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Q59K86 (3HAO_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
ORF Names:CaO19.3515
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length171 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.

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
Gene Ontology (GO)
   Biological processpyridine 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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1711713-hydroxyanthranilate 3,4-dioxygenase
PRO_0000361984

Sites

Metal binding491Iron; catalytic By similarity
Metal binding551Iron; catalytic By similarity
Metal binding931Iron; catalytic By similarity
Metal binding1221Divalent metal cation By similarity
Metal binding1251Divalent metal cation By similarity
Metal binding1591Divalent metal cation By similarity
Metal binding1621Divalent metal cation By similarity
Binding site451Dioxygen By similarity
Binding site551Substrate By similarity
Binding site971Substrate By similarity
Binding site1071Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59K86 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: EAADB3DA38113136

FASTA17119,545
        10         20         30         40         50         60 
MVLGQPINII KWIEENGDLL KPPVNNFCLH RGGFTIMIVG GPNERSDYHI NQTPEYFYQF 

        70         80         90        100        110        120 
KGTMCLKVVD DGEFKDIFIN EGDSFLLPPN VPHNPCRYEN TIGIVVEQDR PAGVNDKVRW 

       130        140        150        160        170 
YCQKCQTVIH EVEFYLTDLG TQIKEAIVKF DADLDARTCK NCGTVNSSRR D 

« Hide

References

[1]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AACQ01000315 Genomic DNA. Translation: EAK90890.1.
RefSeqXP_710160.1. XM_705068.1.

3D structure databases

HSSPHSSP built from PDB template 1ZVF based on UniProtKB P47096.
ProteinModelPortalQ59K86.
SMRQ59K86. Positions 6-169.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ59K86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3648245.
KEGGcal:CaO19.3515.

Organism-specific databases

CGDCAL0005808. orf19.3515.

Phylogenomic databases

OMALKPPVNN.
PhylomeDBQ59K86.

Family and domain databases

InterProIPR010329. 3hydroanth_dOase.
IPR011051. Cupin_RmlC_type.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
KOK00452.
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_CANAL
AccessionPrimary (citable) accession number: Q59K86
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: April 26, 2005
Last modified: January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families