P2OX_PENSG
ID P2OX_PENSG Reviewed; 623 AA.
AC Q8J136;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=poxSG;
OS Peniophora sp. (strain SG) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora; unclassified Peniophora.
OX NCBI_TaxID=204723;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Heckmann-Pohl D.M., Bastian S., Rekowski M.J., Giffhorn F.;
RT "Pyranose oxidase of the white-rot fungus Peniophora sp. strain SG: Cloning
RT and characterization of the gene, heterologous expression in Escherichia
RT coli, and properties of the recombinant enzyme.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), TETRAMERIZATION, COFACTOR, AND
RP FAD-BINDING SITE.
RX PubMed=15362852; DOI=10.1021/bi048609q;
RA Bannwarth M., Bastian S., Heckmann-Pohl D.M., Giffhorn F., Schulz G.E.;
RT "Crystal structure of pyranose 2-oxidase from the white-rot fungus
RT Peniophora sp.";
RL Biochemistry 43:11683-11690(2004).
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}.
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:15362852};
CC Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:15362852};
CC -!- SUBUNIT: Homotetramer.
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; AF535193; AAO13382.1; -; mRNA.
DR PDB; 1TZL; X-ray; 2.35 A; A/B/C/D/E/F/G/H=2-623.
DR PDB; 2F5V; X-ray; 1.41 A; A=29-623.
DR PDB; 2F6C; X-ray; 1.84 A; A=29-623.
DR PDBsum; 1TZL; -.
DR PDBsum; 2F5V; -.
DR PDBsum; 2F6C; -.
DR AlphaFoldDB; Q8J136; -.
DR SMR; Q8J136; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR BRENDA; 1.1.3.10; 7263.
DR EvolutionaryTrace; Q8J136; -.
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; FAD; Flavoprotein; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..38
FT /evidence="ECO:0000250"
FT /id="PRO_0000012346"
FT CHAIN 39..623
FT /note="Pyranose 2-oxidase"
FT /id="PRO_0000012347"
FT ACT_SITE 548
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT ACT_SITE 593
FT BINDING 448
FT /ligand="substrate"
FT BINDING 450
FT /ligand="substrate"
FT MOD_RES 167
FT /note="Tele-8alpha-FAD histidine"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2F6C"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1TZL"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 188..206
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2F5V"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:2F5V"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:2F5V"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 308..318
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2F6C"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2F5V"
FT TURN 350..353
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:2F5V"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 406..418
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:2F6C"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:1TZL"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 468..475
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 484..492
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 496..503
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 510..526
FT /evidence="ECO:0007829|PDB:2F5V"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:2F5V"
FT TURN 543..546
FT /evidence="ECO:0007829|PDB:2F5V"
FT TURN 559..563
FT /evidence="ECO:0007829|PDB:2F5V"
FT STRAND 576..580
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:2F5V"
FT HELIX 595..612
FT /evidence="ECO:0007829|PDB:2F5V"
SQ SEQUENCE 623 AA; 69342 MW; 4B7DB64A387F43D5 CRC64;
MSTSSSDPFF NFAKSSFRSA AAQKASASSL PPLPGPDKKV PGMDIKYDVV IVGSGPIGCT
YARELVGAGY KVAMFDIGEI DSGLKIGAHK KNTVEYQKNI DKFVNVIQGQ LMSVSVPVNT
LVVDTLSPTS WQASTFFVRN GSNPEQDPLR NLSGQAVTRV VGGMSTHWTC ATPRFDREQR
PLLVKDDADA DDAEWDRLYT KAESYFQTGT DQFKESIRHN LVLNKLAEEY KGQRDFQQIP
LAATRRSPTF VEWSSANTVF DLQNRPNTDA PEERFNLFPA VACERVVRNA LNSEIESLHI
HDLISGDRFE IKADVYVLTA GAVHNTQLLV NSGFGQLGRP NPTNPPELLP SLGSYITEQS
LVFCQTVMST ELIDSVKSDM TIRGTPGELT YSVTYTPGAS TNKHPDWWNE KVKNHMMQHQ
EDPLPIPFED PEPQVTTLFQ PSHPWHTQIH RDAFSYGAVQ QSIDSRLIVD WRFFGRTEPK
EENKLWFSDK ITDAYNMPQP TFDFRFPAGR TSKEAEDMMT DMCVMSAKIG GFLPGSLPQF
MEPGLVLHLG GTHRMGFDEK EDNCCVNTDS RVFGFKNLFL GGCGNIPTAY GANPTLTAMS
LAIKSCEYIK QNFTPSPFTS EAQ
