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Database: UniProt
Entry: A0A0D0CKL8_9AGAR
LinkDB: A0A0D0CKL8_9AGAR
Original site: A0A0D0CKL8_9AGAR 
ID   A0A0D0CKL8_9AGAR        Unreviewed;       602 AA.
AC   A0A0D0CKL8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Pyranose dehydrogenase (acceptor) {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GYMLUDRAFT_44993 {ECO:0000313|EMBL:KIK58972.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK58972.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK58972.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK58972.1,
RC   ECO:0000313|Proteomes:UP000053593};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KN834782; KIK58972.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0CKL8; -.
DR   HOGENOM; CLU_002865_6_3_1; -.
DR   OrthoDB; 3215324at2759; -.
DR   Proteomes; UP000053593; 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   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..602
FT                   /note="Pyranose dehydrogenase (acceptor)"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002208473"
FT   DOMAIN          35..349
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          450..590
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   ACT_SITE        535
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        579
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         114
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   602 AA;  65405 MW;  9060BBBABD44AA2B CRC64;
     MQISRLILII WHIFGLPLCF AKVYNNFRDL PSKHYDFVIV GGGTAGNVVA NRLTENPNFS
     VLVLEAGGTN ANAFEIEVPY FSTRGVQPQF DWNYSTIPQN ALNDRLIPMQ RGFVLGGSSS
     VNRMFYTRGS ADDYDRFAAV TGDEGWSWKG VQKYLAMNEK FERPADRHNI SGQFNPSVHS
     FTGINAVSLP GFAQNIDSMV FDAVAELGGI FHFNEDYNSG KPLGFSWLQR TVTTQGHRSS
     SATSYLAPEF IERKNLDVVL NTRVSRVIPS RSNQSSSGLA FRTVEFVHDL DGPRFTVEAS
     KEVILSGGVF GSAHILLNSG IGNSTMLSRL GISPLVNLPS VGQNLTDHPI VETDWLVNST
     QTMDDINRNT TVSDEDEAEF NKTGMGPLVD SSAGNQIAFF RVDESLTERY GDPSAGRDSP
     HLEMIPGNGW SGIPPATGNF FSLGIAVVSP ASRGSMTINS TDPFAPPLIN PGYFSSPFDI
     AAMRQAMRIA LKYASAPTWK GYILSPFGAL ANITAASDDD VLDEYIQNST FSLAHPVGTV
     AMSAKGADYG VVDPDLRVKG VEGLRVVDAS VFPFITSAHT QAPAYVIGER GAELIKANYE
     RG
//
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