ID U4UHU2_DENPD Unreviewed; 518 AA.
AC U4UHU2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=D910_06812 {ECO:0000313|EMBL:ERL89445.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL89445.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL89445.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
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; KB632169; ERL89445.1; -; Genomic_DNA.
DR RefSeq; XP_019766230.1; XM_019910671.1.
DR AlphaFoldDB; U4UHU2; -.
DR GeneID; 109541740; -.
DR KEGG; dpa:109541740; -.
DR OrthoDB; 1434498at2759; -.
DR Proteomes; UP000030742; 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:SF12; 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:UP000030742};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 352..376
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 467..490
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 19..288
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 361..453
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 518 AA; 59084 MW; 9584E8142392B58C CRC64;
MAKEKSPIAE WYGGRSIFLT GGSGFMGKVM LEKLLYSCDR LKTVYILLRE KRGRTPQQRV
EDMWKLPMFE RLRQKDPDAI KKVVALAGDL YTEGLGLKPQ DLDALAKNVS VVFHMAATLK
LEANLRDAVE QNTAGTATVL DVAKKIKNLV AFCHFSTAYC SADIEVFEER VYECKDNPRE
VIEIVRWIDP GALELATKKI IEPHPNTYTY SKRLAEILVA NEKDNMPVCI IRPAVVCPAA
LEPLTGWVDS LNGPMGLLVA AGKGVLRSMH CLSSNKAQVI PVDFAINASI VIAYKLGSQK
RQKDVPVYNL TQDGVIQITM GEVLDKGRNI VYANPFEMQV WYPDGDIRSS KIMHTICCIF
MHWLPALLID FIMLLIRQKR FMIRVQKKIH QGLELLQFFT VREWNFASDK FLALWDEMGE
TDKKIFPMDF NALPIEAYLE NCVLGARQYC MKEPLTSLPR CRLQQKVLYV LHKLFVCFLY
YYAFYLLSLW IPPVRIIYNL LWQVIGSLPL IGLLVAQK
//
