PDH1_AGABI
ID PDH1_AGABI Reviewed; 594 AA.
AC Q3L1D1;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Pyranose dehydrogenase {ECO:0000303|PubMed:11086703};
DE Short=PDH {ECO:0000303|PubMed:11086703};
DE EC=1.1.99.29 {ECO:0000269|PubMed:11086703, ECO:0000269|PubMed:9133318, ECO:0000269|Ref.2};
DE AltName: Full=Glucose dehydrogenase {ECO:0000303|Ref.2};
DE Short=GDH {ECO:0000303|Ref.2};
DE AltName: Full=Pyranose 2-dehydrogenase {ECO:0000303|PubMed:9133318};
DE AltName: Full=Pyranose:quinone oxidoreductase {ECO:0000250|UniProtKB:Q3L245};
DE Flags: Precursor;
GN Name=pdh1 {ECO:0000303|Ref.1};
OS Agaricus bisporus (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX NCBI_TaxID=5341;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sygmund C., Fragner D., Halada P., Volc J., Haltrich D., Peterbauer C.K.;
RT "Pyranose dehydrogenase of Agaricus bisporus.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 26-33, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT, AND GLYCOSYLATION.
RC STRAIN=D649;
RX DOI=10.1007/s002530051363;
RA Morrison S.C., Wood D.A., Wood P.M.;
RT "Characterization of a glucose 3-dehydrogenase from the cultivated mushroom
RT (Agaricus bisporus).";
RL Appl. Microbiol. Biotechnol. 51:58-64(1999).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT, AND GLYCOSYLATION.
RC STRAIN=Horst U3;
RX PubMed=9133318; DOI=10.1007/s002030050424;
RA Volc J., Kubatova E., Wood D.A., Daniel G.;
RT "Pyranose 2-dehydrogenase, a novel sugar oxidoreductase from the
RT basidiomycete fungus Agaricus bisporus.";
RL Arch. Microbiol. 167:119-125(1997).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CCBAS 306;
RX PubMed=11086703; DOI=10.1016/s0008-6215(00)00167-1;
RA Volc J., Sedmera P., Halada P., Prikrylova V., Haltrich D.;
RT "Double oxidation of D-xylose to D-glycero-pentos-2,3-diulose (2,3-diketo-
RT D-xylose) by pyranose dehydrogenase from the mushroom Agaricus bisporus.";
RL Carbohydr. Res. 329:219-225(2000).
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:0000269|PubMed:11086703,
CC ECO:0000269|PubMed:9133318, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000269|PubMed:11086703,
CC ECO:0000269|PubMed:9133318, ECO:0000269|Ref.2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-3-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000269|PubMed:11086703,
CC ECO:0000269|PubMed:9133318, ECO:0000269|Ref.2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2,3-diulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000269|PubMed:11086703,
CC ECO:0000269|PubMed:9133318, ECO:0000269|Ref.2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3-ulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000269|PubMed:11086703,
CC ECO:0000269|PubMed:9133318, ECO:0000269|Ref.2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3,4-diulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000269|PubMed:11086703,
CC ECO:0000269|PubMed:9133318, ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:9133318};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:9133318};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.83 mM for D-glucose (with 1,4-benzoquinone as electron acceptor)
CC {ECO:0000269|Ref.2};
CC KM=2.31 mM for D-cellobiose (with 1,4-benzoquinone as electron
CC acceptor) {ECO:0000269|Ref.2};
CC KM=13.8 mM for D-maltose (with 1,4-benzoquinone as electron acceptor)
CC {ECO:0000269|Ref.2};
CC KM=22.4 mM for L-arabinose (with 1,4-benzoquinone as electron
CC acceptor) {ECO:0000269|Ref.2};
CC KM=28 mM for D-xylose (with 1,4-benzoquinone as electron acceptor)
CC {ECO:0000269|Ref.2};
CC KM=26.1 mM for D-galactose (with 1,4-benzoquinone as electron
CC acceptor) {ECO:0000269|Ref.2};
CC KM=12.6 mM for sucrose (with 1,4-benzoquinone as electron acceptor)
CC {ECO:0000269|Ref.2};
CC KM=1.42 mM for 1,4-benzoquinone (with D-glucose as substrate)
CC {ECO:0000269|Ref.2};
CC Vmax=0.589 umol/sec/mg enzyme for D-glucose (with 1,4-benzoquinone as
CC electron acceptor) {ECO:0000269|Ref.2};
CC Vmax=0.563 umol/sec/mg enzyme for D-cellobiose (with 1,4-benzoquinone
CC as electron acceptor) {ECO:0000269|Ref.2};
CC Vmax=0.612 umol/sec/mg enzyme for D-maltose (with 1,4-benzoquinone as
CC electron acceptor) {ECO:0000269|Ref.2};
CC Vmax=0.951 umol/sec/mg enzyme for L-arabinose (with 1,4-benzoquinone
CC as electron acceptor) {ECO:0000269|Ref.2};
CC Vmax=0.797 umol/sec/mg enzyme for D-xylose (with 1,4-benzoquinone as
CC electron acceptor) {ECO:0000269|Ref.2};
CC Vmax=0.576 umol/sec/mg enzyme for D-galactose (with 1,4-benzoquinone
CC as electron acceptor) {ECO:0000269|Ref.2};
CC Vmax=0.235 umol/sec/mg enzyme for sucrose (with 1,4-benzoquinone as
CC electron acceptor) {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 4.5. the enzyme has a second pH optimum at pH 9.
CC {ECO:0000269|Ref.1, ECO:0000269|Ref.2};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9133318, ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9133318,
CC ECO:0000269|Ref.2}. Note=Also found intracellularly in fungal hyphae.
CC {ECO:0000269|PubMed:9133318}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9133318, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
CC -!- CAUTION: Has been originally mistaken for cellobiose dehydrogenase
CC (CDH) due to low activity with cellobiose. {ECO:0000303|Ref.2}.
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DR EMBL; AY764148; AAW92124.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3L1D1; -.
DR SMR; Q3L1D1; -.
DR KEGG; ag:AAW92124; -.
DR BRENDA; 1.1.99.29; 178.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0033718; F:pyranose dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 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; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 26..594
FT /note="Pyranose dehydrogenase"
FT /id="PRO_0000431292"
FT ACT_SITE 529
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT ACT_SITE 573
FT /evidence="ECO:0000250|UniProtKB:Q3L245"
FT MOD_RES 126
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q3L245"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 594 AA; 64527 MW; 0DDD0EF992979A80 CRC64;
MIPRVAKFNF RLLSLALLGI QVARSAITYQ NPTDLPGDVD YDFIVAGGGT AGLVVASRLS
ENPEWNVLVI EAGPSNKDVF ETRVPGLSSE LRPRFDWNYT TIPQDALGGR SLNYSRAKLL
GGCSSHNGMV YTRCSRDDWD NYAEITGNQA FSWDSILPVM KRAEKFSKDS SHKPVKGHID
PSVHGGDGKL SVVASYTNAS FNDLLLETAK ELSGEFPFKL DMNDGRPLGL TWTQYTIDQR
GERSSSATAY LEGTGNNVHV LVNTLVTRIV SAENGTDFRS VEFATDADSP KIQLRAKKEV
IVSGGVINSP QILMNSGIGG REVLGANGID TLVDNPSVGK NLSDQAATII MLDTTLPITD
YDVDAALIEW KKSHTGPLAQ GGRLNHLTWV RLPDDKLDGL DPSSGENSPH IEFQFGQISH
QLPPSGLTRF SFYRHCSPIP PLINLYTVSR GSISLSNNDP FSHPLIDLNM FGEEIDPAIL
REGIRSARRM LSSQAFKGFV GETVFPPSDA TSDEDLDTFL KTSTFSYVHG VGTLSMSPQS
ASWGVVNPDF RVKGTSGLRV VDASVIPFAP AGHTQEPVYA FAEHASVLIA KSYS
