ID Q29JL4_DROPS Unreviewed; 498 AA.
AC Q29JL4; A0A6I8UGQ9;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 2.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN Name=LOC4815751 {ECO:0000313|RefSeq:XP_001355230.2};
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245 {ECO:0000313|Proteomes:UP000001819, ECO:0000313|RefSeq:XP_001355230.2};
RN [1] {ECO:0000313|RefSeq:XP_001355230.2}
RP IDENTIFICATION.
RC STRAIN=MV2-25 {ECO:0000313|RefSeq:XP_001355230.2};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_001355230.2};
RG RefSeq;
RL Submitted (NOV-2023) 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|RuleBase:RU363097}.
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DR RefSeq; XP_001355230.2; XM_001355194.4.
DR AlphaFoldDB; Q29JL4; -.
DR STRING; 46245.Q29JL4; -.
DR EnsemblMetazoa; FBtr0274715; FBpp0273153; FBgn0074798.
DR GeneID; 4815751; -.
DR KEGG; dpo:4815751; -.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_0_2_1; -.
DR InParanoid; Q29JL4; -.
DR OMA; CNVRRIY; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0074798; Expressed in adult organism and 1 other cell type or tissue.
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:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IEA:EnsemblMetazoa.
DR GO; GO:1901568; P:fatty acid derivative metabolic process; IEA:UniProt.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:EnsemblMetazoa.
DR GO; GO:0010884; P:positive regulation of lipid storage; IEA:EnsemblMetazoa.
DR CDD; cd05236; FAR-N_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR026055; FAR.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11011:SF24; FATTY ACYL-COA REDUCTASE; 1.
DR PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU363097};
KW Lipid metabolism {ECO:0000256|RuleBase:RU363097};
KW NADP {ECO:0000256|RuleBase:RU363097};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW Reference proteome {ECO:0000313|Proteomes:UP000001819}.
FT DOMAIN 14..281
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
SQ SEQUENCE 498 AA; 56719 MW; ACFFE7D38CA0F0F6 CRC64;
MSLANFYEDS EIFVTGGSGV VGKALIEKLL RSCNVRRIYV LLRPRRQLSA EQRLVKLRQA
TIFHVLHQEK PDELDKLVAV PGDVLLPGLG IDPAMAAQMS KVSLVYHCAA TVRFDEPLRV
ALQLNVGGTF EAIKFAETLA HLRVFVHVST FYSNPYLKFV EPKYYSSPMD WRLCLRVIEE
VPDDGMLNAL TRKLIVGFPN TYTFTKNLAE SLVNDYRCRL PLIIYRPSIV LFAVDDPSPG
FSPSLMGAMG LFALVGAGIL KTVYLGKETR LDITPQDVGI KCMLSYTKKG QEKYQKGPPK
EIPVYMSSSC THVPHTFTQI AEQMDTLGLW KKAAFEKSLM VPGCHYTDRR WVYQFLVFTK
QILPALLIDL LLRLFGKRPQ LMGVVRKAYQ TLEVMQPFMF NNYDSPGVTE KDEISKENHG
TDFHLNPFTD PDINGLVIRV SGQMLYSIRA HLFKEDPCTL PRSQRIHTIK TIIYQGLRLI
LLYKLVRWIW ASYLGQHF
//
