ID A0A0V0ZJ38_9BILA Unreviewed; 971 AA.
AC A0A0V0ZJ38;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carnitine O-palmitoyltransferase 2, mitochondrial {ECO:0000313|EMBL:KRY12436.1};
GN Name=Dhps {ECO:0000313|EMBL:KRY12436.1};
GN ORFNames=T12_5062 {ECO:0000313|EMBL:KRY12436.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY12436.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY12436.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY12436.1};
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}.
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:KRY12436.1}.
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DR EMBL; JYDQ01000165; KRY12436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZJ38; -.
DR STRING; 990121.A0A0V0ZJ38; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000054783; 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 Gene3D; 3.40.1230.10; MTH938-like; 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 InterPro; IPR036748; MTH938-like_sf.
DR InterPro; IPR007523; NDUFAF3/AAMDC.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR22589:SF16; CARNITINE O-PALMITOYLTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF04430; DUF498; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF64076; MTH938-like; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
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:UP000054783};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRY12436.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..971
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006873753"
FT DOMAIN 96..687
FT /note="Choline/carnitine acyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00755"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ SEQUENCE 971 AA; 110881 MW; 342E7831BACD0700 CRC64;
MLLILLTFYC LHIIVYIVIA VAAVCSKQAD IDYDIEVADS FLTKMKAKLG DRLEFSQRSS
EKINNNRDQQ AHDLAYQFLE RSKIPTMHFQ DGLPRLPIPK LKYTCQNYLN GIRPFLNDEQ
FDAAKKLVDD FRHSSGERLN RELILWYRRN KHTSYIAEPW FDMYFRYRAA LPINQNPFLV
WKPYNESFNN DQLSVATNIV ISACRFKRSL DYNCLQPEVY HFYPNKSNTP FFRNICSRLP
GKLAWLIAFL MKAFPLDMSQ YSFLFNTTRI PVMIKDQLNT NRSSKCIIVL RRGYFYSLTV
FRKDGSLISP AEIHASLEYI LKDNRPVAEN PVGLLTTVGR EQWSLLRSQL LMIDGNERSL
LTIDGGLFVL NLDELQSVDP ETVGKSFLHG DGINRWFDKS MQIIVHADGL AGVNFEHSWG
DGVAVLRFME DVYRDINLNA WIKPGQPTDA SVDCSEFVEK LEFKLTKPIE EAIKVAGETY
REWCDSLMLR TLQYQAMNRK YLKEKNLSPD AIMQTAIQIA FYRLHSKFVP TYESCSTAAF
KHGRTEAVRP ATMASNEFVQ ALLGSERNFA QLRILLEACS KQHSLLVKQA AMGKGFDRHL
FAMKVLAERR GDRLPDLFID DTYRTANHFT LSTSSLFSDV ILLGGFGPVV HDGYGIGYSI
TDEQLGFLVT TYRLKRNAQQ FCTSLEQSLN DIPLLKNRCL FNRTNAISGK STFAKNDDAA
ENNSKTTEPP RWTPKKAWNE SLASQYYITE EGKSMRTSVT TVQATMDETY LCIAAYNNYG
FRLSNQTQVI GPMIVFPQAA LSWKVASPDE ITEESVSMLR LIEPKPDLVL IGVGNSEDVA
QPDACPLFNY MNADGRFVIA LLFPVRKMPK AGLIALTSNF DRALAHEMDS DVLATLAGVK
AKSIPHAITR DQFLISKVLL KHYNERPSTI YFRPLMRYWF DSLHVFYLLE ISNAVFTASI
LYDCCVFGSL E
//
