ID   A0A0D0CIQ4_9AGAR        Unreviewed;       697 AA.
AC   A0A0D0CIQ4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Pyranose dehydrogenase (acceptor) {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GYMLUDRAFT_260265 {ECO:0000313|EMBL:KIK62544.1};
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:KIK62544.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK62544.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK62544.1,
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; KN834767; KIK62544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0CIQ4; -.
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   CDD; cd22191; DPBB_RlpA_EXP_N-like; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 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   InterPro; IPR036908; RlpA-like_sf.
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; SSF50685; Barwin-like endoglucanases; 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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..697
FT                   /note="Pyranose dehydrogenase (acceptor)"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002208426"
FT   DOMAIN          134..447
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          547..688
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   ACT_SITE        632
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        676
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         212
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         220..223
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   697 AA;  75516 MW;  F4A9BD221982A273 CRC64;
     MPIFSSRMLL YTLFSFCFFN LSSAASFHRN PSLEKRFDNA PFTFYNVGTG TCGKTNVASD
     FVVALNVAQY GSGQDCFRTI NISYGGKSTQ AQIVDEELGL DLSIGLFEFF APLSDGLLIG
     ILYNNFSDLP SRAYDFVIIG GGTAGSVVAN RLTENPESSV LIIEAGGTNI DAFQLDVPFF
     ASIFKSQYDW NFTTTVQQGL NNHSTFLPRG FVLGGSSSVN GMVYTRGSAD DYDRWATVTK
     DDGWSWDNLQ PFIAKNEKWE LPADRHNTTG QFNPSVHSLT GVNAVSLSGF SESIDPMIFE
     AVDELGGIFN FNQDYNSGNP LGFGWLQLTI STEGRRSSSA TSYLAPKYIE RKNLDVLLHA
     RASRVLPSVS KSSLSGYAFR TVEFAQDLDG PLLQVNALKE VILSAGVIGS PHILLNSGIG
     DSDELSEIGI KSLVNLPSVG KNLTDQPAVT NVFLVNSNKT TDDLLRNATL LNKVYTEFNK
     TGMGPLVVTG GNQISFFRAS ESLTHKFGDP SSGRNSPHLE MLPANGFYGI PPPAGHFLTL
     ETTVVSPASR GSLTINSTNP FANPLIDPGY LTSPFDIAAM REVIRITFQY LSAPIWDGYL
     LSQFGDFANI TATSPDNVLD EYIRNNAGSS GHPVGTAAMS AKDADYGVVD PDLRVKRVEG
     LRMIDSSVFP FVTSAHTQAP TYVIAERAAA LVQAAWV
//