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A1C688 (KYNU1_ASPCL) 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:
Kynureninase 1

EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-1
L-kynurenine hydrolase 1
Gene names
Name:bna5-1
ORF Names:ACLA_069390
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively By similarity. HAMAP-Rule MF_03017

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_03017

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_03017

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_03017

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_03017

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_03017

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_03017

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03017.

Sequence similarities

Belongs to the kynureninase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Kynureninase 1 HAMAP-Rule MF_03017
PRO_0000356961

Regions

Region174 – 1774Pyridoxal phosphate binding By similarity

Sites

Binding site1461Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1471Pyridoxal phosphate By similarity
Binding site2311Pyridoxal phosphate By similarity
Binding site2601Pyridoxal phosphate By similarity
Binding site2631Pyridoxal phosphate By similarity
Binding site2851Pyridoxal phosphate By similarity
Binding site3261Pyridoxal phosphate By similarity
Binding site3541Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2861N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1C688 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: B4275CBDF28D6821

FASTA48654,747
        10         20         30         40         50         60 
MGSRLHTREI QNGPPLPYND DIRAFSKEYA ESLDAQDPLH RFRNEFVIPS KEDLKRTTLD 

        70         80         90        100        110        120 
PNQEPEHSPT PSLYLCGNSL GLQPQSTRKY IEYYLRAWAT KGVTGHFVQH DDQLLPPFVD 

       130        140        150        160        170        180 
VDAAGARLMA PIVGAMESEV AVMGTLTTNL HILMASFYQP TQERYKIIIE GKAFPSDHYA 

       190        200        210        220        230        240 
VESQIKHHNF DPKDGMVLIE PEDHTRPVLD TEHIIRTIDE HASSTAVILL SAIQYYTGQY 

       250        260        270        280        290        300 
FDIKRITAHA QSKGILVGWD CAHAAGNVDL QLHDWNVDFA AWCTYKYLNS GPGGTAALFV 

       310        320        330        340        350        360 
HERHGRVNLE QVNSESEPFR PRLSGWWGGD KKTRFLMDNN FIPQPGAAGF QLSNPSVLDM 

       370        380        390        400        410        420 
NAVVASLELF KQASMAEIRK KSLHITGYLE HLLLNYPLDT PSEKKPFTII TPSNPAERGA 

       430        440        450        460        470        480 
QLSVRLQPGL LDHVLETLED NAVVIDERKP DVIRVAPAPL YNTYTDVWEF CRIFHEACQK 


ALKARG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027045 Genomic DNA. Translation: EAW13909.1.
RefSeqXP_001275335.1. XM_001275334.1.

3D structure databases

ProteinModelPortalA1C688.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00006290.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00006450; CADACLAP00006290; CADACLAG00006450.
GeneID4707638.
KEGGact:ACLA_069390.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAGLMNDIV.
OrthoDBEOG7V1G0J.

Enzyme and pathway databases

UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU1_ASPCL
AccessionPrimary (citable) accession number: A1C688
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 23, 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