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P83788 (KYNU_PSEFL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismPseudomonas fluorescens
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_01970

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine. Ref.1

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. Ref.1

Cofactor

Pyridoxal phosphate.

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. Ref.1

Sequence similarities

Belongs to the kynureninase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Kynureninase HAMAP-Rule MF_01970
PRO_0000357010

Regions

Region129 – 1324Pyridoxal phosphate binding HAMAP-Rule MF_01970

Sites

Binding site971Pyridoxal phosphate; via amide nitrogen
Binding site981Pyridoxal phosphate
Binding site1721Pyridoxal phosphate
Binding site2011Pyridoxal phosphate
Binding site2041Pyridoxal phosphate
Binding site2261Pyridoxal phosphate Probable
Binding site2561Pyridoxal phosphate Probable
Binding site2821Pyridoxal phosphate Probable

Amino acid modifications

Modified residue2271N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_01970

Experimental info

Mutagenesis1321D → A: Reduces binding to pyridoxal phosphate and strongly reduces catalytic activity. Ref.1
Mutagenesis1321D → E: Enhances binding to pyridoxal phosphate. Ref.1
Mutagenesis2011D → E: Enhances binding to pyridoxal phosphate. Ref.1

Secondary structure

........................................................................ 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P83788 [UniParc].

Last modified March 15, 2004. Version 1.
Checksum: 50C3DE62A20C779D

FASTA41645,905
        10         20         30         40         50         60 
MTTRNDCLAL DAQDSLAPLR QQFALPEGVI YLDGNSLGAR PVAALARAQA VIAEEWGNGL 

        70         80         90        100        110        120 
IRSWNSAGWR DLSERLGNRL ATLIGARDGE VVVTDTTSIN LFKVLSAALR VQATRSPERR 

       130        140        150        160        170        180 
VIVTETSNFP TDLYIAEGLA DMLQQGYTLR LVDSPEELPQ AIDQDTAVVM LTHVNYKTGY 

       190        200        210        220        230        240 
MHDMQALTAL SHECGALAIW DLAHSAGAVP VDLHQAGADY AIGCTYKYLN GGPGSQAFVW 

       250        260        270        280        290        300 
VSPQLCDLVP QPLSGWFGHS RQFAMEPRYE PSNGIARYLC GTQPITSLAM VECGLDVFAQ 

       310        320        330        340        350        360 
TDMASLRRKS LALTDLFIEL VEQRCAAHEL TLVTPREHAK RGSHVSFEHP EGYAVIQALI 

       370        380        390        400        410 
DRGVIGDYRE PRIMRFGFTP LYTTFTEVWD AVQILGEILD RKTWAQAQFQ VRHSVT 

« Hide

References

[1]"Three-dimensional structure of kynureninase from Pseudomonas fluorescens."
Momany C., Levdikov V., Blagova L., Lima S., Phillips R.S.
Biochemistry 43:1193-1203(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, HOMODIMERIZATION, MUTAGENESIS OF ASP-132 AND ASP-201.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QZ9X-ray1.85A1-416[»]
ProteinModelPortalP83788.
SMRP83788. Positions 2-405.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-7065.
SABIO-RKP83788.
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...

Other

EvolutionaryTraceP83788.

Entry information

Entry nameKYNU_PSEFL
AccessionPrimary (citable) accession number: P83788
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 15, 2004
Last modified: February 19, 2014
This is version 49 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways