ID A0A3P9BX50_9CICH Unreviewed; 670 AA.
AC A0A3P9BX50;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Carnitine palmitoyltransferase 2 {ECO:0000313|Ensembl:ENSMZEP00005014558.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005014558.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005014558.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005014558.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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, ECO:0000256|RuleBase:RU003801}.
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DR RefSeq; XP_004552980.1; XM_004552923.1.
DR AlphaFoldDB; A0A3P9BX50; -.
DR STRING; 106582.ENSMZEP00005014558; -.
DR Ensembl; ENSMZET00005015041.1; ENSMZEP00005014558.1; ENSMZEG00005010955.1.
DR GeneID; 101474307; -.
DR KEGG; mze:101474307; -.
DR CTD; 1376; -.
DR GeneTree; ENSGT01060000248556; -.
DR OrthoDB; 1429709at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000265160; LG23.
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; 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 Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 65..654
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 670 AA; 74864 MW; 57AD54B46E9A8ECC CRC64;
MAGLLSLHCV ASLKKSGSLI HFRSAALGVH MRHYSSKKAP SSSSSEYLHQ SVVPSMHYQK
SLPRLPIPKL EDTIRRYLAA QKPLLDDDQF RTTEKLAQDF QNGAGKQLHE ELVAQDKNNK
HTSYISAPWF DMYLSARDSV VLNFNPFMSF NPDPKTEYND QLLRATNMVC SAVRFMKTLR
AGLLEPEVFH LNPVKSDTDS FKNFIRWVPS SLSWYGAYMV NAYPLDMSQY FRLFNSTRIP
KHGRDELFTD EKGRHLLVMR KGNMYVFDII DRDGNLVKPA EIQSHLKYIL SDSTPAPAFP
LSVLTSENRD VWAGLRDKLI GAGNAEDLRV VDSALFCLSL DDESMRDHIH ISHNMLHGNG
CNRWYDKSFS LIVTKDGQAA INFEHSWGDG VAVLRFQNEV FKDTTEKPLV HPGSAAAAVD
SASAVRRLQF KLNKELENGI QKAKENIDSA VSKLTIDAME FKRGGKEQLK KNRLSPDAIA
QLAFQMGFLR QYGQTVATYE SCSTAAFKHG RTETIRPATV QTKKCSHAFV QQPGKHSVAE
LQAMLDECSK YHGQLTKEAA MGQGFDRHLF AMRYLAASKG QALPSLYTDP AYAAINHNIL
STSTLTSPAV SLGGFAPVVP DGFGVGYGVH DNWIGCNVSS YPARNVHEFL QCVHKSLEDI
FTVLDGKPLS
//
