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Q8PM33 (KYNU_XANAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:XAC1601
OrganismXanthomonas axonopodis pv. citri (Citrus canker) [Complete proteome] [HAMAP]
Taxonomic identifier92829 [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.

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_0000357014

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
Q8PM33 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: D05719233F2F29BC

FASTA42345,845
        10         20         30         40         50         60 
MTDPLSRAHA AALDAADPLR NLRDAFVFPQ HGDDDQTYFV GNSLGLQPRA ARAMVDEVLD 

        70         80         90        100        110        120 
QWGALAVEGH FTGPTQWLTY HQLVGDALAR VVGAQPGEVV AMNTLSVNLH LMMASFYRPT 

       130        140        150        160        170        180 
AERGAILIEA GAFPSDRHAV ESQLRLHGLD PATHLIEVEA DEPNGTVSMS AIAEAIAQHG 

       190        200        210        220        230        240 
PHLALVLWPG IQYRTGQAFD LAEIVRLARA QGAAVGLDLA HAVGNLPLTL HDDGVDFAVW 

       250        260        270        280        290        300 
CHYKYLNAGP GAVGGCFVHA RHATSDLPRM AGWWGHEQQT RFRMDPQFVP SPGAEGWQLS 

       310        320        330        340        350        360 
NPPVLALAPL RASLALFDQA GMAALRAKSE QLTGHLEQMI HARVPQVLQI VTPVEPARRG 

       370        380        390        400        410        420 
CQLSLRVAGG RARGRALFEH LHAAGVLGDW REPDVIRIAP VPLYNRFSDL HTFVEQVEAW 


AAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008923 Genomic DNA. Translation: AAM36469.1.
RefSeqNP_641933.1. NC_003919.1.

3D structure databases

ProteinModelPortalQ8PM33.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1155672.
GenomeReviewsGene locus XAC1601 in contig AE008923_GR.
KEGGxac:XAC1601.
NMPDRfig|190486.1.peg.1577.
PATRIC24055203. VBIXanAxo33670_1680.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG523016.
OMATAEAHKR.
ProtClustDBCLSK903751.

Enzyme and pathway databases

BioCycXAXO190486:XAC1601-MONOMER.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK01556.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. Kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameKYNU_XANAC
AccessionPrimary (citable) accession number: Q8PM33
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families