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Database: UniProt
Entry: A0A2H3J4R8_WOLCO
LinkDB: A0A2H3J4R8_WOLCO
Original site: A0A2H3J4R8_WOLCO 
ID   A0A2H3J4R8_WOLCO        Unreviewed;       583 AA.
AC   A0A2H3J4R8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:PCH36941.1};
GN   ORFNames=WOLCODRAFT_134423 {ECO:0000313|EMBL:PCH36941.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phaeolaceae; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH36941.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH36941.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH36941.1,
RC   ECO:0000313|Proteomes:UP000218811};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; KB467898; PCH36941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3J4R8; -.
DR   STRING; 742152.A0A2H3J4R8; -.
DR   OMA; EIMPMAY; -.
DR   OrthoDB; 3714148at2759; -.
DR   Proteomes; UP000218811; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF219; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218811}.
FT   DOMAIN          95..118
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   ACT_SITE        512
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        558
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         101
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         240
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   583 AA;  64959 MW;  5856A40F9DEF46EE CRC64;
     MWPFSTYPEL TANQLSEEYD FIIVGGGTAG CVLANRLSAD PAVKVLLLER GPRADSWAAR
     VPLFSSDFAS DGSRTLRVAS KEQNQLGRSL LLFTGRALGG TSRINQMLYT RGLPAEYDAW
     SEAGRKGWSW ADLRPYFLRS ERSLSGAVAD VHNAQGEWMN RTFGRFYFPG FEQAITAAED
     LDLPYIDDLN SPTHPPFGCG RLHFTIDERA KRNSTYHAFL PEALARQRAQ NLHICTNTLV
     EKIDIERLEG NGLVARGVTL LSSGDKNPER RYHIRARREI VLSAGPFGSP QTLMLSGIGP
     SGHLQEHGIP VLKDLPAVGS NLQDHFAVST GFFVPMRDSL LSLQTNPWRF LKELFKYLIW
     GTGWLLGPVL QLAIFTHTRL LDESGRPTRT DKAFAQDLPD IEIMPMAYSS HDGIVPRTRG
     LFSFLSVLLH PRSKGSVRLS SPDPRAPLVV DPRYLSNAED MAPLRASLKL SLRLRDQMRE
     RGYTMDDWLV PASESDSDLD AFIRTSNRTT YHYSSTCRMA PEDDTDGGGV VDDELNVHRV
     GHLRVADTSI FPWIPGTHLQ APAVAVAEKC ADMMLTSLNS LYR
//
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