ID A0A0L7QN08_9HYME Unreviewed; 412 AA.
AC A0A0L7QN08;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=WH47_09125 {ECO:0000313|EMBL:KOC59944.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC59944.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC59944.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC59944.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ414868; KOC59944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7QN08; -.
DR STRING; 597456.A0A0L7QN08; -.
DR EnsemblMetazoa; XM_017940344.1; XP_017795833.1; LOC108577212.
DR Proteomes; UP000053825; 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 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:UP000053825};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 274..297
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 382..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 14..110
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 281..371
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 412 AA; 45773 MW; 49C0859B5F1F92AD CRC64;
MALRDWYADR ELLLTGVTSD VGRALLEKIL RSFPNVKVYV IVRPRHGFNK DNRIKNIFLS
PRFERLRHEV PDAISRVKVL QGNVLYDGLG TAKADRERLG KVSVVLHAAG PSDGVLRFCQ
ELPRLQAVVV VSSIFRHASD GEISESAMEK EVVLEGPVAL VRVPLVGSAV REPMPGFVDV
FKGPTALMVG AGLARGNSEF QAEIIPIDLA VNTLIAVAWE RATAKNVEGP VVYNAAPIGC
TWSDLIKKGR RSNRKFTYPT FGLRGMTSMA AVHWILVLLF ECLPSALCDT ILGLLGAKKR
LLEEQQRVRN ALRSLESISS RPWSAERNRV YLVQQRLTPE DQDAFPVATE IDVESYVLCT
AAAAKKYCVD ESNISLVKIF RLLFFFLIAA ALFLAFVSPF RGHHVLEKHS EL
//
