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Q2H7G2 (KYNU2_CHAGB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:CHGG_05403
OrganismChaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus) [Complete proteome]
Taxonomic identifier306901 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeChaetomium

Protein attributes

Sequence length539 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 – 539539Kynureninase 2 HAMAP-Rule MF_03017
PRO_0000356975

Regions

Region199 – 2024Pyridoxal phosphate binding By similarity

Sites

Binding site1711Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1721Pyridoxal phosphate By similarity
Binding site2901Pyridoxal phosphate By similarity
Binding site2931Pyridoxal phosphate By similarity
Binding site3151Pyridoxal phosphate By similarity
Binding site3791Pyridoxal phosphate By similarity
Binding site4071Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue3161N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2H7G2 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 6C22ABAB563342EA

FASTA53957,881
        10         20         30         40         50         60 
MDTEYQSFVE TLRAGQKPEF PAHAKTIEYA RELDAHDKLS QLRSDFNIPT KGSLRKKALD 

        70         80         90        100        110        120 
GGVAGETKEP RVPNGVSSAT KPNGTVNSDL KDDEASIYFV GNSLGAQPKC IRQYIDAHLE 

       130        140        150        160        170        180 
TWASIGVNGH FTSFDNSPLA SWQDMAAACA AQSVDLVGAK SANEIIYMNT LTVNLHLMMA 

       190        200        210        220        230        240 
SFYRPTAKRH KIIAEWKPFP SDSYALASQL HWHGLAPATS LIEIHPPNPT GSSPPTLTLT 

       250        260        270        280        290        300 
TSHILATIDA HADSTALLLL PGIQYYTGQL FDMARITRHA RARGIVVGWD LAHAVGNVEL 

       310        320        330        340        350        360 
ELHAWGVDFA VWCTYKYLNA GPGALGGVFV HGRHHSFHRG GGGSGGVGGG RGEGGDGDGG 

       370        380        390        400        410        420 
DGGDGDGMAL GYRHRLAGWY GADKAVRFEM EKVFWPAEGA AGWQVSNPSV VDLACVRATL 

       430        440        450        460        470        480 
GMFERVGMRA LRDKAVLLTG YLEWLLLGLL ADGVGKGGDG EAAFRIITPG HPADRGSQLS 

       490        500        510        520        530 
LLLRGGLLEG VSKELADGGV VVDVRKPDVI RVAPVPMYCR FEDVWGFITV FNRALDRCA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH408031 Genomic DNA. Translation: EAQ88784.1.
RefSeqXP_001221498.1. XM_001221497.1.

3D structure databases

ProteinModelPortalQ2H7G2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4391213.

Phylogenomic databases

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. 3 hits.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU2_CHAGB
AccessionPrimary (citable) accession number: Q2H7G2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 21, 2006
Last modified: February 19, 2014
This is version 45 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