSKTVVN IDRYGNTSSA SLPLALREAV 310 320 330 340 DDGRIQDGQQ LLLVAFGGGL SWGACTVKWW AGAPSLTAAQ QAEVTA

References

[1]

"Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 11300.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000359 Genomic DNA. Translation: ABF44736.1.
RefSeq	YP_603905.1. NC_008025.1.
3D structure databases
ProteinModelPortal	Q1J198.
SMR	Q1J198. Positions 12-329.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1J198.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4057169.
GenomeReviews	Gene locus Dgeo_0433 in contig CP000359_GR.
KEGG	dge:Dgeo_0433.
NMPDR	fig|68909.1.peg.280.
PATRIC	21622695. VBIDeiGeo41128_0991.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0332.
HOGENOM	HBG649927.
OMA	HTIFMEG.
PhylomeDB	Q1J198.
ProtClustDB	PRK09352.
Enzyme and pathway databases
BioCyc	DGEO319795:DGEO_0433-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_DEIGD

Accession

Primary (citable) accession number: Q1J198

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	June 13, 2006
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program