ID H3CZP5_TETNG Unreviewed; 651 AA.
AC H3CZP5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Carnitine palmitoyltransferase 2 {ECO:0000313|Ensembl:ENSTNIP00000013731.1};
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:ENSTNIP00000013731.1, 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:ENSTNIP00000013731.1}
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; H3CZP5; -.
DR Ensembl; ENSTNIT00000013925.1; ENSTNIP00000013731.1; ENSTNIG00000005804.1.
DR GeneTree; ENSGT01060000248556; -.
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 53..632
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 651 AA; 73882 MW; 67FE20D5665B792A CRC64;
LVTLDKLNNH TSCMSGDSIT AARPWKRLRG PDDYLQRSLV PTMHYQKSLP RRLPIPKLED
TMRRFLAAQR PLLSDVQFRR AEEIAQDFQN GVGRELHKEL VTRDKLNNHT SYTSGPWLDM
YLKNRKSLLD VNVFVPLHQD PKTEYNQQLL RATNLTCSAL RFMKTLRAGL LEPVFYSEPS
KSNQHLFERV IRWVPPSLSW YGAHMVNAYP LDMSQFHRIS NSTRIPRRGR DELVTHEEGR
HIVVMRKGNM YVFDVVDRDG NLLKPAEIQA HLKYILDDLT PAPAFPIGVL STENRDVWAH
LRDKLVHCGN ADNLRTMESA VFCLCLDDAV PENQENLRLM GNSCNRWLDK SFNFCISTSG
EFSAFSEHSW GDGLIGSLAL GGIHKDSTER PQVHPASAAA AVDSAAAVRL LKFNLDSELK
EGIKKAKDNI SLAESQPGVE FMEFRKGGKE TLKKYKISSD SMVQLAIQMG FLRLYGQTVP
TSESCSTAGF KHGRYEVMMP VSMYTKECAH AFVCQRDQHT TQQLKAMLHQ CSDHHRQLIR
EASSGQGFFC HLYCLYDLST SKDQELHSLF TDCGILNGFT LSTSTVPAPS LKTSVFAPDV
PEGFGVFYTF HDNTIFFSLS SFLPRSRQEL SQSIFKSLED IFTVLEENPL E
//
