ID K5XMZ8_AGABU Unreviewed; 525 AA.
AC K5XMZ8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=pyranose dehydrogenase (acceptor) {ECO:0000256|ARBA:ARBA00013177};
DE EC=1.1.99.29 {ECO:0000256|ARBA:ARBA00013177};
GN ORFNames=AGABI1DRAFT_63835 {ECO:0000313|EMBL:EKM75995.1};
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:EKM75995.1, 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; JH971406; EKM75995.1; -; Genomic_DNA.
DR RefSeq; XP_007333329.1; XM_007333267.1.
DR AlphaFoldDB; K5XMZ8; -.
DR GeneID; 18830462; -.
DR KEGG; abp:AGABI1DRAFT63835; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_3_1; -.
DR InParanoid; K5XMZ8; -.
DR OMA; CAVHSSI; -.
DR OrthoDB; 3215324at2759; -.
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; 2.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
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; 2.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR PRINTS; PR00411; PNDRDTASEI.
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|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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..525
FT /note="pyranose dehydrogenase (acceptor)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003886570"
FT DOMAIN 238..252
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 460
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 504
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 525 AA; 56713 MW; E0A34A7BD7B45294 CRC64;
MLASLATLLA LTSLGICAVH SSIKEVPNLN WDFVIVGGGT AGCVLANRLT EISRFNVLLI
EAGPTNEGVM DSIVPALQAG TVRSRVDWNF TVTPQQGLNG RSFPYQRGHV LGGSSSVNGL
FYTRGSSSDF DRFARVTEDP GWSWDQLQTY IKKSEKFEHP ADDHDTSEQF DPNIHGFSGN
VAVTLPGFIH PPVDSATLQA ARQLEQDFRF NLDMNSGSPL GIDSIQVSAS KEVILSSGAI
NTPHILLHSG IGDQSDLETL GIPVLLHNPD VGRNLSDHPF FVTTYNVVPG SIDLGPWANL
GFNSTLQAEA LDLWEKNRTG PFVALLSSDH VAWTRLPDDS PLFKEFPDSS SGPNSPHIEL
VLGAAGTVYA VGVNLVSPVS RGSLKIRSNN PFDNPLIDLG IFNSDFDLFT AREAVKTSLR
FSQAPFWKDI LMDINPPFSS SMTDNEIEAV LKNVTSSALH SVSTAAMSPR NADWGVVDPD
LLVKGVSGLR IVDASVMPFV PAAHTQAPVY IIAERAADMI KAKWN
//
