ID A0A482WRF6_LAOST Unreviewed; 626 AA.
AC A0A482WRF6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=LSTR_LSTR013381 {ECO:0000313|EMBL:RZF36157.1};
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:RZF36157.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF36157.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF36157.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:RZF36157.1};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:RZF36157.1}.
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DR EMBL; QKKF02026906; RZF36157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482WRF6; -.
DR STRING; 195883.A0A482WRF6; -.
DR InParanoid; A0A482WRF6; -.
DR Proteomes; UP000291343; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF154; FI04917P; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000291343}.
FT DOMAIN 137..160
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 314..328
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 139
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 626 AA; 69568 MW; EF2EF9D283E17B02 CRC64;
MVDVGTIVVG ALKAASGVVG ISKLWFLPTF LAALAYYNYD IYDPENQPLN TNNIREEYDF
IVVGGGSAGC VMANRLTEVP QWTTLLLEAG GQETELTDVP VLSLYLHKSK FDWKYRTQPS
DTACQAMKDK RCCWTRGKVI GGSSVLNTML YIRGNRRDYD YWAALGNEGW GYEDILPYFK
KSQDQTNPYL ARNTRYHGTG GYLTVMDAPW MTPLGVAFLQ AGEEMGYPIT DVNGENQTGF
SFYQFTMRRG YRCSAAKAFL RPVRLRQNLH VSLWSHVTKI LIDAETKRAY GVEFIKNGVK
KTVLAKREVI LSAGAIGSPQ LLMVSGVGPA AHLSELNIPV IYDSPGVGEN LMDHIAVGGI
VFQVDYPVSL VMNRVVNLNA ALRYAVSGDG PLTSSVGLET VGFITTKYGN ISDDWPDMEF
MLTSTTTSSD GGTASANAHG LTKEFYDDFL GDLSNKDVFG VFPMILRPKS RGRIKLKSSN
ALHYPLMYHN YLTHPEDMRV LREGVKASLA IGETLAMKRF GARFHRKTVP GCKHLPPFTD
EYWECFIRQY TMTIYHMSGT CKMGPSSDPE AVVDPQLRLY GVQGLRVIDA SIMPQITSGN
INAPVIMIAE KGADMIKEYW LQRDAL
//
