Skip Header

Contribute Send feedback
Read comments (?) or add your own

O05616 (VANA_PSEUH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vanillate O-demethylase oxygenase subunit

EC=1.14.13.82
Alternative name(s):
4-hydroxy-3-methoxybenzoate demethylase
Gene names
Name:vanA
OrganismPseudomonas sp. (strain HR199 / DSM 7063)
Taxonomic identifier86003 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Vanillate + O2 + NADH = 3,4-dihydroxybenzoate + NAD+ + H2O + formaldehyde.

Cofactor

Binds 1 2Fe-2S cluster Probable.

Binds 1 iron ion Probable.

Pathway

Xenobiotic degradation; vanillyl-alcohol degradation.

Subunit structure

This demethylase system consists of two proteins: an oxygenase and an oxygenase reductase.

Sequence similarities

Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.

Contains 1 Rieske domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Vanillate O-demethylase oxygenase subunit
PRO_0000085059

Regions

Domain7 – 107101Rieske

Sites

Metal binding471Iron-sulfur (2Fe-2S) By similarity
Metal binding491Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Metal binding661Iron-sulfur (2Fe-2S) By similarity
Metal binding691Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O05616 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 970AD00DD8A870C3

FASTA35439,491
        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 

« Hide

References

[1]"Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate."
Priefert H., Rabenhorst J., Steinbuechel A.
J. Bacteriol. 179:2595-2607(1997) [PubMed: 9098058] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11521 Genomic DNA. Translation: CAA72287.1.

3D structure databases

ProteinModelPortalO05616.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14062.

Family and domain databases

InterProIPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
[Graphical view]
Gene3DG3DSA:2.102.10.10. Rieske_reg. 1 hit.
PfamPF00355. Rieske. 1 hit.
[Graphical view]
SUPFAMSSF50022. Rieske_dom. 1 hit.
PROSITEPS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVANA_PSEUH
AccessionPrimary (citable) accession number: O05616
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: June 28, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families