ID T1HPR8_RHOPR Unreviewed; 491 AA.
AC T1HPR8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC006042-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC006042-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-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; ACPB03008273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1HPR8; -.
DR STRING; 13249.T1HPR8; -.
DR EnsemblMetazoa; RPRC006042-RA; RPRC006042-PA; RPRC006042.
DR VEuPathDB; VectorBase:RPRC006042; -.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_0_2_1; -.
DR InParanoid; T1HPR8; -.
DR OMA; KWDNLEQ; -.
DR OrthoDB; 3149309at2759; -.
DR Proteomes; UP000015103; 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:SF60; FATTY ACYL-COA REDUCTASE-RELATED; 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:UP000015103};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 378..401
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 41..311
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 388..479
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 491 AA; 56497 MW; C9B5ABB9AA6C36E7 CRC64;
MDYYELRDTN ELDIPETINN PKSFSELSEI QKCFYDKTVL LTGGSGFIGS LLLESFLRSC
VGIKRVYVLL RPKKGKTVEE RLELLFQNEI FEKVLKKNPK ARSIVKIMNG DITEPMCALS
DECINVIKEE VNFIVHAAAG LRMDEPLKIA FHMNVRSTLH LLQIAEHTKC LKSFVYVSTA
YSHAFRPVIS EEFYKPGFNY QQLELLLDKL GDEEIAAITP KIVGPWGNTY TFTKAVCEDL
VRSFGGKFPL AVVRPSIVIG CDKEPLEGWI NNFYGATGVS LAASLGLMRV WYGDPAKIAD
IIPADKVVKA IIASMWYTIG TFKSDHQLVP IYNIVSSPKA PTTWDHYMGL VEKYAIEDKI
VHSKSVGEYN FRLQPKRWLY FLQMYTMQLL SAIFIDLFLV LKGKKARLLN GYMKIHKFNM
ALGFYSKHEW VYQQKNMDNV WNSMSELDKL LFNFDLSTLD WNQYHIRTIR AIRVYILKDP
METLPQAREK Y
//
