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Reviewed, UniProtKB/Swiss-Prot Q8PAD2 (KYNU_XANCP)

Last modified November 3, 2009. Version 35. 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: XCC1553
OrganismXanthomonas campestris pv. campestris [Complete proteome] [HAMAP]
Taxonomic identifier340 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length424 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 – 424424Kynureninase
PRO_0000357018

Regions

Region134 – 1374Pyridoxal phosphate binding By similarity

Sites

Binding site1061Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1071Pyridoxal phosphate By similarity
Binding site2191Pyridoxal phosphate By similarity
Binding site2221Pyridoxal phosphate By similarity
Binding site2441Pyridoxal phosphate By similarity
Binding site2741Pyridoxal phosphate By similarity
Binding site3021Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2451N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8PAD2-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: AFB4C7D41FC3C5AF

FASTA42446,200
        10         20         30         40         50         60 
MMTDPLSRSH AAALDAADPL RALRDAFVFP QHGGQDQTYF VGNSLGLQPR QARAMVSEVL 

        70         80         90        100        110        120 
DQWGALAVEG HFTGPTQWLT YHQLVRDGLA RVVGAQPDEV VAMNTLTVNL HLMMASFYRP 

       130        140        150        160        170        180 
SAERAAILIE AGAFPSDRHA VESQLRLHGL DPDTHLIEVE PDAADGTLSM DAIAATIAQH 

       190        200        210        220        230        240 
GPRLALVLWP GIQYRTGQAF ALGEIARLAR AQGAAVGFDL AHAVGNIPLS LHDDGVDFAV 

       250        260        270        280        290        300 
WCHYKYLNAG PGAVGGCFVH ARHAHSNLPR MAGWWGHEQP TRFRMEPQFV PSPGAEGWQL 

       310        320        330        340        350        360 
SNPPVLALAP LRASLELFDQ AGMPALRAKS EQLTGHLEQL IHTRVPQVLQ IVTPADPAQR 

       370        380        390        400        410        420 
GCQLSLRVAG GRTQGRALFE YLQSVGVLGD WREPDVIRIA PVPLYNRFCD LHQLVEHVET 


WAAA 

« Hide

Cross-references

Sequence databases

AE008922 Genomic DNA. Translation: AAM40848.1.
RefSeqNP_636924.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID998117.
GenomeReviewsGene locus XCC1553 in contig AE008922_GR.
KEGGxcc:XCC1553.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8PAD2.
OMAWQPLSGW.

Enzyme and pathway databases

BioCycXCAM190485:XCC1553-MON.

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_XANCP
AccessionPrimary (citable) accession number: Q8PAD2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: October 1, 2002
Last modified: November 3, 2009
This is version 35 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