ID A0A452IM35_9SAUR Unreviewed; 626 AA.
AC A0A452IM35;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Choline/carnitine acyltransferase domain-containing protein {ECO:0000259|Pfam:PF00755};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000029119.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000029119.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452IM35; -.
DR Ensembl; ENSGAGT00000033075.1; ENSGAGP00000029119.1; ENSGAGG00000021067.1.
DR Proteomes; UP000291020; 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:UP000291020};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT DOMAIN 38..609
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
FT BINDING 419
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 423..430
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 452
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 454
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 456
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 465
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 504
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
FT BINDING 555
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-2"
SQ SEQUENCE 626 AA; 71288 MW; B852EE086F872D1B CRC64;
MERKQQSEKA KPSGWLRPVA LRKLTGRYLA HQEGLPHLPV PPLQQTLDRY LLALQPIISE
EEWTHTKGLV DEFRKPGGVG ERLQKGLERR ARKTENWLSD WWLKTAYLEY RLPVVVHSSP
GVVLPKQDFV DQQGQLRFAA KLIEGILDFK TMIDNETLPV EYLGGKPLCM NQYYQIFSSC
RIPGSKHDSV VNYAKGKKPP SHITVVHNFQ FFELDVYSSD GSPLTTDQIF IQLEKIWNTS
LQTNKEPIGI LTTNHRNSWA KAYNHLIKDK TNKESVRSIE KSIFTVCLDS PIPRVSDDIY
KSRMAAQMLH GGGSRWNSGN RWFDKTLQFI VAEDGSCGLV YEHAPSEGPP IVALLDHIVE
YTKKPELVRS PMIPLPMPKK LRFNITPEIK NDIEKAKQNL NIMVQDLDIK VMVFHHFGKN
FPKLEKISPD AFIQMALQLA YYRMYGQVCA TYESASLRMF RLGRTDTIRS ASVDSLKFVQ
AMDNPSKQNQ EKVELLRRAA QAHRAYTDMA IRGNAIDRHL LGMKLQAIED LVSMPELFMD
TAYAVAMHFN LSTSQVPAKI DCVMCFGPVV PDGYGVCYNP MDDHINFAMS AYNSCAETNA
ARLAHYLEKA LLDMRLLLQS TPKSKL
//
