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PDH2_LEUMG
ID   PDH2_LEUMG              Reviewed;         600 AA.
AC   Q3L243;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Pyranose dehydrogenase 2 {ECO:0000303|PubMed:18097667};
DE            Short=PDH 2 {ECO:0000303|PubMed:18097667};
DE            EC=1.1.99.29 {ECO:0000250|UniProtKB:Q3L245};
DE   AltName: Full=Pyranose:quinone oxidoreductase 2 {ECO:0000250|UniProtKB:Q3L245};
DE   Flags: Precursor;
GN   Name=pdh2 {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 0.2% 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; AY753308; AAW82998.1; -; Genomic_DNA.
DR   EMBL; AY753309; AAW82999.1; -; mRNA.
DR   AlphaFoldDB; Q3L243; -.
DR   SMR; Q3L243; -.
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 2"
FT                   /id="PRO_0000431288"
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"
SQ   SEQUENCE   600 AA;  65163 MW;  74077B81B1800BFD CRC64;
     MLSRVAKLNS RLVSLALLGS QIAFGAITYQ HPDDLPSGVD YDFIVAGGGT AGLVVASRLS
     ENSKWNVLVI EAGPSNKDTP ETRIPGLADN LPGTRTDWNY TTIPQDALGG RSLNYSRAKV
     LGGCSTHNGM VYTRGPRDDW NYWAEITDNQ ALKWDNVLPI MKNTEKFSQD FLDQSMEGHI
     DPSVHGFDGM LSVVASYTNV SFNNLLLETT RELSDEFPFK LDLNDGKPHG LAWTQYTIDQ
     GAERSSSATS YLESTGDNVH VLVNTHVTRI VSAGNETDFR SVEFAVDANS PKKVLTAKKE
     LILSAGVIAS PQILMNSGIG GREELQAIGV DTLIDNPSVG RNLSDQASTL LMFDTTLPNT
     DYDVAAALTE WDNSRSGPMA YAARLNHLTW VRLPDDKLSG SDPSSGHDSP HIEFQFRQIS
     HQLPPADVPN QVQLPDPDSI GVVLQFSVVN LYSISLGSVT LNNNDPFADP IIDLNMFGDQ
     KDIAILREGV RSARRMFSSQ AFKNVVHETV YPPAGVTSDE DLDAFLRTSA VSYLHGVGTL
     SMSPHSASWG VVNPDFRVKG TTGLRVVDAS VIPRAPAGHT QIPVYTFAEH ASALIADSYN
 
 
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