PDH3_LEUMG
ID PDH3_LEUMG Reviewed; 600 AA.
AC Q0R4L2;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Pyranose dehydrogenase 3 {ECO:0000303|PubMed:18097667};
DE Short=PDH 3 {ECO:0000303|PubMed:18097667};
DE EC=1.1.99.29 {ECO:0000250|UniProtKB:Q3L245};
DE AltName: Full=Pyranose:quinone oxidoreductase 3 {ECO:0000250|UniProtKB:Q3L245};
DE Flags: Precursor;
GN Name=pdh3 {ECO:0000303|PubMed:18097667};
OS Leucoagaricus meleagris (Western flat-topped agaric) (Agaricus meleagris).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=201219;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INDUCTION.
RC STRAIN=CCBAS 907;
RX PubMed=18097667; DOI=10.1007/s00294-007-0171-9;
RA Kittl R., Sygmund C., Halada P., Volc J., Divne C., Haltrich D.,
RA Peterbauer C.K.;
RT "Molecular cloning of three pyranose dehydrogenase-encoding genes from
RT Agaricus meleagris and analysis of their expression by real-time RT-PCR.";
RL Curr. Genet. 53:117-127(2008).
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 (By similarity). {ECO:0000250|UniProtKB:Q3L245}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000250|UniProtKB:Q3L245};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-3-ulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000250|UniProtKB:Q3L245};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyranose + acceptor = pyranos-2,3-diulose + reduced acceptor.;
CC EC=1.1.99.29; Evidence={ECO:0000250|UniProtKB:Q3L245};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3-ulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000250|UniProtKB:Q3L245};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyranoside + acceptor = a pyranosid-3,4-diulose + reduced
CC acceptor.; EC=1.1.99.29; Evidence={ECO:0000250|UniProtKB:Q3L245};
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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q3L245}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q3L245}.
CC -!- INDUCTION: Constitutively expressed, but on a much lower level than
CC phd1 (only 4.8% of the amount of transcript).
CC {ECO:0000269|PubMed:18097667}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q3L245}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; DQ117577; AAZ94874.1; -; Genomic_DNA.
DR EMBL; DQ117578; AAZ94875.1; -; mRNA.
DR AlphaFoldDB; Q0R4L2; -.
DR SMR; Q0R4L2; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR BRENDA; 1.1.99.29; 7355.
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 2: Evidence at transcript level;
KW Carbohydrate metabolism; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250|UniProtKB:Q3L245"
FT CHAIN 26..600
FT /note="Pyranose dehydrogenase 3"
FT /id="PRO_0000431289"
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 173
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"
SQ SEQUENCE 600 AA; 65036 MW; 8196B13298CC0BDD CRC64;
MLPRVARLNT HLVSLALLGF QITYGAITYQ HPDDLPSDVD YDFIVAGGGT AGLVVASRLS
ENPDWNILVI EAGPSNKDAP ETRVPGLAGS LPASRTDWNY TTIPQDALGG RSLNYSRAKV
LGGCSSHNSM VYTRGSKDDW NHWADITGDQ GLSWDSILPV MKKAEKFSKD FSNQSVDGHI
DPSMHGHDGL LSVVSSYTNV SFNDLLLETT KELSDEFPFK LDLNDGNPHG LAWTQYTIDH
RAERSSSATS YLESTRDNVH VLVNSRVTRI FSAGNGTDFR SVEFAVDANS PKKVLTAKKE
VILSAGVIAS PQVLMNSGIG GREELQAIGV DTLIDNPSVG KNLSDQAATL LMFDTTLPNT
DYDVAAALTE WEDSRSGPMA YGARLNHLTW VRLLDDKLNG SDPSSGKNSP HIEFQFMQIS
HQLPPADAPN QVKLPDPDSI GAVLLLAVVN LYSVSHGSII LNDNDPFANP MIDLNMFGDQ
KDIAILREGV RSARRMFSSQ AFKDVVNGTV YPPADVTSDE DLDAFLRTSA ISYWHGVGTL
SMSPQNASWG VVDPDFRVKG TSGLRVVDAS VIPYAPAGHT QVPVYTFAEH ASVLIAKSYA
