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A1CHT0 (KYNU2_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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 2

EC=3.7.1.3
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-2
L-kynurenine hydrolase 2
Gene names
Name:bna5-2
ORF Names:ACLA_049070
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length464 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

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processL-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

NAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

tryptophan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionkynureninase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Kynureninase 2 HAMAP-Rule MF_03017
PRO_0000356962

Regions

Region163 – 1664Pyridoxal phosphate binding By similarity

Sites

Binding site1351Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1361Pyridoxal phosphate By similarity
Binding site2481Pyridoxal phosphate By similarity
Binding site2511Pyridoxal phosphate By similarity
Binding site2731Pyridoxal phosphate By similarity
Binding site3131Pyridoxal phosphate By similarity
Binding site3411Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2741N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1CHT0 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 011392A1F27E2766

FASTA46451,324
        10         20         30         40         50         60 
MSTTTTSSKP EFPADAATKE YAASLDASDP LAGFREKFII PSKANIASKK LAKPGLSSEP 

        70         80         90        100        110        120 
CIYFCGNSLG IQPKATAKYL EAQLDTWSSI GVSGHFTNVE DSPLREWQNL AEQAAESMSR 

       130        140        150        160        170        180 
VVGAAPEEVA AMGTLTMNLH LLLASFYRPT ATKHKILMDW KAFPSDHYAI ESHIAWHDLD 

       190        200        210        220        230        240 
PKESMVLIGP DEGTFEIPTE KILSYIDQHA DDAALILLPG IQYYTGQLFD IQKITEYAQS 

       250        260        270        280        290        300 
RGLVVGWDLA HAYGNVHLKL HDWNVDFAAW CTYKYGNAGP GAMAGLFVHE RHGRVDYREG 

       310        320        330        340        350        360 
EDSPKFRHRL TGWYGGDKSV RFKMDNNFKP IPGAGGYQIS NPSAIDLASL CAALSVFDET 

       370        380        390        400        410        420 
SMAELRRKSV LMTAYLEHLL LKDTTDESRL FDIITPSEPA ARGAQLSLLL RPGLLHKVAQ 

       430        440        450        460 
RLQEAGIICD KREPGVVRVA PVPLYNTFTE VWTFVEQLKA ALEE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027054 Genomic DNA. Translation: EAW10435.1.
RefSeqXP_001271861.1. XM_001271860.1.

3D structure databases

ProteinModelPortalA1CHT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00004943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00005044; CADACLAP00004943; CADACLAG00005044.
GeneID4704039.
KEGGact:ACLA_049070.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAGWYGGDK.
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 nameKYNU2_ASPCL
AccessionPrimary (citable) accession number: A1CHT0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 46 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