ID A0A137QXU4_9AGAR Unreviewed; 497 AA.
AC A0A137QXU4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=pyranose dehydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00013177};
DE EC=1.1.99.29 {ECO:0000256|ARBA:ARBA00013177};
DE Flags: Fragment;
GN ORFNames=AN958_10349 {ECO:0000313|EMBL:KXN92019.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN92019.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN92019.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN92019.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the single-oxidation or sequential double oxidation
CC reaction of carbohydrates primarily at carbon-2 and/or carbon-3 with
CC the concomitant reduction of the flavin. The enzyme exhibits a broad
CC sugar substrate specificity, oxidizing different aldopyranoses to the
CC corresponding C-1, C-2, C-3 or C-1,2, C-2,3 and C-3,4 (di)dehydro
CC sugars with substrate-specific regioselectivity. Accepts only a narrow
CC range of electron acceptors such as substituted benzoquinones and
CC complexed metal ions and reacts extremely slowly with O(2) as acceptor.
CC May play a role in the natural recycling of plant matter by oxidizing
CC all major monosaccharides in lignocellulose and by reducing quinone
CC compounds or reactive radical species generated during lignin
CC depolymerization. {ECO:0000256|ARBA:ARBA00024699}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3,4-diulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00034059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3-ulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00034050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2,3-diulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00034010};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00033986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-3-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000256|ARBA:ARBA00034029};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KQ961941; KXN92019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QXU4; -.
DR STRING; 1714833.A0A137QXU4; -.
DR OrthoDB; 3714148at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0033718; F:pyranose dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 199..213
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 428
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 475
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 154
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXN92019.1"
SQ SEQUENCE 497 AA; 55055 MW; A912E0643C907829 CRC64;
IDKEFLLVNG SGLGGTSRIN SMLYSRGIPR EYDMWAETGC EGWSWTEVEA FFKKSERSLE
DHVDPEFHGK DGEWRTRSAP PSFPGFQHVI ASCKNIGLPV IDDINSTKTP LIGCGQVSFT
RDENQYRNST FHAFLPLGLV KQRSNLHILT NAIVEKVVIG KRSTGPFAEG IQIASGINKG
TKKVTKTVTS EREVILCAGP FGSPQVLLLS GIGPADQLRE HGIQVRKDLP AVGNNLQDHF
GVSIAHRVPM SHSLLSIEKR PWVFFIHLLY WLVWGTGMLL APVIQVGIFV SSAALDSKGG
LIKEFKIHQN TIPDVEIIPT SYDSSDLDFD KSRGVFSFLC VLARPKSKGS LRLSAPSVDA
PLKVDLNYLS NPEDLIPLRA GLRLALRISE DMRAQGYPLE DWETERPGGD DDASLDKFIR
WRNRTTYHYS STCRMGPRED TPDGGAVVNE QLKVFGIKGL RVADSSVFPW IPCVHLQAPA
VMVAEKCAHM ILNPKPE
//
