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A1V194 (KYNU_BURMS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:BMASAVP1_A0651
OrganismBurkholderia mallei (strain SAVP1) [Complete proteome] [HAMAP]
Taxonomic identifier320388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length416 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 – 416416Kynureninase HAMAP-Rule MF_01970
PRO_0000356998

Regions

Region129 – 1324Pyridoxal phosphate binding By similarity

Sites

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

Amino acid modifications

Modified residue2271N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1V194 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 35E6734AC426EE17

FASTA41645,922
        10         20         30         40         50         60 
MKTREEALAL DRDDPLAPLR EQFALPAGVI YLDGNSLGAQ PRAAAARAQQ VIGAEWGEGL 

        70         80         90        100        110        120 
IRSWNTAGWF ALPRRLGDRL APLIGAADDE VAITDTISIN LFKLLAAMLR HQARHAPKRR 

       130        140        150        160        170        180 
VIVSERSNFP TDLYIAQGLI AQLDRDYELR LIDDPADLPD ALDDETAVAM ITHVNYRTGY 

       190        200        210        220        230        240 
MHDMPSVTQT VRQAGALMLW DLAHSAGAVP VDLNGALADG AVGCTYKYLN GGPGSPAFVW 

       250        260        270        280        290        300 
VPKRHQRAFE QPLSGWWGHR APFAMQPAFE PDPGIARFLC GTQPIVSMSM VECGLDVFAQ 

       310        320        330        340        350        360 
TDMHAIRRKS LALTDAFVAL VESRCAGQPL KLVTPRAHHQ RGSQASFEHP HGYEVMQALI 

       370        380        390        400        410 
ARGVIGDYRE PRILRFGFTP LYTRFVDVWD AVETLRDILD TEAWRAPEFA TRAAVT 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SAVP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000526 Genomic DNA. Translation: ABM52059.1.
RefSeqYP_991997.1. NC_008785.1.

3D structure databases

ProteinModelPortalA1V194.
SMRA1V194. Positions 3-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING320388.BMASAVP1_A0651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM52059; ABM52059; BMASAVP1_A0651.
GeneID4679338.
KEGGbmv:BMASAVP1_A0651.
PATRIC19154050. VBIBurMal134057_2292.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242437.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycBMAL320388:GHFL-652-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_BURMS
AccessionPrimary (citable) accession number: A1V194
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 51 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