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Reviewed, UniProtKB/Swiss-Prot B2SIT8 (KYNU_XANOP)

Last modified November 3, 2009. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: PXO_00758
OrganismXanthomonas oryzae pv. oryzae (strain PXO99A) [Complete proteome] [HAMAP]
Taxonomic identifier360094 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine.

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

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

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the kynureninase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

tryptophan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   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 – 423423Kynureninase
PRO_0000357020

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
B2SIT8-1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 4DC67FDCBA30463A

FASTA42346,115
        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 VTPAEPMRRG 

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


AAA 

« Hide

Cross-references

Sequence databases

CP000967 Genomic DNA. Translation: ACD58733.1.
RefSeqYP_001913265.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6305630.
GenomeReviewsGene locus PXO_00758 in contig CP000967_GR.
KEGGxop:PXO_00758.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAWQPLSGW.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_XANOP
AccessionPrimary (citable) accession number: B2SIT8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 1, 2008
Last modified: November 3, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents