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Protein
Submitted name:

Pyranose 2-oxidase

Gene

p2o

Organism
Trametes ochracea (White-rot fungus) (Trametes multicolor)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei201GlucoseCombined sources1
Binding sitei205GlucoseCombined sources1
Binding sitei283FAD cofactor analog; via amide nitrogen and carbonyl oxygenCombined sources1
Binding sitei283FAD; via amide nitrogen and carbonyl oxygenCombined sources1
Binding sitei472FAD cofactor analogCombined sources1
Binding sitei548FAD cofactor analogCombined sources1
Binding sitei595FADCombined sources1
Binding sitei610GlucoseCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi56 – 57FADCombined sources2
Nucleotide bindingi56 – 57FAD cofactor analogCombined sources2
Nucleotide bindingi76 – 77FADCombined sources2
Nucleotide bindingi76 – 77FAD cofactor analogCombined sources2
Nucleotide bindingi158 – 171FADCombined sourcesAdd BLAST14
Nucleotide bindingi160 – 164FAD cofactor analogCombined sources5
Nucleotide bindingi169 – 171FAD cofactor analogCombined sources3
Nucleotide bindingi593 – 595FAD cofactor analogCombined sources3

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseImported

Keywords - Ligandi

FADCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BRENDAi1.1.3.10. 1627.
SABIO-RKQ7ZA32.

Names & Taxonomyi

Protein namesi
Submitted name:
Pyranose 2-oxidaseImported (EC:1.1.3.10Imported)
Submitted name:
Pyranose oxidaseImported
Gene namesi
Name:p2oImported
OrganismiTrametes ochracea (White-rot fungus) (Trametes multicolor)Imported
Taxonomic identifieri230624 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesTrametes

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TT0X-ray1.80A/B/C/D1-623[»]
2IGKX-ray1.80A/B/C/D/E/F/G/H1-623[»]
2IGMX-ray1.90A/B/C/D/E/F/G/H1-623[»]
2IGNX-ray1.65A/B/C/D/E/F/G/H1-623[»]
2IGOX-ray1.95A/B/C/D/E/F/G/H1-623[»]
3BG6X-ray1.70A/B/C/D/E/F/G/H1-623[»]
3BG7X-ray2.10A/B/C/D/E/F/G/H1-623[»]
3BLYX-ray1.90A1-623[»]
3FDYX-ray1.55A1-623[»]
3K4BX-ray1.90A1-623[»]
3K4CX-ray1.70A/B/C/D1-623[»]
3K4JX-ray2.00A1-623[»]
3K4KX-ray1.60A1-623[»]
3K4LX-ray1.75A/B1-623[»]
3K4MX-ray2.20A/B/C/D/E/F/G/H1-623[»]
3K4NX-ray2.75A/B1-623[»]
3LSHX-ray1.90A/B/C/D1-623[»]
3LSIX-ray1.90A/B1-623[»]
3LSKX-ray1.95A/B/C/D1-623[»]
3LSMX-ray1.70A/B1-623[»]
3PL8X-ray1.35A1-623[»]
4MOEX-ray2.00A/B/C/D1-622[»]
4MOFX-ray1.85A1-622[»]
4MOGX-ray2.00A1-622[»]
4MOHX-ray2.10A1-622[»]
4MOIX-ray1.90A/B1-622[»]
4MOJX-ray2.00A/B/C/D3-622[»]
4MOKX-ray1.90A/B/C/D1-622[»]
4MOLX-ray2.00A/B/C/D1-622[»]
4MOMX-ray1.90A/B/C/D3-622[»]
4MOOX-ray1.65A1-622[»]
4MOPX-ray2.30A/B/C/D3-622[»]
4MOQX-ray1.60A/B1-622[»]
4MORX-ray1.50A/B/C/D3-622[»]
4MOSX-ray1.80A1-622[»]
ProteinModelPortaliQ7ZA32.
SMRiQ7ZA32.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini546 – 604GMC_oxred_CInterPro annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni63 – 64Glucose bindingCombined sources2

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.

Q7ZA32-1 [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 LVLNKLTEEY KGQRDFQQIP LAATRRSPTF
260 270 280 290 300
VEWSSANTVF DLQNRPNTDA PEERFNLFPA VACERVVRNA LNSEIESLHI
310 320 330 340 350
HDLISGDRFE IKADVYVLTA GAVHNTQLLV NSGFGQLGRP NPANPPELLP
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:October 1, 2003 - v1
Checksum:iBD9B91CCAD0FF8D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY291124 mRNA. Translation: AAP40332.1.
AY753305 Genomic DNA. Translation: AAX09279.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY291124 mRNA. Translation: AAP40332.1.
AY753305 Genomic DNA. Translation: AAX09279.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TT0X-ray1.80A/B/C/D1-623[»]
2IGKX-ray1.80A/B/C/D/E/F/G/H1-623[»]
2IGMX-ray1.90A/B/C/D/E/F/G/H1-623[»]
2IGNX-ray1.65A/B/C/D/E/F/G/H1-623[»]
2IGOX-ray1.95A/B/C/D/E/F/G/H1-623[»]
3BG6X-ray1.70A/B/C/D/E/F/G/H1-623[»]
3BG7X-ray2.10A/B/C/D/E/F/G/H1-623[»]
3BLYX-ray1.90A1-623[»]
3FDYX-ray1.55A1-623[»]
3K4BX-ray1.90A1-623[»]
3K4CX-ray1.70A/B/C/D1-623[»]
3K4JX-ray2.00A1-623[»]
3K4KX-ray1.60A1-623[»]
3K4LX-ray1.75A/B1-623[»]
3K4MX-ray2.20A/B/C/D/E/F/G/H1-623[»]
3K4NX-ray2.75A/B1-623[»]
3LSHX-ray1.90A/B/C/D1-623[»]
3LSIX-ray1.90A/B1-623[»]
3LSKX-ray1.95A/B/C/D1-623[»]
3LSMX-ray1.70A/B1-623[»]
3PL8X-ray1.35A1-623[»]
4MOEX-ray2.00A/B/C/D1-622[»]
4MOFX-ray1.85A1-622[»]
4MOGX-ray2.00A1-622[»]
4MOHX-ray2.10A1-622[»]
4MOIX-ray1.90A/B1-622[»]
4MOJX-ray2.00A/B/C/D3-622[»]
4MOKX-ray1.90A/B/C/D1-622[»]
4MOLX-ray2.00A/B/C/D1-622[»]
4MOMX-ray1.90A/B/C/D3-622[»]
4MOOX-ray1.65A1-622[»]
4MOPX-ray2.30A/B/C/D3-622[»]
4MOQX-ray1.60A/B1-622[»]
4MORX-ray1.50A/B/C/D3-622[»]
4MOSX-ray1.80A1-622[»]
ProteinModelPortaliQ7ZA32.
SMRiQ7ZA32.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.3.10. 1627.
SABIO-RKQ7ZA32.

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 nameiQ7ZA32_TRAOC
AccessioniPrimary (citable) accession number: Q7ZA32
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2003
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.