ID A0A482X8T4_LAOST Unreviewed; 554 AA.
AC A0A482X8T4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN ORFNames=LSTR_LSTR006719 {ECO:0000313|EMBL:RZF42126.1};
OS Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Criomorphinae; Laodelphax.
OX NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF42126.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF42126.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF42126.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:RZF42126.1};
RX PubMed=29136191; DOI=.1093/gigascience/gix109;
RA Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL Gigascience 6:1-12(2017).
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:RZF42126.1}.
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DR EMBL; QKKF02015641; RZF42126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482X8T4; -.
DR STRING; 195883.A0A482X8T4; -.
DR InParanoid; A0A482X8T4; -.
DR Proteomes; UP000291343; 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:SF61; 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:UP000291343};
KW Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 488..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT TRANSMEM 515..534
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 38..310
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 382..474
FT /note="Fatty acyl-CoA reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03015"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 63396 MW; BBC466160308BE7D CRC64;
MSVDDIPKPN YSPTELPEEL KSLPDRVSET LVGKTLLITG GSGFLGKVLI EKILRKSPSV
EKIYLLMRAK KGKEPKQRVE ELFSSPLFDL LKSQRGLSII DKVEAVNGDV SLPDLGLSPE
HRQLLIDNVN IIFHGAATIR FDEPLRKAVL LNTRGTKLML ELATKMKKFQ LFVHISTSYC
HLQEKVLEEK AYPPPTDPHK IIRTCELMSE ELVETVAKKI LGDFPNSYAY TKCLSEGIAV
EHMNAGLPVI ILRPSIVIPI WKEPLPGWTD NINGPTGLLI GAGKGVIRTM YCDNQGYADY
LPVDITVNGI LLATWNYLGL NDTERTISHL TSSMEWQVSW QEIIDMGKKI VTEKIPLNNA
VWYPGGSMKK SKLLHQICVL LFHMIPAYFL DSIIMLSGHK PILCRVQERI NKGFEVFEYY
ANNQWEFRND QIHYMRKIMN RRERFEYKID GEDMDLYKYF EDCILAARIY ILKEMPDTLP
GARRHMRIMY WVDFFTKCLF YGLVMWFFFS NSSSILNFVL GLFKFVENAF WYLLSGRSSS
DASSTASSTP TLEL
//
