ID   M3HHF2_CANMX            Unreviewed;       805 AA.
AC   M3HHF2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
GN   ORFNames=G210_3013 {ECO:0000313|EMBL:EMG46727.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG46727.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG46727.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMG46727.1}.
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DR   EMBL; AOGT01001893; EMG46727.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3HHF2; -.
DR   STRING; 1245528.M3HHF2; -.
DR   eggNOG; KOG3719; Eukaryota.
DR   HOGENOM; CLU_013513_4_0_1; -.
DR   OMA; HILVMRR; -.
DR   OrthoDB; 1429709at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 1.10.275.20; Choline/Carnitine o-acyltransferase; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR042572; Carn_acyl_trans_N.
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   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          13..663
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          701..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        324
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   805 AA;  90881 MW;  9D7BF4611BB1B681 CRC64;
     MSTYSQQETL QKLPIPDLEQ TCANYLNVLK PLQTEHEHEQ TKIAVEKFLN NGTGKYLDSE
     LHQYAKGRPS YIEQFWYDAY LNYDSPVVLN LNPFFLLEDD PFTNESSAVN PQVKRATSLV
     MSSLKFIQAL KNETLSIDTL KNNKPLCMYQ YTKLFGASRI PTEEGCMMQS DPSSNHIIVM
     SKSQLYWFDV LDSENNLILS EAELNVNFQS IIHDSIHTPS EDIAKSSFGV LTTENRRIWA
     NIRKHLMKDN PTNHEVLSLI DSALFVLCFD DIVINDLSEL STNMLCGLSI LDNGIQVGTC
     TNRWYDKLQI IVTKNAKAGI NFEHTGVDGH TVLRFVSDIY TDSILSFAHS INNNAPSLWD
     ATSTTKLEDE DLITVPRKLE WELTPDLSLA LRFGETRLSD LINQNEFRHL EFRDYGSTQI
     KKMKYSPDAF VQMAFQATYY ALYGKVECTY EPAMTKQFYH GRTEAIRTVS QESNLFVRKF
     FDSTISIQKK LDYLADACNK HSAQTRMCSA GQGVDRHLYA LFCIWKRYLQ DCDTKQDDIQ
     EPQPQSQEES TELSRDDTII AQHNSHDDDD STTVVGGANH NNLNKDDDIL KQIPDIFADP
     GWDKLNNTII STSNCGNPSL RLFGFGPVSA NGFGIGYILK DDSISICASS KHRQTQRFLV
     TLNSYLLEIQ SIWKQANRME KLKQELQKSV QLGIAKGLEA QLGKKKQEEE EAAKAKAEQA
     KTADPQQGDA NGDANGTDDN NKENGGGDGE TPSHLSTLLG GYGYFDMGEE DIKSRGQSPE
     PPFLNRGNSG FSIREIGKKL RLSEY
//