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Q9RYH5 (KYNU_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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

EC=3.7.1.3
Alternative name(s):
L-kynurenine hydrolase
Gene names
Name:kynU
Ordered Locus Names:DR_A0338
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length410 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_01970

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_01970

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_01970

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01970

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_01970

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_01970

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01970

Sequence similarities

Belongs to the kynureninase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Kynureninase HAMAP-Rule MF_01970
PRO_0000357003

Regions

Region135 – 1384Pyridoxal phosphate binding By similarity

Sites

Binding site1081Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1091Pyridoxal phosphate By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site2051Pyridoxal phosphate By similarity
Binding site2081Pyridoxal phosphate By similarity
Binding site2301Pyridoxal phosphate By similarity
Binding site2601Pyridoxal phosphate By similarity
Binding site2861Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2311N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RYH5 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 50177666F0EA98F0

FASTA41043,890
        10         20         30         40         50         60 
MTTLLPALDL AQLDALDARD PLAHKRAEFD LPGDIIYLDG NSLGALPRRV PARLSQVATE 

        70         80         90        100        110        120 
EWGHHLIRSW TRNAEAAQDW MALPDRVAAK LAPLLGAGAH EVAVGDSTSV NTFKALAAAL 

       130        140        150        160        170        180 
RLSGRRVILS DADNFPTDLY VAQGLARLLG DVEVRTAPGD EMTQHFTDDV GVVLLTEVDY 

       190        200        210        220        230        240 
RTGRRLDMRA ITAAAHARGI VTVWDLAHSA GAFAVDLGGA GADFAIGCGY KFLNGGPGAP 

       250        260        270        280        290        300 
AFLYVAERHL DRAEVVLSGW MGHADPFEMA RAYAPAPGAR RFVVGTPQVL SLSALDAALD 

       310        320        330        340        350        360 
VFGDVDLGAL REKSLSLTDT FIRLMEPLAE QYPLELVTPL AHAERGSQVS YRHPHAQQVM 

       370        380        390        400        410 
AQLIECGIVG DFRTPDILRF GFTPLYLSHG DVGRAVAGIA AVLDELEGPA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001825 Genomic DNA. Translation: AAF12444.1.
PIRF75588.
RefSeqNP_285661.1. NC_001264.1.

3D structure databases

ProteinModelPortalQ9RYH5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_A0338.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF12444; AAF12444; DR_A0338.
GeneID1799657.
KEGGdra:DR_A0338.
PATRIC21633722. VBIDeiRad64572_3230.

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242437.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycDRAD243230:GH46-3029-MONOMER.
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 nameKYNU_DEIRA
AccessionPrimary (citable) accession number: Q9RYH5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways