ID M3XIE6_LATCH Unreviewed; 631 AA.
AC M3XIE6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|Ensembl:ENSLACP00000022502.1};
GN Name=CRAT {ECO:0000313|Ensembl:ENSLACP00000022502.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000022502.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000022502.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFYH01046078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01046079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01046080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01046081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01046082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005993311.1; XM_005993249.2.
DR AlphaFoldDB; M3XIE6; -.
DR STRING; 7897.ENSLACP00000022502; -.
DR Ensembl; ENSLACT00000024956.1; ENSLACP00000022502.1; ENSLACG00000013470.2.
DR GeneID; 102359761; -.
DR KEGG; lcm:102359761; -.
DR CTD; 449545; -.
DR eggNOG; KOG3717; Eukaryota.
DR GeneTree; ENSGT01060000248556; -.
DR HOGENOM; CLU_013513_5_0_1; -.
DR InParanoid; M3XIE6; -.
DR OMA; ENHSKGP; -.
DR OrthoDB; 1429709at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000013470; Expressed in mesonephros and 1 other cell type or tissue.
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:UP000008672};
KW Transferase {ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 43..613
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT BINDING 424
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 428..435
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 457
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 459
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 461
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 470
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 509
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 560
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
SQ SEQUENCE 631 AA; 71426 MW; E6419CDCFB76FA41 CRC64;
MLLAVRNIMG KQALLKPICL VKPVSLTKIP GRYLAHQEGL PRLPVPPLQQ TLERYLLALE
PIISLEELDH TRGIVKEFGA LGGVGERLQK GLERRARKNE NWLSDWWLQT AYLEYRLPVV
IHSSPGVILP KQDFQDRQGQ LRFAAKLIAG VLDFKAMIDN ETLPVEYLGG KPLCMNQYYQ
ILSSCRIPGS RRDSVVNYAR TSKPPTHITV VHNFQFFELD VYNSDGSPLT VDQIYIQLEK
IWNSSLQTNK EPLGILTSQH RNTWGNAYNN LLKDKTNKES MRIIQKSIFT VCLDAPVPRV
SDELYKSRVA AQMLHGGGSR WNSGNRWFDK TLQFIVAEDG SCGLVYEHAP AEGPPIVALV
DHVMEYTKKS EVVRSPMLPL AMPKKLRFNI TPEIKKDIEN AKQNLNIMIQ DLDIKVFVFS
QFGKSFPKSQ KMSPDAFIQM ALQLAYYRIY GCVCATYESA SLRMFHLGRT DTIRSASYDS
MKFVEAMDDP SKQNQEKVEL LHKAVKYHRT YTDMAIQGQA IDRHLLGLKF QAIEDLVSMP
EIFMDTAYAV AFHFHLSTSQ VPAKVDCVMC FGPVVPDGYG VCYNPMDDHI NFCVSAFNSC
AETNASELAE KLESALSNMQ SLLQQTPKSK L
//