P2OX_TRAPU
ID P2OX_TRAPU Reviewed; 622 AA.
AC Q5G234;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
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; Synonyms=p2o;
OS Trametes pubescens (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=154538;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=CBS 696.94;
RX PubMed=16105703; DOI=10.1016/j.jbiotec.2005.06.021;
RA Maresova H., Vecerek B., Hradska M., Libessart N., Becka S., Saniez M.-H.,
RA Kyslik P.;
RT "Expression of the pyranose 2-oxidase from Trametes pubescens in
RT Escherichia coli and characterization of the recombinant enzyme.";
RL J. Biotechnol. 120:387-395(2005).
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 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:16105703}.
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:0000250};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=133 mM for L-arabinose (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16105703};
CC KM=9.91 mM for D-galactose (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16105703};
CC KM=1.31 mM for D-glucose (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16105703};
CC KM=157 mM for melibiose (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16105703};
CC KM=123 mM for ribose (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16105703};
CC KM=75.4 mM for L-sorbose (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16105703};
CC KM=36.2 mM for D-xylose (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:16105703};
CC Vmax=0.08 umol/min/mg enzyme toward L-arabinose (at pH 6.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:16105703};
CC Vmax=1.52 umol/min/mg enzyme toward D-galactose (at pH 6.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:16105703};
CC Vmax=9.32 umol/min/mg enzyme toward D-glucose (at pH 6.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:16105703};
CC Vmax=1.30 umol/min/mg enzyme toward melibiose (at pH 6.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:16105703};
CC Vmax=0.01 umol/min/mg enzyme toward ribose (at pH 6.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:16105703};
CC Vmax=12.50 umol/min/mg enzyme toward L-sorbose (at pH 6.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:16105703};
CC Vmax=4.02 umol/min/mg enzyme toward D-xylose (at pH 6.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:16105703};
CC pH dependence:
CC Optimum pH is 5.5-6.5. {ECO:0000269|PubMed:16105703};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Note=Hyphal periplasmic
CC space. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AY863215; AAW57304.1; -; mRNA.
DR AlphaFoldDB; Q5G234; -.
DR SMR; Q5G234; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR BRENDA; 1.1.3.10; 6420.
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 FAD; Flavoprotein; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT PROPEP 29..38
FT /evidence="ECO:0000250"
FT /id="PRO_0000012354"
FT CHAIN 39..622
FT /note="Pyranose 2-oxidase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012355"
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"
SQ SEQUENCE 622 AA; 69214 MW; 48B91FB6304D3FC4 CRC64;
MSTSSSDPFY NFAKTSFKSA AAQKASATSL PPLPGPDQKV PGMDIKYDVV IVGSGPIGCT
YARELVEAGY KVAMFDIGEI DSGLKIGAHK KNTVEYQKNI DKFVNVIQGQ LMSVSVPVNK
LVVDTLSPTS WQASTFFVRN GSNPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFDREQR
PLLVKDDPDA DDAIWDQLYT KAESYFKTGT DQFNESIRHN LVLNKLAEEY KGQRTFQQIP
LAATRRNPTF VEWSSANTVF DLQNRPNIDA PEERFNLFPA VACERVMRNA SNTAIESLHI
RDLISGDRFA IQADVYVLTA GAVHNTQLLV NSGFGKLGRP DPANPPELLP FLGSYITEQS
LVFCQTVMST ELIDSVKSDM TIIGNPGELG YSVSYMPGAS TNKHPDWWNE KVQNHMMQHQ
EDPLPIPFED PEPQVTTLFQ PSHPWHTQIH RDAFSYGAVQ QSIDSRLIVD WRFFGRTEPK
EENKLWFSDK ITDAYNMPQP TFDFRFPAGR TSQEAEDMMT DMCVMSAKIG GFLPGSLPQF
MEPGLVLHLG GTHRMGFDEQ EDNCCVDTDS RVFGFNNLFL GGCGNIPTAY GANPTLTAMS
LAIKSCEYIK KNFTPSPFTP AQ
