Q9KNI0 (FADA_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-ketoacyl-CoA thiolase
EC=2.3.1.16

Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Fatty acid oxidation complex subunit beta

Gene names

Name:	fadA
Ordered Locus Names:	VC_2759

Organism

Vibrio cholerae

Taxonomic identifier

666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed By similarity. HAMAP MF_01620
Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. HAMAP MF_01620
Pathway	Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01620
Subunit structure	Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity.
Subcellular location	Cytoplasm By similarity HAMAP MF_01620.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase 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 – 387	387	3-ketoacyl-CoA thiolase HAMAP MF_01620		PRO_0000206395
Sites
	Active site	91	1	Acyl-thioester intermediate By similarity
	Active site	343	1	Proton acceptor By similarity
	Active site	373	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KNI0 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B5242291B63D8E77	FASTA	387	40,842
	10 20 30 40 50 60 MNTVVIVDCL RTPMGRSKGG AFRHQRAEDL SAHLMKGILA RNPQVNPKEI EDIYWGCVQQ 70 80 90 100 110 120 TLEQGFNVAR NAALLAGLPI EIGAVTVNRL CGSSMQALHD AARAIMVGDA EICLVGGVEH 130 140 150 160 170 180 MGHVPMTHGV DFHPGLSKNV AKAAGMMGLT AEMLGKLHGI SRQQQDEFAA RSHARAHAAT 190 200 210 220 230 240 LEGRFKNEIL PTEGHAADGT LFTLDYDEVI RPETTVAGLA ELRPVFDPAN GTVTAGTSSA 250 260 270 280 290 300 LSDGASAMLV MSEQKAKALG LTIRARIKAM AVAGCDPSIM GYGPVPATHK ALQRAGLTMQ 310 320 330 340 350 360 DMDVVELNEA FAAQSLPCAK DLGLLEMMDD KVNLNGGAIA LGHPLGCSGT RISTTLINLM 370 380 EAKDAKYGLA TMCIGLGQGI ATIFERP

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed: 10952301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF95898.1.
PIR	A82036.
RefSeq	NP_232385.1. NC_002505.1.
3D structure databases
ProteinModelPortal	Q9KNI0.
SMR	Q9KNI0. Positions 4-386.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2614936.
GenomeReviews	Gene locus VC_2759 in contig AE003852_GR.
KEGG	vch:VC2759.
PATRIC	20084564. VBIVibCho83274_2634.
TIGR	VC_2759.
Phylogenomic databases
HOGENOM	HBG370930.
OMA	AIDDIYW.
PhylomeDB	Q9KNI0.
ProtClustDB	PRK08947.
Family and domain databases
HAMAP	MF_01620. FadA. [Tree]
InterPro	IPR012805. FadA. IPR002155. Thiolase. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. IPR020615. Thiolase_acyl_enz_int_AS. IPR020610. Thiolase_AS. IPR020617. Thiolase_C. IPR020613. Thiolase_CS. IPR020616. Thiolase_N. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 4 hits.
KO	K00632.
PANTHER	PTHR18919:SF35. PTHR18919:SF35. 1 hit. PTHR18919. Thiolase. 1 hit.
Pfam	PF02803. Thiolase_C. 1 hit. PF00108. Thiolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAM	SSF53901. Thiolase-like. 2 hits.
TIGRFAMs	TIGR01930. AcCoA-C-Actrans. 1 hit. TIGR02445. FadA. 1 hit.
PROSITE	PS00098. THIOLASE_1. 1 hit. PS00737. THIOLASE_2. 1 hit. PS00099. THIOLASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADA_VIBCH

Accession

Primary (citable) accession number: Q9KNI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program