ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q75ZP8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name P2OX_LYOSH
Primary accession number Q75ZP8
Secondary accession numbers None
Integrated into Swiss-Prot on June 7, 2005
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 19)
Name and origin of the protein
Protein name Pyranose 2-oxidase
Synonyms P2Ox
Pyranose oxidase
PROD
POD
POx
EC 1.1.3.10
Pyranose:oxygen 2-oxidoreductase
Glucose 2-oxidase
FAD-oxidoreductase
Gene name
Name: p2ox
Synonyms: lsp2o
From
Lyophyllum shimeji (Hon-shimeji) [TaxID: 47721] 
Taxonomy Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; Agaricomycetidae; Agaricales; Tricholomataceae; Lyophyllum.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Takakura Y., Tsutsumi F., Inoue Y., Kuwata S.;
"Identification and cloning of a novel pyranose oxidase with high catalytic activity from Lyophyllum shimeji and its expression in Escherichia coli.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB119106; BAD12079.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase Q75ZP8.
Ontologies
GO
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0050233; Molecular function: pyranose oxidase activity (inferred from electronic annotation from InterPro).
GO:0006006; Biological process: glucose metabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000172; GMC_OxRdtase_N.
IPR012814; Pyranose_ox.
Graphical view of domain structure.
Pfam PF00732; GMC_oxred_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02462; pyranose_ox; 1.
PROSITE PS00623; GMC_OXRED_1; FALSE_NEG.
PS00624; GMC_OXRED_2; FALSE_NEG.
ProtoNet Q75ZP8.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
FAD; Flavoprotein; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   618  618     Pyranose 2-oxidase. PRO_0000205613
ACT_SITE   540   540        By similarity. 
ACT_SITE   583   583        By similarity. 
BINDING   441   441        Substrate (By similarity). 
BINDING   443   443        Substrate (By similarity). 
MOD_RES   170   170        Tele-8alpha-FAD histidine (By similarity). 
Sequence information
Length: 618 AA [This is the length of the unprocessed precursor] Molecular weight: 68488 Da [This is the MW of the unprocessed precursor] CRC64: 255B99DF266BC541 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLSTEQMLR DYPRSMQING QIPKNAIHET YGNDGVDVFI AGSGPIGATY AKLCVEAGLR 

        70         80         90        100        110        120 
VVMVEIGAAD SFYAVNAEEG TAVPYVPGYH KKNEIEFQKD IDRFVNVIKG ALQQVSVPVR 

       130        140        150        160        170        180 
NQNVPTLDPG AWSAPPGSSA ISNGKNPHQR EFENLSAEAV TRGVGGMSTH WTCSTPRIHP 

       190        200        210        220        230        240 
PMESLPGIGR PKLSNDPAED DKEWNELYSE AERLIGTSTK EFDESIRHTL VLRSLQDAYK 

       250        260        270        280        290        300 
DRQRIFRPLP LACHRLKNAP EYVEWHSAEN LFHSIYNDDK QKKLFTLLTN HRCTRLALTG 

       310        320        330        340        350        360 
GYEKKIGAAE VRNLLATRNP SSQLDSYIMA KVYVLASGAI GNPQILYNSG FSGLQVTPRN 

       370        380        390        400        410        420 
DSLIPNLGRY ITEQPMAFCQ IVLRQEFVDS VRDDPYGLPW WKEAVAQHIA KNPTDALPIP 

       430        440        450        460        470        480 
FRDPEPQVTT PFTEEHPWHT QIHRDAFSYG AVGPEVDSRV IVDLRWFGAT DPEANNLLVF 

       490        500        510        520        530        540 
QNDVQDGYSM PQPTFRYRPS TASNVRARKM MADMCEVASN LGGYLPTSPP QFMDPGLALH 

       550        560        570        580        590        600 
LAGTTRIGFD KATTVADNNS LVWDFANLYV AGNGTIRTGF GENPTLTSMC HAIKSARSII 

       610 
NTLKGGTDGK NTGEHRNL 

Q75ZP8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!