ID M1RM75_9NEOP Unreviewed; 463 AA.
AC M1RM75;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:AGG19596.1};
OS Ostrinia nr. zaguliaevi JML-2013.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC Crambidae; Pyraustinae; Ostrinia.
OX NCBI_TaxID=1297678 {ECO:0000313|EMBL:AGG19596.1};
RN [1] {ECO:0000313|EMBL:AGG19596.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pheromone gland {ECO:0000313|EMBL:AGG19596.1};
RA Lassance J.-M., Lienard M.A., Antony B., Qian S., Fujii T., Tabata J.,
RA Ishikawa Y., Lofstedt C.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGG19596.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pheromone gland {ECO:0000313|EMBL:AGG19596.1};
RX PubMed=23407169;
RA Lassance J.M., Lienard M.A., Antony B., Qian S., Fujii T., Tabata J.,
RA Ishikawa Y., Lofstedt C.;
RT "Functional consequences of sequence variation in the pheromone
RT biosynthetic gene pgFAR for Ostrinia moths.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:3967-3972(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; JX683346; AGG19596.1; -; mRNA.
DR AlphaFoldDB; M1RM75; -.
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}; NADP {ECO:0000256|RuleBase:RU363097};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363097}.
FT DOMAIN 30..295
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 370..456
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 463 AA; 52723 MW; 9E030AFA5D28920B CRC64;
MSANTVETDE QFTDNNSPIV NFYSGKSVFV TGATGFLGTV LVEKLLFSCK GINNIYILIK
QTEDLTIETR ILNYLNSKAF HRVKNTNPEL MKKIIPICGN LEDKNLGISD SDMKTLLEEV
SIVFHLAAKL LFKMSLTAAV NINTKPTEQL IAICKKMRRN PIFIYVSSAY SNVNKQIIDE
KVYSTGVPLE TIYDTLDTEN TRITDILLDK RPNTYTYSKA LAEVVVEKEF DESAAIVRPS
IIVSSIREPI PGWMSGSHGF PRVVGAACKG LLLRWHGDST VVFDVIPVDH VANLIIAAAW
ESNERRLMGN KGVKVYNCCS GLRNPIDVST IMNTCLKYRK YFGTRTLSIF PPRFIVKKNY
FIYKLLYFTY HTIPAAIVDG FFWLTRRTPM MLNTLHKLSK LSSVLEYFTL HQFLFLDSNV
RGLLRRMEST DRQTFNFDVT EIEWEPYLQN CVRGIANNCD YSM
//
