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UniProtKB/Swiss-Prot entry O05616

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

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Entry information
Entry name VANA_PSEUH
Primary accession number O05616
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
Name and origin of the protein
Protein name Vanillate O-demethylase oxygenase subunit
Synonyms EC 1.14.13.82
4-hydroxy-3-methoxybenzoate demethylase
Gene name
Name: vanA
From
Pseudomonas sp. (strain HR199 / DSM 7063) [TaxID: 86003] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9098058 [NCBI, ExPASy, EBI, Israel, Japan]
Priefert H., Rabenhorst J., Steinbuechel A.;
"Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate.";
J. Bacteriol. 179:2595-2607(1997).
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
Y11521; CAA72287.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase O05616.
Enzyme and pathway databases
BioCyc MetaCyc:MON-14062; -.
Ontologies
GO
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0018489; Molecular function: vanillate monooxygenase activity (inferred from electronic annotation from EC).
GO:0046274; Biological process: lignin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR005806; Rieske_reg.
IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
Graphical view of domain structure.
Gene3D G3DSA:2.102.10.10; Rieske_reg; 1.
Pfam PF00355; Rieske; 1.
Pfam graphical view of domain structure.
PROSITE PS51296; RIESKE; 1.
PS00570; RING_HYDROXYL_ALPHA; 1.
PROSITE graphical view of domain structure (profiles).
Other
ProtoNet O05616.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Aromatic hydrocarbons catabolism; Iron; Iron-sulfur; Lignin degradation; Metal-binding; Monooxygenase; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1   354  354     Vanillate O-demethylase oxygenase subunit. PRO_0000085059
DOMAIN   7   107  101     Rieske. 
METAL   47    47        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   49    49        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   66    66        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   69    69        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
Sequence information
Length: 354 AA [This is the length of the unprocessed precursor] Molecular weight: 39491 Da [This is the MW of the unprocessed precursor] CRC64: 970AD00DD8A870C3 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MFPKNAWYVA CTPDEIADKP LGRQICNEKI VFYRGPEGRV AAVEDFCPHR GAPLSLGFVR 

        70         80         90        100        110        120 
DGKLICGYHG LEMGCEGKTL AMPGQRVQGF PCIKSYAVEE RYGFIWVWPG DRELADPALI 

       130        140        150        160        170        180 
HHLEWADNPE WAYGGGLYHI ACDYRLMIDN LMDLTHETYV HASSIGQKEI DEAPVSTRVE 

       190        200        210        220        230        240 
GDTVITSRYM DNVMAPPFWR AALRGNGLAD DVPVDRWQIC RFAPPSHVLI EVGVAHAGKG 

       250        260        270        280        290        300 
GYDAPAEYKA GSIVVDFITP ESDTSIWYFW GMARNFRPQG TELTETIRVG QGKIFAEDLD 

       310        320        330        340        350 
MLEQQQRNLL AYPERQLLKL NIDAGGVQSR RVIDRILAAE QEAADAALIA RSAS
O05616 in FASTA format

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