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

Last modified May 1, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-hydroxyanthranilate 3,4-dioxygenase
EC=1.13.11.6
Alternative name(s):
3-hydroxyanthranilate oxygenase
Short name=3-HAO
3-hydroxyanthranilic acid dioxygenase
Short name=HAD
Biosynthesis of nicotinic acid protein 1
Gene names
Name:BNA1
Ordered Locus Names:ACL127W
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium ›

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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-Rule MF_03019

Catalytic activity

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. HAMAP-Rule MF_03019

Cofactor

Fe2+ ion By similarity.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. HAMAP-Rule MF_03019

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the 3-HAO family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processde novo NAD biosynthetic process from tryptophan

Inferred from electronic annotation. Source: EnsemblFungi

   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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1801803-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_03019
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

Sequences

Sequence LengthMass (Da)Tools
Q75CP6 [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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016816 Genomic DNA. Translation: AAS51101.1.
RefSeqNP_983277.1. NM_208630.1.

3D structure databases

ProteinModelPortalQ75CP6.
SMRQ75CP6. Positions 1-176.
ModBaseSearch...

Protein-protein interaction databases

STRING33169.AGOS_ACL127W.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS51101; AAS51101; AGOS_ACL127W.
GeneID4619397.
KEGGago:AGOS_ACL127W.

Phylogenomic databases

eggNOGNOG77058.
HOGENOMHOG000218448.
KOK00452.
OMAHSPQRPE.
OrthoDBEOG476P8N.
PhylomeDBQ75CP6.

Enzyme and pathway databases

UniPathwayUPA00253; UER00330.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
HAMAPMF_00825. 3_HAO.
InterProIPR010329. 3hydroanth_dOase.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR15497. PTHR15497. 1 hit.
PfamPF06052. 3-HAO. 1 hit.
[Graphical view]
SUPFAMSSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMsTIGR03037. anthran_nbaC. 1 hit.
ProtoNetSearch...

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: May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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