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Reviewed, UniProtKB/Swiss-Prot Q1E5I0 (3HAO_COCIM)

Last modified November 3, 2009. Version 21. 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

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
ORF Names: CIMG_02183
OrganismCoccidioides immitis (Valley fever fungus) [Complete proteome]
Taxonomic identifier5501 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1921923-hydroxyanthranilate 3,4-dioxygenase
PRO_0000361986

Sites

Metal binding541Iron; catalytic By similarity
Metal binding601Iron; catalytic By similarity
Metal binding1021Iron; catalytic By similarity
Metal binding1311Divalent metal cation By similarity
Metal binding1341Divalent metal cation By similarity
Metal binding1681Divalent metal cation By similarity
Metal binding1711Divalent metal cation By similarity
Binding site501Dioxygen By similarity
Binding site601Substrate By similarity
Binding site1061Substrate By similarity
Binding site1161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1E5I0-1 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 00503228EB6FC03A

FASTA19221,611
        10         20         30         40         50         60 
MLAPALNLPK WLEENSHLLQ PPINNYCVYH PSAPATQGYT VMVVGGPNVR TDYHINPTPE 

        70         80         90        100        110        120 
FFYQHRGSML LRTVDQSTSP PTFQDIPIHE GSLFLLPANT PHCPVRFADT VGVVLEVPRP 

       130        140        150        160        170        180 
ENATDCMRWY CKGCGEIVWE KKFHCTDLGT QVKEVVEEFA ADDEKRKCKA CGSVRSVRYE 

       190 
DGEVVQPPRA PE 

« Hide

References

[1]"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives."
Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. expand/collapse author list , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.
Genome Res. 19:1722-1731(2009) [PubMed: 19717792] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RS.

Cross-references

Sequence databases

CH476726 Genomic DNA. Translation: EAS36829.1.
RefSeqXP_001248412.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4567554.

Family and domain databases

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

Entry information

Entry name3HAO_COCIM
AccessionPrimary (citable) accession number: Q1E5I0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 11, 2006
Last modified: November 3, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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