ID T1H885_RHOPR Unreviewed; 373 AA.
AC T1H885;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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:RPRC000223-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:RPRC000223-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|RuleBase:RU363097}.
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DR EMBL; ACPB03002152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1H885; -.
DR STRING; 13249.T1H885; -.
DR EnsemblMetazoa; RPRC000223-RA; RPRC000223-PA; RPRC000223.
DR VEuPathDB; VectorBase:RPRC000223; -.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_024661_0_0_1; -.
DR InParanoid; T1H885; -.
DR OMA; CISREIT; -.
DR OrthoDB; 1434498at2759; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
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 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:SF60; FATTY ACYL-COA REDUCTASE-RELATED; 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:UP000015103}.
SQ SEQUENCE 373 AA; 41584 MW; EF03CC5697FD47C0 CRC64;
MANNSEIIDY FNGKNIFLTG ATGFVGKLLI DQLLRKCQPN KLYLLIRSKK GIEPDKRLEQ
LFEDVVYERL KREKPDILDK IQLISGDLAE NNLGINGKSE ATLIENVNIV IHGGATVKFD
EHIKKATDIN VKGTISIIKL CHRLKKLDAF VYISTAYSNC PYKEIKEEFY DPPIICDELI
LITSKYNNKE LEEMTEKIIG KWPNSYAFTK AVAENAVNTY AKGLPVCVFR PAIIIGTLNE
PVPGWIDNIY GPTGLLAGVA AGVVRVIHTD PKAKAAIVPA DMVAFAIVAA IHKTKLMGPT
NEIPIYNFVT AKDNPITWSD YMNMALKVGK DMPLEKAVWK HSCTLQSNPV IFALYTFFLH
FLPAALLDLV SII
//
