P2OX_PHACH
ID P2OX_PHACH Reviewed; 621 AA.
AC Q6QWR1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Pyranose 2-oxidase;
DE Short=P2O;
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=pox;
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-30; 66-96; 98-150;
RP 182-191; 202-216; 223-229; 236-272; 275-282; 421-444; 458-472 AND 479-517,
RP AND INDUCTION.
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=15466516; DOI=10.1128/aem.70.10.5794-5800.2004;
RA de Koker T.H., Mozuch M.D., Cullen D., Gaskell J., Kersten P.J.;
RT "Isolation and purification of pyranose 2-oxidase from Phanerochaete
RT chrysosporium and characterization of gene structure and regulation.";
RL Appl. Environ. Microbiol. 70:5794-5800(2004).
RN [2]
RP PROTEIN SEQUENCE OF 66-96 AND 366-388, BIOPHYSICOCHEMICAL PROPERTIES,
RP FAD-BINDING, AND TETRAMERIZATION.
RX PubMed=9210340; DOI=10.1007/s002530050964;
RA Artolozaga M.J., Kubatova E., Volc J., Kalisz H.M.;
RT "Pyranose 2-oxidase from Phanerochaete chrysosporium -- further biochemical
RT characterisation.";
RL Appl. Microbiol. Biotechnol. 47:508-514(1997).
RN [3]
RP FUNCTION.
RA Volc J., Kubatova E., Sedmera P., Daniel G., Gabriel J.;
RT "Pyranose oxidase and pyranosone dehydratase: enzymes responsible for
RT conversion of D-glucose to cortalcerone by the basidiomycete Phanerochaete
RT chrysosporium.";
RL Arch. Microbiol. 156:297-301(1991).
RN [4]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=16348809; DOI=10.1128/aem.58.11.3667-3676.1992;
RA Daniel G., Volc J., Kubatova E., Nilsson T.;
RT "Ultrastructural and immunocytochemical studies on the H(2)O(2)-producing
RT enzyme pyranose oxidase in Phanerochaete chrysosporium grown under liquid
RT culture conditions.";
RL Appl. Environ. Microbiol. 58:3667-3676(1992).
RN [5]
RP FUNCTION.
RX PubMed=8661938; DOI=10.1007/s002030050348;
RA Volc J., Kubatova E., Daniel G., Prikrylova V.;
RT "Only C-2 specific glucose oxidase activity is expressed in ligninolytic
RT cultures of the white rot fungus Phanerochaete chrysosporium.";
RL Arch. Microbiol. 165:421-424(1996).
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, an intermediate
CC of a secondary metabolic pathway leading to the antibiotic
CC cortalcerone. Acts also on D-xylose, together with D-glucose the major
CC sugars derived from wood, on L-sorbose, D-galactose and 1,5-
CC anhydroglucitol, a diagnostic marker of diabetes mellitus.
CC {ECO:0000269|PubMed:8661938, ECO:0000269|Ref.3}.
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;
CC Evidence={ECO:0000269|PubMed:9210340};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:9210340};
CC -!- ACTIVITY REGULATION: Inhibited by HgCl(2).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=83.2 uM for O(2) {ECO:0000269|PubMed:9210340};
CC KM=1.43 mM for D-glucose {ECO:0000269|PubMed:9210340};
CC KM=1.53 mM for alpha-D-glucose {ECO:0000269|PubMed:9210340};
CC KM=0.97 mM for beta-D-glucose {ECO:0000269|PubMed:9210340};
CC KM=55 mM for 2-deoxy-D-glucose {ECO:0000269|PubMed:9210340};
CC KM=25 mM for D-xylose {ECO:0000269|PubMed:9210340};
CC KM=108 mM for L-sorbose {ECO:0000269|PubMed:9210340};
CC Vmax=26.64 uM/min/mg enzyme towards O(2)
CC {ECO:0000269|PubMed:9210340};
CC pH dependence:
CC Optimum pH is 8.0-8.5. Active from pH 4.5 to 10. Stable from pH 4 to
CC 11. {ECO:0000269|PubMed:9210340};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. Thermostable for 2 hours
CC up to 70 degrees Celsius. {ECO:0000269|PubMed:9210340};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16348809}.
CC Note=Hyphal periplasmic space.
CC -!- DEVELOPMENTAL STAGE: During autolysis, associated with extracellular
CC slime surrounding lysed hyphae. {ECO:0000269|PubMed:16348809}.
CC -!- INDUCTION: Induced by carbon starvation. {ECO:0000269|PubMed:15466516,
CC ECO:0000269|PubMed:16348809}.
CC -!- PTM: Not glycosylated.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AY522922; AAS93628.1; -; mRNA.
DR PDB; 4MIF; X-ray; 1.80 A; A/B/C/D=1-620.
DR PDB; 4MIG; X-ray; 1.80 A; A/B/C/D=1-621.
DR PDB; 4MIH; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-620.
DR PDBsum; 4MIF; -.
DR PDBsum; 4MIG; -.
DR PDBsum; 4MIH; -.
DR AlphaFoldDB; Q6QWR1; -.
DR SMR; Q6QWR1; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR CLAE; POX3A_PHACH; -.
DR PRIDE; Q6QWR1; -.
DR VEuPathDB; FungiDB:AGR57_3659; -.
DR OMA; QFMAPGL; -.
DR BRENDA; 1.1.3.10; 1380.
DR SABIO-RK; Q6QWR1; -.
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 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW Periplasm.
FT PROPEP 1..9
FT /evidence="ECO:0000269|PubMed:15466516"
FT /id="PRO_0000012348"
FT CHAIN 10..621
FT /note="Pyranose 2-oxidase"
FT /id="PRO_0000012349"
FT ACT_SITE 553
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT ACT_SITE 596
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250"
FT CONFLICT 78
FT /note="H -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="K -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4MIF"
FT TURN 59..63
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:4MIH"
FT HELIX 186..204
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4MIF"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 215..229
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 299..306
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:4MIF"
FT TURN 377..380
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 388..396
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:4MIG"
FT HELIX 412..424
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:4MIH"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 490..498
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 504..509
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 514..531
FT /evidence="ECO:0007829|PDB:4MIF"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:4MIF"
FT TURN 548..551
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:4MIF"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:4MIF"
FT HELIX 598..616
FT /evidence="ECO:0007829|PDB:4MIF"
SQ SEQUENCE 621 AA; 69298 MW; 08A1C1264D824A4C CRC64;
MFLDTTPFRA DEPYDVFIAG SGPIGATFAK LCVDANLRVC MVEIGAADSF TSKPMKGDPN
APRSVQFGPG QVPIPGYHKK NEIEYQKDID RFVNVIKGAL STCSIPTSNN HIATLDPSVV
SNSLDKPFIS LGKNPAQNPF VNLGAEAVTR GVGGMSTHWT CATPEFFAPA DFNAPHRERP
KLSTDAAEDA RIWKDLYAQA KEIIGTSTTE FDHSIRHNLV LRKYNDIFQK ENVIREFSPL
PLACHRLTDP DYVEWHATDR ILEELFTDPV KRGRFTLLTN HRCTKLVFKH YRPGEENEVD
YALVEDLLPH MQNPGNPASV KKIYARSYVV ACGAVATAQV LANSHIPPDD VVIPFPGGEK
GSGGGERDAT IPTPLMPMLG KYITEQPMTF CQVVLDSSLM EVVRNPPWPG LDWWKEKVAR
HVEAFPNDPI PIPFRDPEPQ VTIKFTEEHP WHVQIHRDAF SYGAVAENMD TRVIVDYRFF
GYTEPQEANE LVFQQHYRDA YDMPQPTFKF TMSQDDRARA RRMMDDMCNI ALKIGGYLPG
SEPQFMTPGL ALHLAGTTRC GLDTQKTVGN THCKVHNFNN LYVGGNGVIE TGFAANPTLT
SICYAIRASN DIIAKFGRHR G
