ID A0A0L0C4W2_LUCCU Unreviewed; 995 AA.
AC A0A0L0C4W2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=FF38_08623 {ECO:0000313|EMBL:KNC26484.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC26484.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC26484.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC26484.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC26484.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC26484.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRES01000984; KNC26484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0C4W2; -.
DR STRING; 7375.A0A0L0C4W2; -.
DR EnsemblMetazoa; KNC26484; KNC26484; FF38_08623.
DR OMA; IIMALWH; -.
DR Proteomes; UP000037069; 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; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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:SF24; FATTY ACYL-COA REDUCTASE; 1.
DR PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR Pfam; PF07993; NAD_binding_4; 2.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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:UP000037069};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 828..851
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 949..966
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 13..282
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 489..760
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 838..883
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
SQ SEQUENCE 995 AA; 114825 MW; F133E51F5894F270 CRC64;
MIKEFFENSE IFVTGGSGVV GKALIEKLLR SCNVKKIYVL LRPKKNVSIE DRLEKVKNAM
VFRQLKLQKP DEMDKKLMAI PGDAIVPFLG ITPEYQQILK NVSIVFHCAA TVRFDEPLRD
ALRLNVGGTL ETLKFAETLK NLKVFMHVST FFSNPYLERV EEKVYESPMD WRVCLNLLER
NDISEEQLDI ITRKLIIGFP NTYCFTKNLA ESLVNDYKDK LPVAIYRPSI VLFAIEEPEP
GFAPSLMGAM GLFAVTAAGI LKTIYIGKDT RLDLTPQDFG IKNLCYYTVK TANLYKSKNK
PQNIPVFLTS SCTHSELTFR QYIHLVQDHG FWAEAAFEKN LLIPGLHCTD NRLMYLFLVL
FKHILPSLLA DFGLILSGRK PVLMSVHRKL YITLEVMKPF LFNSYSSSGI TDADEMMAKL
KGTEFNMDIL PACKEFYRNV GFCQTMVYSV REHLFKEDPK TLPKSRKILQ TVKANKMLPE
FYKDKEIFIT GGSGIVGTAL IEQLLRSCNV RKIYLLLRPK RSMTLEKRLE RVKEEQVFRQ
LKIQKPQELD QKLVAIAGDA KLPMLGITEE SAKLMKNVSI IYHCAATVRF DEPLRDALKL
NVGGTLEAIK FAQTLKKLKI FMHVSTFYSN PYLTRVEPKF YKAPMDWKFC LDLLERKDIG
EEELDIITRK LIVGFPNTYC FTKNLAESLV NDYKDKLPVC IYRPSIVFFA LEQPEPGFSP
SLMGVMGLFA VTGAGLLKTI YINKKNRLDI TPQDVSVKNM LYYTFKAAQV YEKSKPLDIP
VYMTSTCTNF DMTLIEYIQI MDDFGLWEKA AYEKSLLVPG IRTTSNRFIY MFFVLLLQLL
PALLVDFVLL LTGRKPVLMR IQRKVFQTLE VMQPFMFNNY ESEGITHYQE MKEKLKGTTF
SVDVLDNGCD LFSNVGFCNN MVFSARDLLF KEDPKSLPKA RRIFKLKVWL YKFVQFIVLY
KVYVWTMEYI KNSYAEWRHN DFFLDLPLNN RLQLS
//
