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Protein

Pyranose 2-oxidase

Gene

p2ox

Organism
Peniophora sp. (strain SG) (White-rot fungus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O2 to H2O2. Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H2O2 for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase (By similarity).By similarity

Catalytic activityi

D-glucose + O2 = 2-dehydro-D-glucose + H2O2.

Cofactori

FAD1 PublicationNote: Binds 1 FAD covalently per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei448 – 4481Substrate
Binding sitei450 – 4501Substrate
Active sitei548 – 5481Proton acceptorBy similarity
Active sitei593 – 5931

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.1.3.10. 7263.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyranose 2-oxidase (EC:1.1.3.10)
Short name:
P2Ox
Short name:
POD
Short name:
POx
Short name:
PROD
Short name:
Pyranose oxidase
Alternative name(s):
FAD-oxidoreductase
Glucose 2-oxidase
Pyranose:oxygen 2-oxidoreductase
Gene namesi
Name:p2ox
Synonyms:poxSG
OrganismiPeniophora sp. (strain SG) (White-rot fungus)
Taxonomic identifieri204723 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesRussulalesPeniophoraceaePeniophora

Subcellular locationi

  • Periplasm By similarity

  • Note: Hyphal periplasmic space.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Propeptidei29 – 3810By similarityPRO_0000012346
Chaini39 – 623585Pyranose 2-oxidasePRO_0000012347Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei167 – 1671Tele-8alpha-FAD histidine

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
623
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 528Combined sources
Helixi56 – 6712Combined sources
Beta strandi71 – 755Combined sources
Beta strandi77 – 793Combined sources
Beta strandi82 – 854Combined sources
Helixi94 – 985Combined sources
Helixi100 – 1023Combined sources
Helixi103 – 1097Combined sources
Beta strandi112 – 1143Combined sources
Helixi148 – 1503Combined sources
Helixi163 – 1664Combined sources
Helixi177 – 1793Combined sources
Beta strandi183 – 1864Combined sources
Helixi188 – 20619Combined sources
Beta strandi208 – 2103Combined sources
Turni212 – 2154Combined sources
Helixi217 – 22913Combined sources
Turni230 – 2323Combined sources
Beta strandi241 – 2477Combined sources
Beta strandi250 – 2534Combined sources
Helixi256 – 2594Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi270 – 2789Combined sources
Beta strandi280 – 2889Combined sources
Beta strandi295 – 3028Combined sources
Turni303 – 3053Combined sources
Beta strandi308 – 31811Combined sources
Helixi322 – 33110Combined sources
Beta strandi342 – 3443Combined sources
Beta strandi347 – 3493Combined sources
Turni350 – 3534Combined sources
Beta strandi361 – 3688Combined sources
Helixi370 – 3767Combined sources
Turni377 – 3793Combined sources
Beta strandi381 – 3844Combined sources
Beta strandi392 – 3943Combined sources
Helixi406 – 41813Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi445 – 4506Combined sources
Beta strandi453 – 4553Combined sources
Beta strandi458 – 4603Combined sources
Helixi465 – 4673Combined sources
Beta strandi468 – 4758Combined sources
Beta strandi484 – 4929Combined sources
Beta strandi496 – 5038Combined sources
Helixi510 – 52617Combined sources
Turni527 – 5293Combined sources
Beta strandi530 – 5323Combined sources
Beta strandi538 – 5403Combined sources
Turni543 – 5464Combined sources
Turni559 – 5635Combined sources
Beta strandi576 – 5805Combined sources
Helixi583 – 5853Combined sources
Helixi595 – 61218Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TZLX-ray2.35A/B/C/D/E/F/G/H2-623[»]
2F5VX-ray1.41A29-623[»]
2F6CX-ray1.84A29-623[»]
ProteinModelPortaliQ8J136.
SMRiQ8J136. Positions 43-619.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8J136.

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR007867. GMC_OxRtase_C.
IPR012814. P2OX.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR02462. pyranose_ox. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8J136-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSSSDPFF NFAKSSFRSA AAQKASASSL PPLPGPDKKV PGMDIKYDVV
60 70 80 90 100
IVGSGPIGCT YARELVGAGY KVAMFDIGEI DSGLKIGAHK KNTVEYQKNI
110 120 130 140 150
DKFVNVIQGQ LMSVSVPVNT LVVDTLSPTS WQASTFFVRN GSNPEQDPLR
160 170 180 190 200
NLSGQAVTRV VGGMSTHWTC ATPRFDREQR PLLVKDDADA DDAEWDRLYT
210 220 230 240 250
KAESYFQTGT DQFKESIRHN LVLNKLAEEY KGQRDFQQIP LAATRRSPTF
260 270 280 290 300
VEWSSANTVF DLQNRPNTDA PEERFNLFPA VACERVVRNA LNSEIESLHI
310 320 330 340 350
HDLISGDRFE IKADVYVLTA GAVHNTQLLV NSGFGQLGRP NPTNPPELLP
360 370 380 390 400
SLGSYITEQS LVFCQTVMST ELIDSVKSDM TIRGTPGELT YSVTYTPGAS
410 420 430 440 450
TNKHPDWWNE KVKNHMMQHQ EDPLPIPFED PEPQVTTLFQ PSHPWHTQIH
460 470 480 490 500
RDAFSYGAVQ QSIDSRLIVD WRFFGRTEPK EENKLWFSDK ITDAYNMPQP
510 520 530 540 550
TFDFRFPAGR TSKEAEDMMT DMCVMSAKIG GFLPGSLPQF MEPGLVLHLG
560 570 580 590 600
GTHRMGFDEK EDNCCVNTDS RVFGFKNLFL GGCGNIPTAY GANPTLTAMS
610 620
LAIKSCEYIK QNFTPSPFTS EAQ
Length:623
Mass (Da):69,342
Last modified:March 1, 2003 - v1
Checksum:i4B7DB64A387F43D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF535193 mRNA. Translation: AAO13382.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF535193 mRNA. Translation: AAO13382.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TZLX-ray2.35A/B/C/D/E/F/G/H2-623[»]
2F5VX-ray1.41A29-623[»]
2F6CX-ray1.84A29-623[»]
ProteinModelPortaliQ8J136.
SMRiQ8J136. Positions 43-619.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.3.10. 7263.

Miscellaneous databases

EvolutionaryTraceiQ8J136.

Family and domain databases

Gene3Di3.50.50.60. 4 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR007867. GMC_OxRtase_C.
IPR012814. P2OX.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR02462. pyranose_ox. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Pyranose oxidase of the white-rot fungus Peniophora sp. strain SG: Cloning and characterization of the gene, heterologous expression in Escherichia coli, and properties of the recombinant enzyme."
    Heckmann-Pohl D.M., Bastian S., Rekowski M.J., Giffhorn F.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp."
    Bannwarth M., Bastian S., Heckmann-Pohl D.M., Giffhorn F., Schulz G.E.
    Biochemistry 43:11683-11690(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), TETRAMERIZATION, COFACTOR, FAD-BINDING SITE.

Entry informationi

Entry nameiP2OX_PENSG
AccessioniPrimary (citable) accession number: Q8J136
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: March 16, 2016
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.