ID K5WJK3_AGABU Unreviewed; 599 AA.
AC K5WJK3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=pyranose dehydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00013177};
DE EC=1.1.99.29 {ECO:0000256|ARBA:ARBA00013177};
GN ORFNames=AGABI1DRAFT_123150 {ECO:0000313|EMBL:EKM75486.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM75486.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
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; JH971412; EKM75486.1; -; Genomic_DNA.
DR RefSeq; XP_007333837.1; XM_007333775.1.
DR AlphaFoldDB; K5WJK3; -.
DR SMR; K5WJK3; -.
DR STRING; 597362.K5WJK3; -.
DR GeneID; 18825969; -.
DR KEGG; abp:AGABI1DRAFT123150; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_3_1; -.
DR InParanoid; K5WJK3; -.
DR OMA; QAATIIM; -.
DR OrthoDB; 601859at2759; -.
DR Proteomes; UP000008493; 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: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:UP000008493};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..599
FT /note="pyranose dehydrogenase (acceptor)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003885643"
FT DOMAIN 41..345
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 454..590
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 534
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 578
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 127..130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 599 AA; 64820 MW; C4A6F36EE720A3E0 CRC64;
MIPRVAKFNF RLLSLALLGI QVARSAITYQ NPTDLPGDVD YDFIVAGGGT AGLVVASRLS
ENPEWNVLVI EAGPSNKDVF ETRVPGLSSE LRPRFDWNYT TIPQDALGGR SLNYSRAKLL
GGCSSHNGMV YTRGSRDDWD NYAEITGDQA LSWDSILPVM KRAEKFSKDS SHKPVKGHID
PSVHGDDGKL SVVASYTNAS FNDLLLETAK ELSGEFPFKL DMNDGRPLGL TWTQYTIDQR
GERSSSATAY LEGTGNNVHV LVNTLVTRIV SAENGTDFRS VEFATDADSP KIQLRAKKEV
IVSGGVINSP QILMNSGIGR REVLGANGID TLVDNPSVGK NLSDQAATII MLDTTLPITD
YDVDAALIEW KKSHTGPLAQ GGRLNHLTWV RLPDDKLDGL DPSSGKNSPH IEFQFGQISH
QLPPSGVPRE APIPSEASID TVLQFAVVNL YTVSRGSISL SNNDPFSHPL IDLNMFGEEI
DPAILREGIR SARRMLSSQA FKGFVGETVF PPSDATSDED LDTFLKTSTV SYVHGVGTLS
MSPQSASWGV VNPDFRVKGT SGLRVVDASV IPFAPAGHTQ EPVYAFAEHA SALIAKSYS
//
