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Q5H039 (KYNU_XANOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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

EC=3.7.1.3
Alternative name(s):
L-kynurenine hydrolase
Gene names
Name:kynU
Ordered Locus Names:XOO2428
OrganismXanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) [Complete proteome] [HAMAP]
Taxonomic identifier291331 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length423 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 – 423423Kynureninase HAMAP-Rule MF_01970
PRO_0000357021

Regions

Region133 – 1364Pyridoxal phosphate binding By similarity

Sites

Binding site1051Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1061Pyridoxal phosphate By similarity
Binding site2181Pyridoxal phosphate By similarity
Binding site2211Pyridoxal phosphate By similarity
Binding site2431Pyridoxal phosphate By similarity
Binding site2731Pyridoxal phosphate By similarity
Binding site3011Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2441N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5H039 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 4DD38A3CAFC5A63A

FASTA42346,096
        10         20         30         40         50         60 
MTDLLSRAHA DALDAADPLR SLRDAFVFPQ HGDRDQTYLV GNSLGLQPRA ARAMVDEVLD 

        70         80         90        100        110        120 
QWGTLGVEGH FTGPTQWLTY HQLVRDALAR VVGAQPGEVV AMNTLSVNLH LMMASFYRPT 

       130        140        150        160        170        180 
HERGAILIEA GAFPSDRHAV ESQLRLRGLD PATHLIEVEA DEPNGTLSMA AIADAIAQHG 

       190        200        210        220        230        240 
PRLALVLWPG IQYRTGQAFD LAEIVRLARA QGAAVGCDLA HAVGNIPLTL HDDGVDFAVW 

       250        260        270        280        290        300 
CNYKYLNAGP GAVGGCFVHE RHANSDLPRI AGWWGHEQQT RFRMDPQFVP SPGAEGWQLS 

       310        320        330        340        350        360 
NPPVLALAPL RASLTLFDQA GMAALRAKSE RLTGHLEQLI RARVPQVLQI VTPAEPMHRG 

       370        380        390        400        410        420 
CQLSLRVAGG RAQGRSLFEH LHAAGVLGDW REPDVIRIAP VPLYNRFSDL HTFVGQVEAW 


AAA 

« Hide

References

[1]"The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice."
Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., Go S.-J.
Nucleic Acids Res. 33:577-586(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KACC10331 / KXO85.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013598 Genomic DNA. Translation: AAW75682.1.
RefSeqYP_201067.1. NC_006834.1.

3D structure databases

ProteinModelPortalQ5H039.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING291331.XOO2428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW75682; AAW75682; XOO2428.
GeneID3261809.
KEGGxoo:XOO2428.
PATRIC24104135. VBIXanOry111333_2699.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAYLATWRT.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycXORY291331:GJBV-2270-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_XANOR
AccessionPrimary (citable) accession number: Q5H039
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 1, 2005
Last modified: May 14, 2014
This is version 65 of the entry and version 1 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