PDH1_AGACM
ID PDH1_AGACM Reviewed; 595 AA.
AC V5NDL4;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Pyranose dehydrogenase {ECO:0000303|PubMed:24970179};
DE Short=PDH {ECO:0000303|PubMed:24970179};
DE EC=1.1.99.29 {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 campestris (Field mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX NCBI_TaxID=56157;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND GLYCOSYLATION.
RC STRAIN=CCBAS 20649;
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).
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:24970179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={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:24970179};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2,3-diulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={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: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:24970179};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q3L245};
CC Note=Binds 1 FAD covalently per subunit.
CC {ECO:0000250|UniProtKB:Q3L245};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.35 mM for D-glucose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:24970179};
CC KM=7.13 mM for D-galactose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:24970179};
CC KM=4.19 mM for D-xylose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:24970179};
CC KM=4.23 mM for L-arabinose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:24970179};
CC KM=53.16 mM for lactose (with ferricenium ion (Fc(+)) as electron
CC acceptor) {ECO:0000269|PubMed:24970179};
CC KM=1.19 mM for ferricenium (at pH 8.5 with D-glucose as substrate)
CC {ECO:0000269|PubMed:24970179};
CC KM=0.12 mM for 1,4-benzoquinone (at pH 4.0 with D-glucose as
CC substrate) {ECO:0000269|PubMed:24970179};
CC KM=0.11 uM for 2,6-dichloroindophenol (DCIP) (at pH 4.0 with D-
CC glucose as substrate) {ECO:0000269|PubMed:24970179};
CC pH dependence:
CC Optimum pH is 8.5 with ferricenium ion (Fc(+)) and 7.0 with 1,4-
CC benzoquinone as electron acceptor, respectively.
CC {ECO:0000269|PubMed:24970179};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24970179}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3L245}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:24970179}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; KF534750; AHA85313.1; -; mRNA.
DR AlphaFoldDB; V5NDL4; -.
DR SMR; V5NDL4; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR BRENDA; 1.1.99.29; 179.
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; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..595
FT /note="Pyranose dehydrogenase"
FT /id="PRO_0000431291"
FT ACT_SITE 530
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT ACT_SITE 574
FT /evidence="ECO:0000250|UniProtKB:Q3L245"
FT MOD_RES 123
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q3L245"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 595 AA; 64241 MW; 014BA9A338C38946 CRC64;
MARFNARLFS IAILGFQVAR SAITYQHPDD LPGDVDYDFI VAGGGTAGLV VASRLGENSK
WNVLVIEAGP SNKDVFATRV PGLAETLPTS HIDWNYTTVP QQALGGRSLN YSRAMILGGC
STHNGMVYTR GSKDDWNKWA DVTGNRDLSW DSILPIMKKV EKFSEDFSDQ SVEGHIDPSV
HGNDGKLSVV ASYTNVSFND LLLETTKELV DEFPFKLDMN DGNPVGLTWN QYTIDHNAER
SSSATAYLES TGDNVHVLLN TRVTRIVPTG KTNFRTVEFA VDAGGPRKQL TAKKEVILSG
GFIASPQILM NSGIGDQEAL KAVGVDTLVN NPSVGKNVSD QAATLVLFDT TLPNTDFDVD
AAIVEWNNSH AGPLATGAPL NHLIWVRLSD DKLSGSDPSS GKDSPHIEFQ FSKISHRIPP
ANVPNQVALP SQDSIGVVIQ FSVVNLNSIS RGSVSLNDNN PFSHPLIDLN MLGEEQDIAI
LREGVHSARR MLSSEAFKPF VNGSVHPPAN ITSDEDLDAF LHTTTKSYLH GVGTLSMSPQ
NASWGVVDPD FRVKGTTGLR VVDASVIPSV PAGHTQTPVY AFAEYASIVI AKSYN
