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Protein

Kynureninase

Gene

kynU

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathway:iL-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Kynureninase (kynU)
This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Pathway:iNAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Kynureninase (kynU)
  3. no protein annotated in this organism
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei108 – 1081Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei109 – 1091Pyridoxal phosphateUniRule annotation
Binding sitei176 – 1761Pyridoxal phosphateUniRule annotation
Binding sitei205 – 2051Pyridoxal phosphateUniRule annotation
Binding sitei208 – 2081Pyridoxal phosphateUniRule annotation
Binding sitei230 – 2301Pyridoxal phosphateUniRule annotation
Binding sitei260 – 2601Pyridoxal phosphateUniRule annotation
Binding sitei286 – 2861Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciDRAD243230:GH46-3029-MONOMER.
UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:kynUUniRule annotation
Ordered Locus Names:DR_A0338
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524 Componenti: Chromosome II

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410KynureninasePRO_0000357003Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei231 – 2311N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243230.DR_A0338.

Structurei

3D structure databases

ProteinModelPortaliQ9RYH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 1384Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242437.
InParanoidiQ9RYH5.
KOiK01556.
OMAiVWDLAHS.
OrthoDBiEOG6N67XP.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9RYH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLLPALDL AQLDALDARD PLAHKRAEFD LPGDIIYLDG NSLGALPRRV
60 70 80 90 100
PARLSQVATE EWGHHLIRSW TRNAEAAQDW MALPDRVAAK LAPLLGAGAH
110 120 130 140 150
EVAVGDSTSV NTFKALAAAL RLSGRRVILS DADNFPTDLY VAQGLARLLG
160 170 180 190 200
DVEVRTAPGD EMTQHFTDDV GVVLLTEVDY RTGRRLDMRA ITAAAHARGI
210 220 230 240 250
VTVWDLAHSA GAFAVDLGGA GADFAIGCGY KFLNGGPGAP AFLYVAERHL
260 270 280 290 300
DRAEVVLSGW MGHADPFEMA RAYAPAPGAR RFVVGTPQVL SLSALDAALD
310 320 330 340 350
VFGDVDLGAL REKSLSLTDT FIRLMEPLAE QYPLELVTPL AHAERGSQVS
360 370 380 390 400
YRHPHAQQVM AQLIECGIVG DFRTPDILRF GFTPLYLSHG DVGRAVAGIA
410
AVLDELEGPA
Length:410
Mass (Da):43,890
Last modified:December 16, 2008 - v2
Checksum:i50177666F0EA98F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001825 Genomic DNA. Translation: AAF12444.1.
PIRiF75588.
RefSeqiNP_285661.1. NC_001264.1.
WP_010889597.1. NC_001264.1.

Genome annotation databases

EnsemblBacteriaiAAF12444; AAF12444; DR_A0338.
GeneIDi1799657.
KEGGidra:DR_A0338.
PATRICi21633722. VBIDeiRad64572_3230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001825 Genomic DNA. Translation: AAF12444.1.
PIRiF75588.
RefSeqiNP_285661.1. NC_001264.1.
WP_010889597.1. NC_001264.1.

3D structure databases

ProteinModelPortaliQ9RYH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_A0338.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF12444; AAF12444; DR_A0338.
GeneIDi1799657.
KEGGidra:DR_A0338.
PATRICi21633722. VBIDeiRad64572_3230.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242437.
InParanoidiQ9RYH5.
KOiK01556.
OMAiVWDLAHS.
OrthoDBiEOG6N67XP.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.
BioCyciDRAD243230:GH46-3029-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiKYNU_DEIRA
AccessioniPrimary (citable) accession number: Q9RYH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: July 22, 2015
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.