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 Q3BV37


[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 3HAO_XANC5
Primary accession number Q3BV37
Secondary accession numbers None
Integrated into Swiss-Prot on July 11, 2006
Sequence was last modified on November 22, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 25)
Name and origin of the protein
Protein name 3-hydroxyanthranilate 3,4-dioxygenase
Synonyms EC 1.13.11.6
3-hydroxyanthranilic acid dioxygenase
HAD
3-hydroxyanthranilate oxygenase
3-HAO
Gene name
OrderedLocusNames: XCV1645
From
Xanthomonas campestris pv. vesicatoria (strain 85-10) [TaxID: 316273] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.187.21.7254-7266.2005; PubMed=16237009 [NCBI, ExPASy, EBI, Israel, Japan]
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.;
"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence.";
J. Bacteriol. 187:7254-7266(2005).
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
AM039952; CAJ23322.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_363376.1; -.
3D structure databases
ModBase Q3BV37.
Enzyme and pathway databases
BioCyc XCAM316273:XCV1645-MON; -.
Ontologies
GO
GO:0000334; Molecular function: 3-hydroxyanthranilate 3,4-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0008198; Molecular function: ferrous iron binding (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00825; -; 1.
PBIL [Tree]
InterPro IPR010329; 3hydroanth_dOase.
Graphical view of domain structure.
Pfam PF06052; 3-HAO; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR03037; anthran_nbaC; 1.
BLOCKS Q3BV37.
Genome annotation databases
GeneID 3731279; -.
GenomeReviews AM039952_GR; XCV1645.
KEGG xcv:XCV1645; -.
NMPDR fig|316273.3.peg.1708; -.
Phylogenomic databases
HOGENOM Q3BV37; -.
Genome annotation databases
CMR Q3BV37; XCV1645.
Other
ProtoNet Q3BV37.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   176  176     3-hydroxyanthranilate 3,4-dioxygenase. PRO_0000245480
METAL   48    48        Iron 1; catalytic (By similarity). 
METAL   54    54        Iron 1; catalytic (By similarity). 
METAL   92    92        Iron 1; catalytic (By similarity). 
METAL   121   121        Iron 2 (By similarity). 
METAL   124   124        Iron 2 (By similarity). 
METAL   158   158        Iron 2 (By similarity). 
METAL   161   161        Iron 2 (By similarity). 
BINDING   44    44        Dioxygen (By similarity). 
BINDING   54    54        Substrate (By similarity). 
BINDING   96    96        Substrate (By similarity). 
BINDING   106   106        Substrate (By similarity). 
Sequence information
Length: 176 AA [This is the length of the unprocessed precursor] Molecular weight: 20210 Da [This is the MW of the unprocessed precursor] CRC64: F9638C9EA4618289 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLIPPINLHA WIEEHRHLLK PPVGNKCIQQ DGFIIMVVGG PNARTDYHYD EGPEWFFQLE 

        70         80         90        100        110        120 
GEMVLKVQDE GVARDIPIRA GEVFLLPPKV PHSPQRAAGS IGLVIERERL PNEQDGLQWY 

       130        140        150        160        170 
CPQCNHKLYE AMFPLKNIET DFPPVFDRFY RSLALRTCSQ CGHLHPAPER YATVED 

Q3BV37 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 kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!