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
//