ID D7P5E5_9NEOP Unreviewed; 449 AA.
AC D7P5E5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN Name=pgFAR {ECO:0000313|EMBL:ADD62441.1};
OS Yponomeuta rorrellus (willow ermine moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Yponomeutoidea;
OC Yponomeutidae; Yponomeutinae; Yponomeuta.
OX NCBI_TaxID=263928 {ECO:0000313|EMBL:ADD62441.1};
RN [1] {ECO:0000313|EMBL:ADD62441.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pheromone gland {ECO:0000313|EMBL:ADD62441.1};
RX PubMed=20534481; DOI=10.1073/pnas.1000823107;
RA Lienard M.A., Hagstrom A.K., Lassance J.M., Lofstedt C.;
RT "Evolution of multicomponent pheromone signals in small ermine moths
RT involves a single fatty-acyl reductase gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10955-10960(2010).
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; GQ907234; ADD62441.1; -; mRNA.
DR AlphaFoldDB; D7P5E5; -.
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 2: Evidence at transcript level;
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 Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 20..288
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 358..446
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 449 AA; 50931 MW; 14B6B8E2639C3A74 CRC64;
MVQLKEDSVA AFYAEKSIFI TGGTGFLGKV LIEKLLYSCK AVDQIYVLIR KKKDQTPSER
IAQLLESELF SRLRKDDPSA LKKVVPVVGD LTMPNLGLSA AVEDLIVSKV TVIFHVAATV
KFNERMKNAL VNNVEATREV INLCHRLEKV DAFIHVSTAY SNTDQKVVEE RVYPPPAPLS
EVYAFVKNYG DDMDIIQNLL NGRPNTYTYT KALAEDIVLK EHGGIPTAII RPSIVLSVLK
EPIPGWLDNW NGPTGLLHAS SQGVHCSMLG SGSNVADLIP VDIVTNLMIV VASRCRKSNG
LKVYNSCSGT TNPITYQAFT KMFLDSCISR GWNKVPFPLL IFVKWAFLNR VLKFLLVIVP
FFLIDVYLRF FGKPNYMRMI TYTKKAEDLM TFFTSHEWQF KDGNVRDLIN MMSPEDRKIF
YCDPEEIQWK PYFDDYCVGV FKYLLKRKV
//
