ID H3CZP4_TETNG Unreviewed; 664 AA.
AC H3CZP4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Carnitine palmitoyltransferase 2 {ECO:0000313|Ensembl:ENSTNIP00000013730.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000013730.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000013730.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; H3CZP4; -.
DR STRING; 99883.ENSTNIP00000013730; -.
DR Ensembl; ENSTNIT00000013924.1; ENSTNIP00000013730.1; ENSTNIG00000010805.1.
DR GeneTree; ENSGT01060000248556; -.
DR HOGENOM; CLU_013513_4_2_1; -.
DR InParanoid; H3CZP4; -.
DR OMA; WRTHREC; -.
DR TreeFam; TF315202; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000007303; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 63..642
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 664 AA; 75209 MW; 9ECD95ADA17849A0 CRC64;
MAKLLSVCYT SPLGKPGKIL LRNAALNVYG LNYGSKKPSS SDYLQRSLVP TMHYQKSLPR
TRLPIPELED TMRRFVAAQR PLLSDHEFRS NKRKITSKLQ IGVGRELHKE LVTQDKLNNH
TSYMSGPWLD MYLKNRKSLL DVNVFMLLHQ DPKTEYNQQL VRATNLTCSA LRFMKTLRAG
LLEPTVFYSE PSKSNRHLFE RVIRWVPPSL SWYGAHMVNA YPLDMSQYYR IFNSTRIPRR
GRDELVTHEE GRHIVVMRKG NMYVFDVVDR DGNLLKPAEI QAHLKYILDD LTPAPAFPIG
VLSTENRDVW AHLRDKLVHC GNADNLRTME SAIFCLCLDD AVPENQENLW LMSDSCNRWL
DKTLSFRIST SGEACSIFEH SGGDGVSVSH FVDVILKDST ERPQVHPASA PAAVDSAAAV
RLLKFNLDSE LKEGIKKAKD NISLAESQLG VEFMEFRKGG KETLKKCKIS PDSMVQLAIQ
MGFLRLYGQT VPTSESCSMA GFKHGRYEVM MPVSMYTKEC AHAFVCQRDQ HTTQQLKAML
HQCSDHHRQL IREASSAGQG FFCHLYGLYD LATSKDKELH SLFTDCGVLD GFTLSTTILS
MPSSKITFFA PDVPEGFGIH YIFQDNVITC NTSSYLSHSC QELSESIYTS LEDIFTVLEE
KPLG
//
