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Database: UniProt
Entry: A0A1I8PNU3_STOCA
LinkDB: A0A1I8PNU3_STOCA
Original site: A0A1I8PNU3_STOCA 
ID   A0A1I8PNU3_STOCA        Unreviewed;       629 AA.
AC   A0A1I8PNU3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   28-JUN-2023, entry version 27.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   Name=106085757 {ECO:0000313|EnsemblMetazoa:SCAU009783-PA};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU009783-PA, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU009783-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU009783-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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}.
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DR   RefSeq; XP_013105615.1; XM_013250161.1.
DR   AlphaFoldDB; A0A1I8PNU3; -.
DR   STRING; 35570.A0A1I8PNU3; -.
DR   EnsemblMetazoa; SCAU009783-RA; SCAU009783-PA; SCAU009783.
DR   GeneID; 106085757; -.
DR   KEGG; scac:106085757; -.
DR   VEuPathDB; VectorBase:SCAU009783; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000095300; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF215; FI02019P; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          136..159
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          312..326
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         275
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   629 AA;  70806 MW;  802F7A83A0ED6766 CRC64;
     MVFNLLFITT VIKSTFGVVT TGLWLIPLLL ATITYYKYDQ VDPEARAFDH QDLYADYDFI
     VVGAGSAGAV VANRLSEVRK WKVLLLEAGP DENEISDVPS LAAYLQLSKL DWQYKTAPSN
     KSCLGMKNNR CNWPRGKVLG GSSVLNYMLY VRGNRHDYDH WESLGNEGWG YDNVLHYFKK
     SEDNRNPYLS GNAYHGSGGY LTVQESPWHT PLVAAFVEAG TELGYENRDI NGETQTGFMI
     AQGTIRRGSR CSTAKAFLRP IRQRKNFHLS LNSQVTKVII DESNMRVKGV EFVKYGQVRR
     VYAKREVILS AGALNTPQIM MLSGIGPRQH LEEHGIKVLQ DLPVGENMQD HVGMGGLTFL
     VDKPVAIVQD RFNPTGITLQ YVLRERGPMT TLGGVEGLAF VHTPYSNRSL DWPDIQFHMA
     PASINSDNGA RVKKVMGLKE SLYQEVYHPI GNKDSWSIIP LLLRPRSRGW VRLRSANPFV
     YPIIDANYFD DPLDVKVLVE GAKIALRVAE AKVFKQFGSR LYQKPLPNCK KFRFMSDAYI
     ECHIRTISMT IYHPCGTAKM GPAWDEEAVV DPRLRVYGIR GLRVIDASIM PTISSGNTNA
     PVIMIGEKGA DLIKEDWFHN PEYRVNEKS
//
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