Q00614 (CACP_CANTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carnitine O-acetyltransferase, mitochondrial
Short name=Carnitine acetylase
EC=2.3.1.7

Gene names

Name:	CAT2
Synonyms:	CAT

Organism

Candida tropicalis (Yeast)

Taxonomic identifier

5482 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	627 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria By similarity.
Catalytic activity	Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.
Subcellular location	Peroxisome By similarity. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.
Sequence similarities	Belongs to the carnitine/choline acetyltransferase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane Peroxisome
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carnitine O-acetyltransferase 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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 627		Carnitine O-acetyltransferase, mitochondrial		PRO_0000004430
Regions
	Region	417 – 429	13	Coenzyme A binding By similarity
	Motif	625 – 627	3	Microbody targeting signal Potential
Sites
	Active site	336	1	Proton acceptor By similarity
	Binding site	451	1	Carnitine By similarity
	Binding site	453	1	Carnitine By similarity
	Binding site	454	1	Coenzyme A By similarity
	Binding site	464	1	Carnitine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q00614 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: B00878F37CC7D84B	FASTA	627	70,762
	10 20 30 40 50 60 MFNFKLSQQV LKNSTKSIMP ILKKPFSTSH AKGDLFKYQS QLPKLPVPTL EETASKYLKT 70 80 90 100 110 120 VEPFLNQEQL ESTKAKVAEF VRPGGAGEAL QARLNNFAAD KDNWLAEFWD DYAYMSYRDP 130 140 150 160 170 180 VVPYVSYFFS HKDVKNIIGQ DQLLKATLIA YYTIEFQEKV LDESLDPEVI KGNPFCMNAF 190 200 210 220 230 240 KYMFNNSRVP AEGSDITQHY NGEENQFFVV IYKNNFYKVP THKNGQRLTK GEIYSYLQEI 250 260 270 280 290 300 KNDATPKGLG LGALTSLNRD EWLSAYNNLL KSPINEASLG SIFASSFVIA LDSNNPVTIE 310 320 330 340 350 360 EKSKNCWHGD GQNRFFDKPL EFFVSANGNS GFLGEHSRMD ATPTVQLNNT IYKQILETNP 370 380 390 400 410 420 NDLIVEIGSS APRFGNAEIL PFDINPTTRA NIKDAIAKFD ATIAAHDEEI FQHYGYGKGL 430 440 450 460 470 480 IKKFKVSPDA YVQLLMQLAY FKYTGKIRPT YESAATRKFL KGRTETGRTV SNESKKFVET 490 500 510 520 530 540 WSDPNASSAD KVATFQAAAK QHVAYLSAAA DGKGVDRHLF GLKQMIQPGE PIPEIFTDPI 550 560 570 580 590 600 FSYSQTWYIS SSQVPSEFFQ SWGWSQVIDD GFGLAYLINN DWIHVHISCK RGNGLQSDHL 610 620 KWYLVDSANE MKDVLTKGLL TDAKPKL

References

[1]

"Peroxisomal and mitochondrial carnitine acetyltransferases of the n-alkane-assimilating yeast Candida tropicalis. Analysis of gene structure and translation products." Kawachi H., Atomi H., Ueda M., Tanaka A. Eur. J. Biochem. 238:845-852(1996) [PubMed: 8706689] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 20336 / pK233 / NCYC 997.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D84549 Genomic DNA. Translation: BAA12696.1.
PIR	S68958.
3D structure databases
ProteinModelPortal	Q00614.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000542. Carn_acyl_trans. [Graphical view]
PANTHER	PTHR22589. Carn_acyl_trans. 1 hit.
Pfam	PF00755. Carn_acyltransf. 1 hit. [Graphical view]
PROSITE	PS00439. ACYLTRANSF_C_1. 1 hit. PS00440. ACYLTRANSF_C_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CACP_CANTR

Accession

Primary (citable) accession number: Q00614

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program