Reviewed, UniProtKB/Swiss-Prot A5EXD7 (FABH_DICNV)

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:	DNO_1207

Organism

Dichelobacter nodosus (strain VCS1703A) [Complete proteome] [HAMAP]

Taxonomic identifier

246195 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Cardiobacteriales › Cardiobacteriaceae › Dichelobacter

Protein attributes

Sequence length	322 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 – 322	322	3-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815		PRO_1000088310
Regions
	Region	250 – 254	5	ACP-binding By similarity
Sites
	Active site	113	1	By similarity
	Active site	249	1	By similarity
	Active site	279	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5EXD7-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 40D7BE253FA614D7	FASTA	322	35,048
	10 20 30 40 50 60 MMYSKIIGTG GYLPSRIVSN DELSQSMQTS DEWIYSRTGI RQRHLASPDE SCSDMAFYAA 70 80 90 100 110 120 KRALENAHIE ADAIDLIIVA TSTPEHIFPS TATVVQSRLS CQRAAAFDVQ AACTGFMYAL 130 140 150 160 170 180 NTADCFIKSG QYQNVLVIGA EVFSRIVDWQ DRNTAVLFGD GAGAVVLSAS EEAGILGTIL 190 200 210 220 230 240 HADGSHKELL WVPQGIGSSE TDFATRRPFI EMQGREVFKF AVRSLTHLVS ELLVQCQMSA 250 260 270 280 290 300 DEIDFLIPHQ ANSRIIQAVA EHLNLPIEKV IITVNQHANT SAASVPLALD YGVQNGIIKR 310 320 GDNLLLEAFG GGFTWGGCIL TY

References

[1]

"Genome sequence and identification of candidate vaccine antigens from the animal pathogen Dichelobacter nodosus." Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T., Fedorova N. , Khouri H., Bottomley S.P., Whittington R.J., Adler B., Songer J.G., Rood J.I., Paulsen I.T. Nat. Biotechnol. 25:569-575(2007) [PubMed: 17468768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000513 Genomic DNA. Translation: ABQ13902.1.
RefSeq	YP_001210090.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A5EXD7.
Genome annotation databases
GeneID	5122835.
GenomeReviews	Gene locus DNO_1207 in contig CP000513_GR.
KEGG	dno:DNO_1207.
TIGR	DNO_1207.
Phylogenomic databases
OMA	CEAYEEG.
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

FABH_DICNV

Accession

Primary (citable) accession number: A5EXD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	June 12, 2007
Last modified:	November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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