ID G3BDA1_CANTC Unreviewed; 737 AA.
AC G3BDA1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN ORFNames=CANTEDRAFT_110734 {ECO:0000313|EMBL:EGV60279.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV60279.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR EMBL; GL996528; EGV60279.1; -; Genomic_DNA.
DR RefSeq; XP_006689493.1; XM_006689430.1.
DR AlphaFoldDB; G3BDA1; -.
DR STRING; 590646.G3BDA1; -.
DR GeneID; 18246218; -.
DR KEGG; cten:CANTEDRAFT_110734; -.
DR eggNOG; KOG3719; Eukaryota.
DR HOGENOM; CLU_013513_4_0_1; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000000707; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR22589:SF29; MITOCHONDRIAL CARNITINE O-ACETYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 12..636
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 323
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 737 AA; 83588 MW; 6192004137E5FB0C CRC64;
MTYQYQDQLQ KLPIPDLHQT CTNYLRVLKP LQTEKEYEKT MEAVAKFLKS GTGKYLDEQL
REYSKNRNSY IEQFWYDSYL NYDSPVVLNL NPFFLLEDDP FNNESNSINP QVKRAASLTL
SSLKFIRALK NETLPPDRLK NDQVLDMYQY SKLFGSARIP TDEGCVMQSD QNSNHIVVLS
KSQFYWFDVL NGNNDLILSE SDLIINFNSI IKDSLDTNAD AVAKSSFGIL TTENRRVWAK
LRNTNLSNNS SNREILSIID SALFILCLDD IKLYDLSDLA KNMLCGLSIL DRGVQVGTCT
NRWYDKLQII ITQNGKAGIN FEHTGVDGHT VLRFVSDIYT DSILSFAHQI NANSPNLWGD
EGKKASIDNS ENLITIPRKL EWDLTPDLSL ALRFAETRLS DLINQNEFKH LEFKNYGSST
IKNMKFSPDA FIQMAFQATY YALYGKVECT YEPAMTKQFL HGRTEAIRPV SQESNLFVRK
FFDSSVPNKT KLEFLSIACQ SHSKQTRLAS NGEGVDRHLF ALFCIWKRYI EDEANEANEN
DDSNSDRTLG NEIQFTGPDK SSLQEIPSLF ADSGWDKLNN TILSTSNCGN PSLRLFGFGP
VSANGFGIGY IIKDDSVSIC ASSKHRQTSR FLATLESYLN EIYRIFKEVN SPTNEFLSSP
VETKHTHSPA STPIYIENPK PAAYNGLSNL LGGYGYFDMG DDDIKSRGPS PEPPFLNRHN
SGFSIKEIGK KLRLSEY
//
