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Q2H9P7 (KYNU1_CHAGB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:CHGG_03057
OrganismChaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) (Soil fungus) [Complete proteome]
Taxonomic identifier306901 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Chaetomiaceae › Chaetomium ›

Protein attributes

Sequence length509 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.

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.

Subcellular location

Cytoplasm By similarity.

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: 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 – 509509Kynureninase 1 HAMAP-Rule MF_03017
PRO_0000356974

Regions

Region183 – 1864Pyridoxal phosphate binding By similarity

Sites

Binding site1541Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1551Pyridoxal phosphate By similarity
Binding site2701Pyridoxal phosphate By similarity
Binding site2731Pyridoxal phosphate By similarity
Binding site2951Pyridoxal phosphate By similarity
Binding site3451Pyridoxal phosphate By similarity
Binding site3731Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2961N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2H9P7 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: B95634E76F9ED0D2

FASTA50955,240
        10         20         30         40         50         60 
MSEILKSPIQ SPLLRGFVTS RRCDASEIED LGSNVTKGLR VAGGRRVLRS HFFSYCLTYP 

        70         80         90        100        110        120 
AVNVAATTET GSGDGATEKC VYLCGNSLGL QPKRTQTRVN QYLSTWGTQG VQGHFKPLEE 

       130        140        150        160        170        180 
SPLPTWLDAD DRAAQLIAPI VGASKAEVAV MQTLTANLHL LMSAFYKPDI NGKHKIILES 

       190        200        210        220        230        240 
KAFPSDHFAV ETQLRHHNLD PATSMITLTS PSSPEDNILT TAEILSAITT HAATTALILL 

       250        260        270        280        290        300 
PGIQYYTGQL LDIPTITAHA RTHSVFLIWD LAHAVGNAPL HLHDWGVDAA AWCSYKYLNG 

       310        320        330        340        350        360 
GPGCIGGLFV HERNSAVPPP VGELEVQQKE GEWEREGYAN RLAGWWGNDK RTRFAMVNRF 

       370        380        390        400        410        420 
RPVPGAAGFQ LSNPSILDIT SLTASLEVFA EAGGVGALRG KSLRLTAFLE ELLVGEGSSI 

       430        440        450        460        470        480 
VGVEERALFR VITPSDPGQR GAQLSLMLRG GLLEAVMREL EKRAVIVDER KPDVIRVAPA 

       490        500 
PLYNSFEDCV RFVVAFGEAL AVARKEVAV

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CH408030 Genomic DNA. Translation: EAQ91122.1.
RefSeqXP_001229573.1. XM_001229572.1.

3D structure databases

ProteinModelPortalQ2H9P7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4389081.

Phylogenomic databases

OrthoDBEOG4TB7KQ.

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. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU1_CHAGB
AccessionPrimary (citable) accession number: Q2H9P7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 21, 2006
Last modified: March 6, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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