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Reviewed, UniProtKB/Swiss-Prot A3LP72 (3HAO_PICST)

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

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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
ORF Names: PICST_76205
OrganismPichia stipitis (Yeast) [Complete proteome]
Taxonomic identifier4924 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

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Protein attributes

Sequence length170 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 – 1701703-hydroxyanthranilate 3,4-dioxygenase
PRO_0000361993

Sites

Metal binding481Iron; catalytic By similarity
Metal binding541Iron; catalytic By similarity
Metal binding921Iron; catalytic By similarity
Metal binding1211Divalent metal cation By similarity
Metal binding1241Divalent metal cation By similarity
Metal binding1581Divalent metal cation By similarity
Metal binding1611Divalent metal cation 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
A3LP72-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 8E3C88628833596D

FASTA17019,326
        10         20         30         40         50         60 
MLPEPININK WIEENGHLLQ PPVNNYCLHR GGFTIMIVGG PNERTDYHIN ETPEHFHQLK 

        70         80         90        100        110        120 
GAMCLKVVDD GEFRDIIINE GDSFLLPGNT PHNPVRFADT IGLVVEQDRP ETALDRLRWY 

       130        140        150        160        170 
CSNCREIVHE AAFHLTDLGT QIKEAILAFD GDKESRTCKK CGTLNYSKPQ

« Hide

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References

[1]"Genome sequence of the lignocellulose-bioconverting and xylose-fermenting yeast Pichia stipitis."
Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S., Passoth V., Richardson P.M.
Nat. Biotechnol. 25:319-326(2007) [PubMed: 17334359] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 58785 / CBS 6054 / IFO 10063 / NRRL Y-11545.

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Cross-references

Sequence databases

CP000496 Genomic DNA. Translation: ABN64447.1.
RefSeqXP_001382476.1.

3D structure databases

SMRA3LP72. Positions 5-170.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3LP72.

Genome annotation databases

GeneID4837528.
GenomeReviewsGene locus BNA1 in contig CP000496_GR.
KEGGpic:PICST_76205.

Phylogenomic databases

OMARHSPQRP.

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_PICST
AccessionPrimary (citable) accession number: A3LP72
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: April 3, 2007
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)

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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