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Reviewed, UniProtKB/Swiss-Prot Q75CP6 (3HAO_ASHGO)

Last modified November 3, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
    Biosynthesis of nicotinic acid protein 1
Gene names
Name: BNA1
Ordered Locus Names: ACL127W
OrganismAshbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]
Taxonomic identifier33169 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

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Protein attributes

Sequence length180 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.

Cofactor

Fe2+ ion By similarity.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the 3-HAO family.

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Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pyridine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-hydroxyanthranilate 3,4-dioxygenase activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1801803-hydroxyanthranilate 3,4-dioxygenase
PRO_0000245471

Sites

Metal binding491Iron; catalytic By similarity
Metal binding551Iron; catalytic By similarity
Metal binding981Iron; catalytic By similarity
Metal binding1271Divalent metal cation By similarity
Metal binding1301Divalent metal cation By similarity
Metal binding1641Divalent metal cation By similarity
Metal binding1671Divalent metal cation By similarity
Binding site451Dioxygen By similarity
Binding site551Substrate By similarity
Binding site1021Substrate By similarity
Binding site1121Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q75CP6-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 24B84FC51F52BA85

FASTA18020,378
        10         20         30         40         50         60 
MLNTTPINID AWLAENSHLL QPPVNNFCLH RGGFTVMLVG GPNERTDYHV NPTPEWFYQK 

        70         80         90        100        110        120 
TGAMTLRIVD EQLSGAARFR DVTIREGDSF LLPANVPHNP VRYADTVGIV VEQDRPAGHF 

       130        140        150        160        170        180 
DQLRWYCRGC RELVCKYEFY MSDLSSQVRE GIERFAASAE DRVCKHCGTL NYPTPQASAT

« Hide

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References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.

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Cross-references

Sequence databases

AE016816 Genomic DNA. Translation: AAS51101.1.
RefSeqNP_983277.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ75CP6.

Genome annotation databases

GeneID4619397.
GenomeReviewsGene locus ACL127W in contig AE016816_GR.
KEGGago:AGOS_ACL127W.
NMPDRfig|33169.1.peg.922.

Organism-specific databases

AGDACL127W.

Phylogenomic databases

HOGENOMQ75CP6.
OMARHSPQRP.

Enzyme and pathway databases

BRENDA1.13.11.6. 279361.

Family and domain databases

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_ASHGO
AccessionPrimary (citable) accession number: Q75CP6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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