ID T1KR48_TETUR Unreviewed; 508 AA.
AC T1KR48;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN Name=107366553 {ECO:0000313|EnsemblMetazoa:tetur18g02250.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur18g02250.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur18g02250.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
CC {ECO:0000256|RuleBase:RU363097}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain
CC primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84;
CC Evidence={ECO:0000256|RuleBase:RU363097};
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000256|ARBA:ARBA00005928, ECO:0000256|RuleBase:RU363097}.
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DR EMBL; CAEY01000384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015789664.1; XM_015934178.1.
DR RefSeq; XP_015789665.1; XM_015934179.1.
DR AlphaFoldDB; T1KR48; -.
DR EnsemblMetazoa; tetur18g02250.1; tetur18g02250.1; tetur18g02250.
DR GeneID; 107366553; -.
DR KEGG; tut:107366553; -.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_0_2_1; -.
DR OrthoDB; 1434498at2759; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0102965; F:alcohol-forming long-chain fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0080019; F:alcohol-forming very long-chain fatty acyl-CoA reductase activity; IEA:InterPro.
DR GO; GO:1901568; P:fatty acid derivative metabolic process; IEA:UniProt.
DR CDD; cd05236; FAR-N_SDR_e; 1.
DR CDD; cd09071; FAR_C; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR026055; FAR.
DR InterPro; IPR033640; FAR_C.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11011:SF45; FATTY ACYL-COA REDUCTASE; 1.
DR PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU363097};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU363097}; Membrane {ECO:0000256|RuleBase:RU363097};
KW NADP {ECO:0000256|RuleBase:RU363097};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 365..384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 476..494
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 25..293
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 367..459
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 508 AA; 57806 MW; 29C47FB966BB4EE1 CRC64;
MNNNNESTLD QSSILDFYAG KTLFITGFSG FLGKVLVEKI LRCIDVKRVY VLLRGKRGLS
PAERLKQILN KQPFTFHDKT VLNAYKVVAV EGDLGAPNLG IDQKTCDKLI EEVNVVLHCA
ADVRFDADLE SNLVNNVKGT EYLIDLCHQF AHLEAMVHVS TAYSFCDRLV IEEKVYPMEF
GYDEVENVLK SPDAAFKKKQ TEKFLAGRPN PYTLTKALGE DLVMKKRGNI PTSIVRPSIV
ISSVNEPAPG WVDTIQGIQG IGLAAQIGLL QTVDWNYWAA VDTIAVDICA NFIIASAWYS
ACKKPNECMV YNLTAGAFHP EMTWGGIFEL AREAAYVYPS KKQLRPLMAP PKYKRARFYY
PLEKFLYHTF FAILLDMIIS LFGYKRFLYK QACRLNKGLD LVVFFTTHEF KIKTDRYLEL
VNSLSPKDYK LFYCDVRKFN FSEYIVDCVK GFKKYFLKED EADIASAKKQ VMIVCALYRF
IQLMFLGLIG KYLFSLGCYL MNNTVTSS
//
