Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei448Substrate1
Binding sitei450Substrate1
Active sitei548Proton acceptorBy similarity1
Active sitei5931

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.1.3.10. 7263.

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000001234629 – 38By similarity10
ChainiPRO_000001234739 – 623Pyranose 2-oxidaseAdd BLAST585

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei167Tele-8alpha-FAD histidine1

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1623
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi45 – 52Combined sources8
Helixi56 – 67Combined sources12
Beta strandi71 – 75Combined sources5
Beta strandi77 – 79Combined sources3
Beta strandi82 – 85Combined sources4
Helixi94 – 98Combined sources5
Helixi100 – 102Combined sources3
Helixi103 – 109Combined sources7
Beta strandi112 – 114Combined sources3
Helixi148 – 150Combined sources3
Helixi163 – 166Combined sources4
Helixi177 – 179Combined sources3
Beta strandi183 – 186Combined sources4
Helixi188 – 206Combined sources19
Beta strandi208 – 210Combined sources3
Turni212 – 215Combined sources4
Helixi217 – 229Combined sources13
Turni230 – 232Combined sources3
Beta strandi241 – 247Combined sources7
Beta strandi250 – 253Combined sources4
Helixi256 – 259Combined sources4
Beta strandi265 – 267Combined sources3
Beta strandi270 – 278Combined sources9
Beta strandi280 – 288Combined sources9
Beta strandi295 – 302Combined sources8
Turni303 – 305Combined sources3
Beta strandi308 – 318Combined sources11
Helixi322 – 331Combined sources10
Beta strandi342 – 344Combined sources3
Beta strandi347 – 349Combined sources3
Turni350 – 353Combined sources4
Beta strandi361 – 368Combined sources8
Helixi370 – 376Combined sources7
Turni377 – 379Combined sources3
Beta strandi381 – 384Combined sources4
Beta strandi392 – 394Combined sources3
Helixi406 – 418Combined sources13
Beta strandi434 – 436Combined sources3
Beta strandi445 – 450Combined sources6
Beta strandi453 – 455Combined sources3
Beta strandi458 – 460Combined sources3
Helixi465 – 467Combined sources3
Beta strandi468 – 475Combined sources8
Beta strandi484 – 492Combined sources9
Beta strandi496 – 503Combined sources8
Helixi510 – 526Combined sources17
Turni527 – 529Combined sources3
Beta strandi530 – 532Combined sources3
Beta strandi538 – 540Combined sources3
Turni543 – 546Combined sources4
Turni559 – 563Combined sources5
Beta strandi576 – 580Combined sources5
Helixi583 – 585Combined sources3
Helixi595 – 612Combined sources18

3D structure databases

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

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.

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...

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: November 2, 2016
This is version 71 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.