PDH1_AGAXA
ID PDH1_AGAXA Reviewed; 600 AA.
AC V5NC32; Q3L1D2;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Pyranose dehydrogenase {ECO:0000303|PubMed:17227387};
DE Short=PDH {ECO:0000303|PubMed:17227387};
DE EC=1.1.99.29 {ECO:0000269|PubMed:17227387, ECO:0000269|PubMed:24970179};
DE AltName: Full=Pyranose:quinone oxidoreductase 1 {ECO:0000250|UniProtKB:Q3L245};
DE Flags: Precursor;
GN Name=pdh1 {ECO:0000303|PubMed:24970179};
OS Agaricus xanthodermus (Poison yellow meadow mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX NCBI_TaxID=83518;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CCBAS 225;
RX PubMed=24970179; DOI=10.3390/biom3030535;
RA Staudigl P., Krondorfer I., Haltrich D., Peterbauer C.K.;
RT "Pyranose dehydrogenase from Agaricus campestris and Agaricus xanthoderma:
RT Characterization and applications in carbohydrate conversions.";
RL Biomolecules 3:535-552(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-600, PROTEIN SEQUENCE OF 26-35, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR
RP LOCATION, SUBUNIT, GLYCOSYLATION, AND MASS SPECTROMETRY.
RC STRAIN=CCBAS 225;
RX PubMed=17227387; DOI=10.1111/j.1742-4658.2007.05634.x;
RA Kujawa M., Volc J., Halada P., Sedmera P., Divne C., Sygmund C.,
RA Leitner C., Peterbauer C., Haltrich D.;
RT "Properties of pyranose dehydrogenase purified from the litter-degrading
RT fungus Agaricus xanthoderma.";
RL FEBS J. 274:879-894(2007).
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:17227387,
CC ECO:0000269|PubMed:24970179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000269|PubMed:17227387,
CC ECO:0000269|PubMed:24970179};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-3-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000269|PubMed:17227387,
CC ECO:0000269|PubMed:24970179};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2,3-diulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000269|PubMed:17227387,
CC ECO:0000269|PubMed:24970179};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3-ulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000269|PubMed:17227387,
CC ECO:0000269|PubMed:24970179};
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:17227387,
CC ECO:0000269|PubMed:24970179};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17227387};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:17227387};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.78 mM for D-glucose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:17227387};
CC KM=11 mM for D-galactose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:17227387};
CC KM=25 mM for D-xylose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:17227387};
CC KM=17 mM for L-arabinose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:17227387};
CC KM=12 mM for maltose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:17227387};
CC KM=120 mM for lactose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:17227387};
CC KM=100 mM for maltotriose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:17227387};
CC KM=17 mM for gentiobiose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:17227387};
CC KM=1100 uM for 1,4-benzoquinone (at pH 8.0 with D-glucose as
CC substrate) {ECO:0000269|PubMed:17227387};
CC KM=1040 uM for 1,4-benzoquinone (at pH 2.5 with D-glucose as
CC substrate) {ECO:0000269|PubMed:17227387};
CC KM=280 uM for tetrachloro-1,4-benzoquinone (at pH 8.0 with D-glucose
CC as substrate) {ECO:0000269|PubMed:17227387};
CC KM=390 uM for tetrafluoro-1,4-benzoquinone (at pH 9.5 with D-glucose
CC as substrate) {ECO:0000269|PubMed:17227387};
CC KM=120 uM for methyl-1,4-benzoquinone (at pH 7.0 with D-glucose as
CC substrate) {ECO:0000269|PubMed:17227387};
CC KM=180 uM for 2-(hydroxymethyl)-6-methoxy-1,4-benzoquinone (at pH 10
CC with D-glucose as substrate) {ECO:0000269|PubMed:17227387};
CC KM=20 uM for 3,5-di-tert-butyl-1,2-benzoquinone (at pH 4.0 with D-
CC glucose as substrate) {ECO:0000269|PubMed:17227387};
CC KM=1600 uM for 2-chloro-1,4-benzoquinone (at pH 5.5 with D-glucose as
CC substrate) {ECO:0000269|PubMed:17227387};
CC KM=120 uM for ferricenium (at pH 8.5 with D-glucose as substrate)
CC {ECO:0000269|PubMed:17227387};
CC KM=420 uM for dimethylaminomethyl-ferricenium (at pH 8.0 with D-
CC glucose as substrate) {ECO:0000269|PubMed:17227387};
CC KM=330 uM for ferricyanide (at pH 2.0 with D-glucose as substrate)
CC {ECO:0000269|PubMed:17227387};
CC KM=950 uM for CuSO(4)) (at pH 9.5 with D-glucose as substrate)
CC {ECO:0000269|PubMed:17227387};
CC KM=1.7 uM for azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid (ABTS)
CC cation radical (at pH 2.0 with D-glucose as substrate)
CC {ECO:0000269|PubMed:17227387};
CC KM=50 uM for 2,6-dichloroindophenol (DCIP) (at pH 4.0 with D-glucose
CC as substrate) {ECO:0000269|PubMed:17227387};
CC pH dependence:
CC Optimum pH is 7.5-9 with ferricenium ion (Fc(+)) as electron
CC acceptor. Optimum pH values vary between 2 and 10 depending on the
CC electron acceptor (with D-glucose as substrate).
CC {ECO:0000269|PubMed:17227387};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius with ferricenium ion
CC (Fc(+)) as electron acceptor. {ECO:0000269|PubMed:17227387};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17227387}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17227387}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17227387}.
CC -!- MASS SPECTROMETRY: Mass=65400; Method=MALDI; Note=Mass of the N-
CC glycosylated protein.; Evidence={ECO:0000269|PubMed:17227387};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; KF534751; AHA85314.1; -; mRNA.
DR EMBL; AY764147; AAW92123.1; -; mRNA.
DR AlphaFoldDB; V5NC32; -.
DR SMR; V5NC32; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR PRIDE; V5NC32; -.
DR BRENDA; 1.1.99.29; 185.
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 GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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 Carbohydrate metabolism; Direct protein sequencing; FAD; Flavoprotein;
KW Glycoprotein; Oxidoreductase; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:17227387"
FT CHAIN 26..600
FT /note="Pyranose dehydrogenase"
FT /id="PRO_0000431290"
FT ACT_SITE 535
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT ACT_SITE 579
FT /evidence="ECO:0000250|UniProtKB:Q3L245"
FT MOD_RES 127
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q3L245"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 197
FT /note="Y -> H (in Ref. 2; AAW92123)"
FT CONFLICT 441
FT /note="G -> R (in Ref. 2; AAW92123)"
SQ SEQUENCE 600 AA; 65092 MW; 8E4AED8D71417AD6 CRC64;
MFPRVVRLNS RLVSFALLGL QIANGAITYQ HPDDLPSNVN YDFIVAGGGT AGLVVASRLS
ENSDWNILVI EAGPSNKDTP ETRVPGLADS LPGSRTDWNY TTIPQDALGG RSLNYSRAKV
LGGCSTHNGM VYTRGSEDDW NYWAEVTGDQ ALSWDSVLPI MKKAEKFSQD FSDQSVDGHI
DPAVHGRDGL LSVVASYTNV SFNDLLLQTT KELSDEFPFK LDLNDGKPHE LAWTQYTIDH
NAERSSSATS YLETTGDNVH VLVNTHVTRI VSAGNGTNFR SVEFAVDSNS PKKVLQAKKE
LILSAGVIAS PQVLMNSGIG GREELQAIGV DTLIDNPSVG KNLSDQAATL LMFDTTLPNT
DYDVAAALTE WDKSRSGPMA HGARLNHLTW VRLPDDKLNG SDPSSGKDSP HIEFQFRQIS
HQLPPADVPN QVQLPDPDSI GVVLQFSVVN LYSISPGSVI LNDNDPFANP MIDLNMFGDQ
KDIAILREGV RSARRMFSSP AFKDVINGTV YPPADVTSDE DLDAFLRTSA ESYWHGVGTL
SMSPQNASWG VVNPDFRVKG TSGLRVVDAS VIPRAPAGHT QVPVYTFAEH ASVLIAASYH
