ID A0A194QKX4_PAPMA Unreviewed; 564 AA.
AC A0A194QKX4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=RR48_14624 {ECO:0000313|EMBL:KPJ06182.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ06182.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ06182.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ06182.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ06182.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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; KQ461198; KPJ06182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194QKX4; -.
DR InParanoid; A0A194QKX4; -.
DR Proteomes; UP000053240; 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:UP000053240};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..564
FT /note="Fatty acyl-CoA reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008264425"
FT TRANSMEM 396..420
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 511..533
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 62..332
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 405..497
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 564 AA; 64419 MW; EB6F22786457E3A7 CRC64;
MESMCNMLHY CMLYACLFLT DHLPISDDEA GRSELKCYMI GNTGGKMNSE VNEWYKGRNV
LVTGASGLMG KVLIEKMLYS VPDIGCVYAL VRSKRGKTPE SRIEDMWKLP LFSRIREEKP
HMMKKLVPVS GDIMYDNLGI DSKILEQIYD EVSVVFHFAA SLRLEAPLKE GLEMNTKGTM
RVLDVAKRIK NLVSFVHLST AFCYPDYSRM AEKVHDPPAN PHEVLQAASW LTDEQVNLLT
PTLLQSHANS YTYSKRLAET LVKEQYPELP VCVVRPSIVT PSYKEPVEGW VDNLNGPVGL
MVGAGKGVIR SMHCIGHYHA EVIPVDIAIN AIIVIPYYIN SLPERSPEIP VFNLTSGDDR
DTTWKEVLDV GKATVRKYPF EGPLWYPDGN IRHNKFIHSI CVLFFHILPA YLIDFLMLIF
GQKRFMVRIQ NRISVGLEVL QYFTTREWWF DTHNFKALST RLNQVDTKTF PMDLKIIEVE
PYIESCMLGA KMFCLKEKLE NLSKARLQNN ILYVLDLVVT AFVFYLLPLY LLATYVEPFR
MLLSFGGPFV RYLPLVGKAV FTEG
//
