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Reviewed, UniProtKB/Swiss-Prot Q3BV37 (3HAO_XANC5)

Last modified February 9, 2010. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    3-hydroxyanthranilate 3,4-dioxygenase
    EC=1.13.11.6
Alternative name(s):
    3-hydroxyanthranilic acid dioxygenase
      Short name=HAD
    3-hydroxyanthranilate oxygenase
      Short name=3-HAO
Gene names
Ordered Locus Names: XCV1645
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

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Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate By similarity. HAMAP MF_00825

Catalytic activity

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP MF_00825

Cofactor

Binds 2 Fe2+ ions per subunit By similarity. HAMAP MF_00825

Subunit structure

Homodimer By similarity. HAMAP MF_00825

Sequence similarities

Belongs to the 3-HAO family.

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Ontologies

Keywords
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-hydroxyanthranilate 3,4-dioxygenase activity

Inferred from electronic annotation. Source: HAMAP

ferrous iron binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1761763-hydroxyanthranilate 3,4-dioxygenase HAMAP MF_00825
PRO_0000245480

Sites

Metal binding481Iron 1; catalytic By similarity
Metal binding541Iron 1; catalytic By similarity
Metal binding921Iron 1; catalytic By similarity
Metal binding1211Iron 2 By similarity
Metal binding1241Iron 2 By similarity
Metal binding1581Iron 2 By similarity
Metal binding1611Iron 2 By similarity
Binding site441Dioxygen By similarity
Binding site541Substrate By similarity
Binding site961Substrate By similarity
Binding site1061Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q3BV37-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: F9638C9EA4618289

FASTA17620,210
        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

« Hide

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References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
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. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed: 16237009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM039952 Genomic DNA. Translation: CAJ23322.1.
RefSeqYP_363376.1.

3D structure databases

SMRQ3BV37. Positions 2-168.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3BV37.

Genome annotation databases

GeneID3731279.
GenomeReviewsGene locus XCV1645 in contig AM039952_GR.
KEGGxcv:XCV1645.
NMPDRfig|316273.3.peg.1708.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG77058.
HOGENOMHBG341987.
OMARHSPQRP.

Family and domain databases

HAMAPMF_00825. 3_HAO.
[Tree]
InterProIPR010329. 3hydroanth_dOase.
IPR011051. Cupin_RmlC_type.
[Graphical view]
PfamPF06052. 3-HAO. 1 hit.
[Graphical view]
TIGRFAMsTIGR03037. anthran_nbaC. 1 hit.
ProtoNetSearch...

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Entry information

Entry name3HAO_XANC5
AccessionPrimary (citable) accession number: Q3BV37
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 22, 2005
Last modified: February 9, 2010
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents