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Database: UniProt
Entry: L9KLJ3_TUPCH
LinkDB: L9KLJ3_TUPCH
Original site: L9KLJ3_TUPCH 
ID   L9KLJ3_TUPCH            Unreviewed;       636 AA.
AC   L9KLJ3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|EMBL:ELW61982.1};
GN   ORFNames=TREES_T100004296 {ECO:0000313|EMBL:ELW61982.1};
OS   Tupaia chinensis (Chinese tree shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX   NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW61982.1, ECO:0000313|Proteomes:UP000011518};
RN   [1] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang G., Fan Y., Yao Y., Huang Z.;
RT   "Genome of the Chinese tree shrew, a rising model animal genetically
RT   related to primates.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23385571; DOI=10.1038/ncomms2416;
RA   Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA   Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA   Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA   Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA   Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT   "Genome of the Chinese tree shrew.";
RL   Nat. Commun. 4:1426-1426(2013).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; KB320843; ELW61982.1; -; Genomic_DNA.
DR   AlphaFoldDB; L9KLJ3; -.
DR   STRING; 246437.L9KLJ3; -.
DR   eggNOG; KOG3717; Eukaryota.
DR   InParanoid; L9KLJ3; -.
DR   Proteomes; UP000011518; 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:SF50; CARNITINE O-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
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:UP000011518};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          35..619
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT   BINDING         429
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         433..440
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         462
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         464
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         466
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         475
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         514
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT   BINDING         565
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
SQ   SEQUENCE   636 AA;  71586 MW;  884E7FD6BFE73E44 CRC64;
     MLCCLQVKPL GFLKPSSLTK VSGRFKAHQD ALPRLPVPPL RQSLDHYLRA LRPIVSEEEW
     AHTKQLVDEF RTAGGVGDRL QKGLERRARK SENWLSDWWL KTAYLQYRQP VVIYSSPGLM
     LPKQDFVDLQ GQLRFAAKLI EGVLDFKAMI DNETLPVEYL GGKPLCMNQY YQILSSCRVP
     GPKQDSVISA SKAKKPPMHI TVVHNYQFFE LDVYHSDGTP LTSDQIFVQL EKIWNSSLQA
     NKEPVGILTS NHRNSWAKAY NTLIKDKVNR ESVRSIQNSI FTVCLDAPVP RVSEDVYRNH
     VAGQILHGGG SKINSGNRWF DKTLQFIVAE DGSCGLVYEH AAAEGPPIIT LVDHVIEFTK
     KPELVRSPMV PLPMPKKLRF NITPEIKSDI EKAKQNLSMA AGPLLLIMPP TSMIQDLDIT
     VMVFHHFGKD FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS
     ASVDSLAFVK AMDDSNATEH QKVELLRKAV QAHRAYADRA IHGEAFDRHL LGLKLQAIED
     LVSMPDIFMD TSYAIAMHFN LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP METHINFSVS
     AYNSCAETNA ARLAHYLERA LLDMRALLQS HPRAKL
//
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