ID A0A137QNB4_9AGAR Unreviewed; 755 AA.
AC A0A137QNB4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=pyranose dehydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00013177};
DE EC=1.1.99.29 {ECO:0000256|ARBA:ARBA00013177};
GN ORFNames=AN958_06214 {ECO:0000313|EMBL:KXN88670.1};
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:KXN88670.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN88670.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN88670.1,
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 -!- 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; KQ962129; KXN88670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QNB4; -.
DR STRING; 1714833.A0A137QNB4; -.
DR OrthoDB; 3382025at2759; -.
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; 2.
DR Gene3D; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027424; Glucose_Oxidase_domain_2.
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; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..755
FT /note="pyranose dehydrogenase (acceptor)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007295457"
FT DOMAIN 302..316
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 570..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 81139 MW; 892C570FA4DB9669 CRC64;
MFSGHLNCLL LLSCARIALG VQYFQQPSDL PHDAYDFIIL GGGTAGAVVG ARLGEVSKYR
ILVIEAGPSN QDVFDSQVPG LAMKIGFQTA VDWNYTTVPQ VNVNNAVINY PRAMLLGGCS
SHNQMVYTRG SRDDYDRWAK VTGNDNLSWD KILPYILKAE KLTSPNDPNF PEDGHFDPSY
HSTTGAVSVS AAYYPHPFND LMLNTTNELS KEFPFLLDVN SGRPLGIGWG QTTVEHGFRS
SAATSYIANA RNNVHVLLQT RITRVLPVDK ERRDFRKVEF ATKPEGPRMT LTAKKELILS
AGAMNSPQIL LLSGIGPKAE LEAVGIENIV DNPSVGKNFS EQVALQINFT TSLPVTDFDE
AAALTQWKLN HTGRLGAPLR LPQIGWHRLP ASSEAFKNGS SDPTGGPDAP HVELFFEGIG
APSNSSTGTD GLSVGSLITD VVNLNPASRG SITLSSSSPF DPPKIDPALL GSPLDAAILL
EGVKSLLRLL SSTTFATHIQ GFTSSGPSSN DTEAIINYME HSASHWGHPV GSCAMAPHGA
TWGVVDPDFK LRGLNGLRVV DASVFAEELT SPNDPNFSEE GHFDPSDHGT DGKVSVSAEC
NELRENFPFL PLDVKSGRPI GVGWGQTTIA HGFRSSAATN YLANTSDNVH VLLQTHITRV
LHVNKGRRDS RKVEFTVKPD GHGPRTTLTA KKGLILSAGV MNSPQILLLS GIGPKAELDS
LGIETILDSP SVGKNFRDQL SLPVSFVTSL PATDL
//
