Reviewed, UniProtKB/Swiss-Prot A5F464 (FADA_VIBC3)

Names and origin

Protein names

Recommended name:
    3-ketoacyl-CoA thiolase
    EC=2.3.1.16
Alternative name(s):
    Fatty acid oxidation complex subunit beta
    Beta-ketothiolase
    Acetyl-CoA acyltransferase

Gene names

Name:	fadA
Ordered Locus Names:	VC0395_A2533

Organism

Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [Complete proteome] [HAMAP]

Taxonomic identifier

345073 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: HAMAP lipid catabolic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: HAMAP
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_0000323556
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)
	A5F464-1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: A02AD9651DDC94CD	FASTA	387	40,828
	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 ALKRAGLTMQ 310 320 330 340 350 360 DMDVVELNEA FAAQSLPCAK DLGLLDMMDD KVNLNGGAIA LGHPLGCSGT RISTTLINLM 370 380 EAKDAKYGLA TMCIGLGQGI ATIFERP

References

[1]	Heidelberg J. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000627 Genomic DNA. Translation: ABQ20531.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A5F464.
Genome annotation databases
GenomeReviews	Gene locus VC0395_A2533 in contig CP000627_GR.
KEGG	vco:VC0395_A2533.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	AIDDIYW.
Family and domain databases
HAMAP	MF_01620. [Tree]
InterPro	IPR012805. FadA. IPR002155. Thiolase. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
PANTHER	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.
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_VIBC3

Accession

Primary (citable) accession number: A5F464

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	June 12, 2007
Last modified:	November 3, 2009
This is version 23 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)