ID A0A2C5XBA8_9HYPO Unreviewed; 665 AA.
AC A0A2C5XBA8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=CDD81_1228 {ECO:0000313|EMBL:PHH65859.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH65859.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH65859.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH65859.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-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}.
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:PHH65859.1}.
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DR EMBL; NJET01000013; PHH65859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5XBA8; -.
DR STRING; 1399860.A0A2C5XBA8; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000226192; 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:SF80; -; 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|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000226192};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..665
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013287850"
FT DOMAIN 364..378
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 19..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 665 AA; 73343 MW; 507D52BDB08B7DEC CRC64;
MFLRHTLTLW GLFATALGSA SRGTGKTSDS GRDSGSDSGS DSDVFDYVVV GSGPGGGPLA
VNLAEAGYSV LLLEAGQNHS SSYKQEIPAF FVEAQFDESQ GWWFYVKHYG DEATSARVNK
MVWKKPDGGL WVGQDAPAGS SMLGVWYPRA GTLGGCDTHN GGVTVYPSEW DWEAIAQRTN
DSSWKAQHMR HYFERLERNM LVPPHTPGHG FAGYQPIDVG AKEHYEAEPQ MLAIAQASAA
ALGFTQRSTS TDWDVILNKD SNAYTPDRDR RNDAYQISLK KDHKGRRFSA ASRVNQAVAR
GLPLTVRFNS LVTRVVIDDA SKRATGVDYL EGAHLYRADP LVRTNSTGLP RSVRASREVI
VSGGTFNTPQ ILQLSGIGPR QELQRLGIPV IVDLGGVGRN LQDHYEVPVV HEFRNDFTYW
DRCDPYNHSS ACFQEWRNEG KGPYTTIGFS HLVTHTSSVA PRGERDLILY GAPNTVRGHL
PPYTHWPRFQ TGNNKFTFTV SESHSRNRAG RVTLTSTDPR DVPDINFEYF AHGAQDDMQG
LMDGVAFARN IFDSIPARNR SVAEAWPGRH LSSPDSMRDW IKEEAYGHHA TGTASIGAHD
DPLAVLDSDF RVRGIDGLRV VDASVFPDVP GTFPIIAIFM VSEKASHVIL ADARRHDLGQ
IQNLL
//
