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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei201 – 2011GlucoseCombined sources
Binding sitei205 – 2051GlucoseCombined sources
Binding sitei283 – 2831FAD cofactor analog; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei283 – 2831FAD; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei472 – 4721FAD cofactor analogCombined sources
Binding sitei548 – 5481FAD cofactor analogCombined sources
Binding sitei595 – 5951FADCombined sources
Binding sitei610 – 6101GlucoseCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 572FADCombined sources
Nucleotide bindingi56 – 572FAD cofactor analogCombined sources
Nucleotide bindingi76 – 772FADCombined sources
Nucleotide bindingi76 – 772FAD cofactor analogCombined sources
Nucleotide bindingi158 – 17114FADCombined sourcesAdd
BLAST
Nucleotide bindingi160 – 1645FAD cofactor analogCombined sources
Nucleotide bindingi169 – 1713FAD cofactor analogCombined sources
Nucleotide bindingi593 – 5953FAD cofactor analogCombined sources

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.

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
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[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini546 – 60459GMC_oxred_CInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 642Glucose bindingCombined sources

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
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[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.3.10. 1627.

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. "Molecular cloning and expression of the pyranose 2-oxidase cDNA from Trametes ochracea MB49 in Escherichia coli."
    Vecerek B., Maresova H., Kocanova M., Kyslik P.
    Appl. Microbiol. Biotechnol. 64:525-530(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MB49Imported.
  2. "Crystal structure of the 270 kDa homotetrameric lignin-degrading enzyme pyranose 2-oxidase."
    Hallberg B.M., Leitner C., Haltrich D., Divne C.
    J. Mol. Biol. 341:781-796(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH FAD.
  3. "Cloning and expression of a pyranose oxidase encoding gene from Trametes multicolor."
    Leitner C.A., Peterbauer C.K., Halada P., Volc J., Haltrich D.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Expression of the pyranose 2-oxidase from Trametes pubescens in Escherichia coli and characterization of the recombinant enzyme."
    Maresova H., Vecerek B., Hradska M., Libessart N., Becka S., Saniez M.H., Kyslik P.
    J. Biotechnol. 120:387-395(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: MB49Imported.
  5. "Structural basis for substrate binding and regioselective oxidation of monosaccharides at C3 by pyranose 2-oxidase."
    Kujawa M., Ebner H., Leitner C., Hallberg B.M., Prongjit M., Sucharitakul J., Ludwig R., Rudsander U., Peterbauer C., Chaiyen P., Haltrich D., Divne C.
    J. Biol. Chem. 281:35104-35115(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH FAD.
  6. "A thermostable triple mutant of pyranose 2-oxidase from Trametes multicolor with improved properties for biotechnological applications."
    Spadiut O., Radakovits K., Pisanelli I., Salaheddin C., Yamabhai M., Tan T.C., Divne C., Haltrich D.
    Biotechnol. J. 4:525-534(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH FAD.
  7. "Improving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design."
    Spadiut O., Leitner C., Salaheddin C., Varga B., Vertessy B.G., Tan T.C., Divne C., Haltrich D.
    FEBS J. 276:776-792(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH FAD.
  8. "Importance of the gating segment in the substrate-recognition loop of pyranose 2-oxidase."
    Spadiut O., Tan T.C., Pisanelli I., Haltrich D., Divne C.
    FEBS J. 277:2892-2909(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH FAD.
  9. "A conserved active-site threonine is important for both sugar and flavin oxidations of pyranose 2-oxidase."
    Pitsawong W., Sucharitakul J., Prongjit M., Tan T.C., Spadiut O., Haltrich D., Divne C., Chaiyen P.
    J. Biol. Chem. 285:9697-9705(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH FAD.
  10. "H-bonding and positive charge at the N5/O4 locus are critical for covalent flavin attachment in trametes pyranose 2-oxidase."
    Tan T.C., Pitsawong W., Wongnate T., Spadiut O., Haltrich D., Chaiyen P., Divne C.
    J. Mol. Biol. 402:578-594(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH FAD; FAD COFACTOR ANALOG AND GLUCOSE.
  11. "Regioselective control of beta-d-glucose oxidation by pyranose 2-oxidase is intimately coupled to conformational degeneracy."
    Tan T.C., Haltrich D., Divne C.
    J. Mol. Biol. 409:588-600(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH FAD.
  12. "Structural basis for binding of fluorinated glucose and galactose to Trametes multicolor pyranose 2-oxidase variants with improved galactose conversion."
    Tan T.C., Spadiut O., Gandini R., Haltrich D., Divne C.
    PLoS ONE 9:e86736-e86736(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 3-622 IN COMPLEX WITH FAD.

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: July 6, 2016
This is version 85 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.