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Reviewed, UniProtKB/Swiss-Prot Q4UT95 (3HAO_XANC8)

Last modified June 16, 2009. Version 27. 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: XC_2679
OrganismXanthomonas campestris pv. campestris (strain 8004) [Complete proteome] [HAMAP]
Taxonomic identifier314565 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

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Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Cofactor

Binds 2 Fe2+ ions per subunit By similarity.

Subunit structure

Homodimer By similarity.

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_0000245481

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
Q4UT95-1 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 3C2FDD218C8458D4

FASTA17620,128
        10         20         30         40         50         60 
MLVPPINLHA WVEQHRHLLK PPVGNKCIQQ DGFIIMIVGG PNARTDYHYD EGPEWFFQLE 

        70         80         90        100        110        120 
GEMVLKVQDD GTARDIPIRA GEIFLLPPKV PHSPQRAAGS IGLVIERERL PHEQDGLQWY 

       130        140        150        160        170 
CPQCNHKLYE AMFPLENIET DFPPVFDHFY RSLALRTCTQ CGHVHPAPER YAAVEA

« Hide

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References

[1]"Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris."
Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q., Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S., Gu W.-Y., Lu G., Rong L. expand/collapse author list , Tian Y., Yao Z., Fu G., Chen B., Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.
Genome Res. 15:757-767(2005) [PubMed: 15899963] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000050 Genomic DNA. Translation: AAY49728.1.
RefSeqYP_243748.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3381213.
GenomeReviewsGene locus XC_2679 in contig CP000050_GR.
KEGGxcb:XC_2679.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ4UT95.
OMAQ4UT95. RHSPQRP.

Enzyme and pathway databases

BioCycXCAM314565:XC_2679-MON.

Family and domain databases

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

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Entry information

Entry name3HAO_XANC8
AccessionPrimary (citable) accession number: Q4UT95
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 5, 2005
Last modified: June 16, 2009
This is version 27 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