ID   A0A2C9K9I8_BIOGL        Unreviewed;       619 AA.
AC   A0A2C9K9I8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   Name=106076716 {ECO:0000313|EnsemblMetazoa:BGLB016741-PA};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB016741-PA, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB016741-PA}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB016741-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   RefSeq; XP_013092990.1; XM_013237536.1.
DR   AlphaFoldDB; A0A2C9K9I8; -.
DR   STRING; 6526.A0A2C9K9I8; -.
DR   EnsemblMetazoa; BGLB016741-RA; BGLB016741-PA; BGLB016741.
DR   KEGG; bgt:106076716; -.
DR   VEuPathDB; VectorBase:BGLB016741; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000076420; 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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          315..329
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         144
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         148
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         280
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   619 AA;  68998 MW;  4228E348F3CD02CD CRC64;
     MSKSKTPEKK QKKAAQVTQN INVLSIGNIL LVAALAILAY RYFQCCDQPG EGLAKKLNAS
     YDYIVIGAGS AGCVLANRLS EDSDVSVLLL EAGGDDRGDF NLMTPGLSHL NMHSKYDWEY
     YTEPQKHGLK GYNQRRSFWP RGKVLGGTSN LYSMVVIRGH KLDYDTWAEL GSEGWSYNDV
     LPFFKKSEDM QDPTLAQSEF HGTGGPLKVS VPKTMPLTDI LLAAGQELGL QISDPNGEVM
     EGLSQTQSHS YKGVRWSTSR GYIHPILSRK NLHVYLNSHV TKILFEGKQA VGVSLIHEGR
     KETVRANKEI ILSAGAIGSP QILMLSGIGP KEHLTELGVP VVADLPVGSN LQDHLFYEYS
     IGLNQTVSAT PEKLDSLWSR LQLKLFGSGV LSSSHFVEVQ VFDCTDEKSR KRNYPDFQIM
     FHQTPWTVES LRKFGYSEET LKESEHRNTH TDMFACEASL LRPESRGTIK LRSSDPFDYP
     ILDPNYLHRQ EDVDLLVRGI RYCQRFEQTK ALKALGAVPA DRPNKFCKDL GYDTDSYWEC
     MVRQKIHTIY HHSGTCKMGK KGDATAVVDP RLRVHGVKGL RVADASIMPL IPSGNTHTPV
     VMVAEKAAHM IKEDRHASG
//