Skip Header

Contribute Send feedback
Read comments (?) or add your own

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

Last modified May 1, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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:PICST_76205
OrganismScheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis) [Complete proteome]
Taxonomic identifier322104 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Scheffersomyces ›

Protein attributes

Sequence length170 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
Gene Ontology (GO)
   Biological_processNAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 1701703-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_03019
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

Sequences

Sequence LengthMass (Da)Tools
A3LP72 [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

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000496 Genomic DNA. Translation: ABN64447.1.
RefSeqXP_001382476.1. XM_001382439.1.

3D structure databases

ProteinModelPortalA3LP72.
SMRA3LP72. Positions 5-170.
ModBaseSearch...

Protein-protein interaction databases

STRING4924.PICST_76205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4837528.
KEGGpic:PICST_76205.

Phylogenomic databases

eggNOGNOG77058.
KOK00452.
OMAHSPQRPE.
OrthoDBEOG476P8N.

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_PICST
AccessionPrimary (citable) accession number: A3LP72
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: April 3, 2007
Last modified: May 1, 2013
This is version 50 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents