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A5E0Z9 (3HAO_LODEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 47. 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

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:LELG_03286
OrganismLodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome]
Taxonomic identifier379508 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeLodderomyces

Protein attributes

Sequence length175 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. HAMAP-Rule MF_03019

Pathway

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03019.

Sequence similarities

Belongs to the 3-HAO family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1751753-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_03019
PRO_0000361988

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
A5E0Z9 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 6ABC58FEBA0680A1

FASTA17520,157
        10         20         30         40         50         60 
MPLPEPLNIK AWVEENEHLL KPPVNNFCLH RGGFTVMIVG GPNERSDYHI NQTPEYFYQY 

        70         80         90        100        110        120 
KGTMCLKVVD EGKFRDIYIR EGDTFLLPPN VPHNPCRFEN TVGIVVEQDR PKGVNDRIRW 

       130        140        150        160        170 
YCARCESIVC EEEFYLTDLG TQIKDAIVAF DSNIEAKTCK NCGHVNSSKR EPAEF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH981527 Genomic DNA. Translation: EDK45107.1.
RefSeqXP_001525358.1. XM_001525308.1.

3D structure databases

ProteinModelPortalA5E0Z9.
SMRA5E0Z9. Positions 6-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36914.A5E0Z9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5232567.
KEGGlel:LELG_03286.

Phylogenomic databases

eggNOGNOG77058.
KOK00452.
OMAHINQTPE.
OrthoDBEOG7QK0Q0.

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. SSF51182. 1 hit.
TIGRFAMsTIGR03037. anthran_nbaC. 1 hit.
ProtoNetSearch...

Entry information

Entry name3HAO_LODEL
AccessionPrimary (citable) accession number: A5E0Z9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: June 12, 2007
Last modified: June 11, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways