ID   A0A2A4K2V8_HELVI        Unreviewed;       656 AA.
AC   A0A2A4K2V8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=B5V51_3685 {ECO:0000313|EMBL:PCG78591.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG78591.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG78591.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG78591.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG78591.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PCG78591.1}.
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DR   EMBL; NWSH01000190; PCG78591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4K2V8; -.
DR   STRING; 7102.A0A2A4K2V8; -.
DR   Proteomes; UP000218220; 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:UP000218220}.
FT   DOMAIN          136..159
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          313..327
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         138
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         276
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   656 AA;  73050 MW;  01E0334F15697C50 CRC64;
     MGVVSVAAAA TKAALAIGGL SKLSIIPVLI AAMAYFNYET LDPEQRPFNQ KHLREKYDFI
     IVGGGSAGSV LANRLSEIEG WNVLLLEAGG HETDISDVPL LSLYLHKSKL DWKYRTQPQD
     TACQAMIDKR CAWTKGKVLG GSSVLNTMLY IRGNRRDFDH WVEQGNPGWG YEDVLPYFKK
     SQDQRNPYLA KDTRHHATGG YLTVQDSPFN TPIGAALIQA GEEMGYDFID VNGAQQTGYA
     WYQFTIRRGT RCSAAKAFLR PVRLRQNLHI ALFTHVTKVL IDKDGKRAYG VEFIRDGVKQ
     VVYATHEVIL SAGSIGSPQL LMLSGVGPAK HLQEVGVDVI QDSPGVGRNL QDHIAVGGIV
     FRIDAPVSLV MNRLVNINSA LRYAITEDGP LTSSIGLEVV AFINTKYANA SDDWPDIEFM
     MTSASTPSDG GTQVKRAHSL TDDFYNEVFS EINNKDVFGI FPMMLRPKSR GFIKLRSNNP
     LDYPIMVHNY LTHPDDVGVL REGVKAAIAV GETTAMKRFG ARYHSKPLPN CKHLPPYTDE
     YWDCYIRQYT MTIYHISCTA KMGPSTDPMA VVDPQLRVYG IKGLRVIDAS IMPTITNGNI
     NAPVMMIAEK GADMIKEEWM AKSNKKRRTR RSAKCAMLEH LGLNSDRRKK YCRTER
//