Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A1C874 (3HAO2_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 49. 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 2

EC=1.13.11.6
Alternative name(s):
3-hydroxyanthranilate oxygenase 2
Short name=3-HAO-2
3-hydroxyanthranilic acid dioxygenase 2
Short name=HAD-2
Biosynthesis of nicotinic acid protein 1-2
Gene names
Name:bna1-2
ORF Names:ACLA_076350
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length191 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 caution

The sequence EAW14595.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1911913-hydroxyanthranilate 3,4-dioxygenase 2 HAMAP-Rule MF_03019
PRO_0000361975

Sites

Metal binding521Iron; catalytic By similarity
Metal binding731Iron; catalytic By similarity
Metal binding1111Iron; catalytic By similarity
Binding site481Dioxygen By similarity
Binding site731Substrate By similarity
Binding site1151Substrate By similarity
Binding site1251Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1C874 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: C43A5FC087711AC8

FASTA19122,148
        10         20         30         40         50         60 
MNPMPLSPLF FATWLAENED QLRPPVNNYC LYQGNDFILM AVGGPNERND YHVNETEVCL 

        70         80         90        100        110        120 
QPSWCSREAN EQEWFYQVKG DMLLRVVENN AFRDIPIKEG EMFLLPGNTP HNPVRFKDTI 

       130        140        150        160        170        180 
GLVMERQRPA GSRDRLRWYC TKGDHASPTI IREEVFHCSD LGTQLKPIIE QWQQDEDGRR 

       190 
CAECSCIADP K 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027045 Genomic DNA. Translation: EAW14595.1. Sequence problems.
RefSeqXP_001276021.1. XM_001276020.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00006828.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4708052.
KEGGact:ACLA_076350.

Phylogenomic databases

eggNOGNOG77058.
HOGENOMHOG000218448.
KOK00452.
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. 2 hits.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Entry information

Entry name3HAO2_ASPCL
AccessionPrimary (citable) accession number: A1C874
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: June 11, 2014
This is version 49 of the entry and version 2 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