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

A1C408 (3HAO1_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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 1

EC=1.13.11.6
Alternative name(s):
3-hydroxyanthranilate oxygenase 1
Short name=3-HAO-1
3-hydroxyanthranilic acid dioxygenase 1
Short name=HAD-1
Biosynthesis of nicotinic acid protein 1-1
Gene names
Name:bna1-1
ORF Names:ACLA_058050
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length192 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.

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: UniProtKB-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 – 1921923-hydroxyanthranilate 3,4-dioxygenase 1 HAMAP-Rule MF_03019
PRO_0000361974

Sites

Metal binding541Iron; catalytic By similarity
Metal binding601Iron; catalytic By similarity
Metal binding1021Iron; catalytic By similarity
Metal binding1311Divalent metal cation By similarity
Metal binding1341Divalent metal cation By similarity
Metal binding1681Divalent metal cation By similarity
Metal binding1711Divalent metal cation By similarity
Binding site501Dioxygen By similarity
Binding site601Substrate By similarity
Binding site1061Substrate By similarity
Binding site1161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1C408 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 3361901AC98CDBF1

FASTA19221,563
        10         20         30         40         50         60 
MLPPALNIPK WLEANSHLLQ PPVNNYCVYH PSSPATAGYT VMIVGGPNAR TDYHINTTPE 

        70         80         90        100        110        120 
FFYQYRGSML LKTVDTSVSP PVFQDIPIHE GSIFLLPANT PHCPVRFKDT VGVVMEQPRA 

       130        140        150        160        170        180 
EGAVDQMRWY CRGCGEIVWE KQFVCTDLGT QVKEVVEEFG ADQEKRTCKA CGTIAETRFK 

       190 
EGEIVQPPRF VE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS026990 Genomic DNA. Translation: EAW15148.1.
RefSeqXP_001276574.1. XM_001276573.1.

3D structure databases

ProteinModelPortalA1C408.
SMRA1C408. Positions 5-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00005585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00005710; CADACLAP00005585; CADACLAG00005710.
GeneID4708890.
KEGGact:ACLA_058050.

Phylogenomic databases

eggNOGNOG77058.
HOGENOMHOG000218448.
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 name3HAO1_ASPCL
AccessionPrimary (citable) accession number: A1C408
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 48 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