ID A0A0V1CMC1_TRIBR Unreviewed; 744 AA.
AC A0A0V1CMC1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carnitine O-palmitoyltransferase 2, mitochondrial {ECO:0000313|EMBL:KRY49891.1};
GN Name=Cpt2 {ECO:0000313|EMBL:KRY49891.1};
GN ORFNames=T03_7194 {ECO:0000313|EMBL:KRY49891.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY49891.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY49891.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY49891.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-
CC dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
CC ChEBI:CHEBI:84654; Evidence={ECO:0000256|ARBA:ARBA00024283};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
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:KRY49891.1}.
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DR EMBL; JYDI01000163; KRY49891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CMC1; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1280.180; -; 1.
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:SF16; CARNITINE O-PALMITOYLTRANSFERASE 2, MITOCHONDRIAL; 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:UP000054653};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 145..732
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 462
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 744 AA; 85652 MW; 97BD87FA6F1F76CD CRC64;
MPRGSGFDNS IKNYENEKTM QPENNRLSGQ IYKNDKKANN WSYVKLKKNA INLTYILLSA
HYYLHSVIAV AAVCSKQADI DYDIEVADSF LTKMKAKLGD RLEFSQRSSE KINNNRDQEA
HDLAYQFLER SKIPTMHFQD GLPRLPIPKL KYTCQNYLNG IRPFLNDEQF DAAKKLVDDF
RHSSGERLNR ELILWYRRNK HTKPWFDMYF RYRAALPINQ NPFLVWKPYN ESFNNDQLSV
ATNIVISACR FKRSLDYNCL QPEVYHFYPN KSNTPFFRNI CSRLPGKLAW LIAFLMKAFP
LDMSQYSFLF NTTRIPVMIK DQLNTNRSSK CIIVLRRGYF YSLTVFRKDG SLISPAEIHA
SLEYILKDNR PVAENPIGLL TTVGREQWSL LRSQLLMIDG NERSLLTIDG GLFVLNLDEL
QSVDPETVGK SFLHGDGINR WFDKSMQIIV HADGLAGVNF EHSWGDGVAV LRFMEDVYRD
ISLNAWIKPG QPTDASIDCS EFVEKLEFKL TKPIEEAIKV AGETYREWCD SLMLRTLQYQ
AMNRKYLKEK NLSPDAIMQT AIQIAFYRLH SKFVPTYESC STAAFKHGRT EAVRPATMAS
NEFVQALLGS ERNFAQLRLL LEACSKQHSL LVKQAAMGKG FDRHLFAMKV LAERRGDRLP
DLFIDDTYRI ANHFTLSTSS LFSDVILLGG FGPVVHDGYG IGYSITDEQL GFLVTTYRLK
RNAQQFCTSL EQSLNDIRMV LENS
//
