P2OX_TRAVE
ID P2OX_TRAVE Reviewed; 623 AA.
AC P79076;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Pyranose 2-oxidase;
DE Short=P2Ox;
DE Short=POD;
DE Short=POx;
DE Short=PROD;
DE Short=Pyranose oxidase;
DE EC=1.1.3.10;
DE AltName: Full=FAD-oxidoreductase;
DE AltName: Full=Glucose 2-oxidase;
DE AltName: Full=Pyranose:oxygen 2-oxidoreductase;
DE Flags: Precursor;
GN Name=P2OX;
OS Trametes versicolor (White-rot fungus) (Coriolus versicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5325;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-63; 92-98; 186-207;
RP 215-225; 378-411; 491-513 AND 611-621, CHARACTERIZATION, AND
RP TETRAMERIZATION.
RC STRAIN=ATCC 62976 / IAM 13013 / NBRC 30340 / FES 1030 / Ps-4a;
RC TISSUE=Mycelium;
RX PubMed=9025322; DOI=10.1016/s0168-1656(96)01618-5;
RA Nishimura I., Okada K., Koyama Y.;
RT "Cloning and expression of pyranose oxidase cDNA from Coriolus versicolor
RT in Escherichia coli.";
RL J. Biotechnol. 52:11-20(1996).
RN [2]
RP FAD-BINDING.
RX AGRICOLA=IND85055664;
RA Machida Y., Nakanishi T.;
RT "Purification and properties of pyranose oxidase from Coriolus
RT versicolor.";
RL Agric. Biol. Chem. 48:2463-2470(1984).
RN [3]
RP FUNCTION.
RX PubMed=16349330; DOI=10.1128/aem.60.7.2524-2532.1994;
RA Daniel G., Volc J., Kubatova E.;
RT "Pyranose oxidase, a major source of H(2)O(2) during wood degradation by
RT Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella
RT mucida.";
RL Appl. Environ. Microbiol. 60:2524-2532(1994).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, TETRAMERIZATION, AND MUTAGENESIS OF GLU-542.
RX DOI=10.1023/A:1005460028591;
RA Masuda-Nishimura I., Minamihara T., Koyama Y.;
RT "Improvement in thermal stability and reactivity of pyranose oxidase from
RT Coriolus versicolor by random mutagenesis.";
RL Biotechnol. Lett. 21:203-207(1999).
CC -!- FUNCTION: Catalyzes the oxidation of various aldopyranoses and
CC disaccharides on carbon-2 to the corresponding 2-keto sugars
CC concomitant with the reduction of O(2) to H(2)O(2). Plays an important
CC role in lignin degradation of wood rot fungi by supplying the essential
CC cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin
CC peroxidase and manganese-dependent peroxidase. The preferred substrate
CC is D-glucose which is converted to 2-dehydro-D-glucose. Acts also on D-
CC xylose, together with D-glucose the major sugars derived from wood, on
CC L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of
CC diabetes mellitus. {ECO:0000269|PubMed:16349330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + O2 = 2-dehydro-D-glucose + H2O2;
CC Xref=Rhea:RHEA:10552, ChEBI:CHEBI:4167, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16609; EC=1.1.3.10;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.2};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for D-glucose {ECO:0000269|Ref.4};
CC KM=35.3 mM for 1,5-anhydro-D-glucitol {ECO:0000269|Ref.4};
CC pH dependence:
CC Optimum pH is about 6.5. Active from pH 5 to 9. Stable from pH 3 to
CC 11. {ECO:0000269|Ref.4};
CC Temperature dependence:
CC Optimum temperature is about 50 degrees Celsius. Active from 30 to 65
CC degrees Celsius. Thermostable for 30 minutes up to 55 degrees
CC Celsius. {ECO:0000269|Ref.4};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Hyphal periplasmic
CC space. {ECO:0000250}.
CC -!- PTM: Not glycosylated.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; D73369; BAA11119.1; -; mRNA.
DR AlphaFoldDB; P79076; -.
DR SMR; P79076; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050233; F:pyranose oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR012814; P2OX.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02462; pyranose_ox; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Periplasm;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000305"
FT PROPEP 28..38
FT /evidence="ECO:0000269|PubMed:9025322"
FT /id="PRO_0000012356"
FT CHAIN 39..623
FT /note="Pyranose 2-oxidase"
FT /id="PRO_0000012357"
FT ACT_SITE 548
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT ACT_SITE 593
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 167
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT MUTAGEN 542
FT /note="E->K: Increases thermostability up to 65 degrees
FT Celsius and enhances pH stability in alkaline solution.
FT Increases the catalytic efficiency 2-fold for D-glucose and
FT 3-fold for 1,5-anhydro-D-glucitol, mainly by lowering the
FT Km values for these two substrates to 0.74 mM and 14.3 mM,
FT respectively."
FT /evidence="ECO:0000269|Ref.4"
SQ SEQUENCE 623 AA; 69495 MW; 5D3FC81B35FA5B54 CRC64;
MSTSSSDPFF NFTKSSFRSA AAQKASATSL PPLPGPDKKV PGMDIKYDVV IVGSGPIGCT
YARELVEAGY KVAMFDIGEI DSGLKIGAHK KNTVEYQKNI DKFVNVIQGQ LMSVSVPVNT
LVIDTLSPTS WQASSFFVRN GSNPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFDREQR
PLLVKDDQDA DDAEWDRLYT KAESYFKTGT DQFKESIRHN LVLNKLAEEY KGQRDFQQIP
LAATRRSPTF VEWSSANTVF DLQNRPNTDA PNERFNLFPA VACERVVRNT SNSEIESLHI
HDLISGDRFE IKADVFVLTA GAVHNAQLLV NSGFGQLGRP DPANPPQLLP SLGSYITEQS
LVFCQTVMST ELIDSVKSDM IIRGNPGDLG YSVTYTPGAE TNKHPDWWNE KVKNHMMQHQ
EDPLPIPFED PEPQVTTLFQ PSHPWHTQIH RDAFSYGAVQ QSIDSRLIVD WRFFGRTEPK
EENKLWFSDK ITDTYNMPQP TFDFRFPAGR TSKEAEDMMT DMCVMSAKIG GFLPGSLPQF
MEPGLVLHLG GTHRMGFDEQ EDKCCVNTDS RVFGFKNLFL GGCGNIPTAY GANPTLTAMS
LAIKSCEYIK NNFTPSPFTD QAE
