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K0HWX1 (K0HWX1_9BURK) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Kynureninase PIRNR PIRNR038800 HAMAP-Rule MF_01970

EC=3.7.1.3 PIRNR PIRNR038800 HAMAP-Rule MF_01970
Alternative name(s):
L-kynurenine hydrolase HAMAP-Rule MF_01970
Gene names
Name:kynU HAMAP-Rule MF_01970
ORF Names:C380_18720 EMBL AFU47438.1
OrganismAcidovorax sp. KKS102 [Complete proteome] EMBL AFU47438.1
Taxonomic identifier358220 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length449 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. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Catalytic activity

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_01970

L-kynurenine + H2O = anthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Cofactor

Pyridoxal phosphate By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Subunit structure

Homodimer By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Sequence similarities

Belongs to the kynureninase family. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region130 – 1334Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site981Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site991Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1701Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1991Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2021Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2241Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2581Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2841Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2251N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
K0HWX1 [UniParc].

Last modified November 28, 2012. Version 1.
Checksum: EDF276613DC7A779

FASTA44947,851
        10         20         30         40         50         60 
MPITFQDCRT RDAQDPLRAL RDHFALPPGV IYLDGNSLGV APKAAAARVA DVVTREWGTD 

        70         80         90        100        110        120 
LIKSWNTASW FDLPQRLGNQ LAPLIGAGKD EVVCTDSTSI NLYKVLSAAL NIAREDSPAR 

       130        140        150        160        170        180 
KRIVSERSNF PTDLYIAEGL CKERGLELVL VEPEEIAASL TSDVAVLMLT HVNYRTGAMH 

       190        200        210        220        230        240 
DMAAITAAAH AQGILCVWDL AHSAGAVPVD LNGAGADFSI GCGYKYLNGG PGAPAFVWVH 

       250        260        270        280        290        300 
PRHANRPDLK FMQPLSGWWG HAAPFAFTPD YQPAPGITRY LCGTQPIISL SALQCGLDVF 

       310        320        330        340        350        360 
TAAQGLGGMA ALRTKSLALT DLFIQLVEER CAGHGLGLAT PRDHAQRGSQ VCLTRDEGAG 

       370        380        390        400        410        420 
VGGQGSGAYA IVQALIARGV IGDFRAGSGA APDAGKGDGG TGHKDILRFG FTPLYLGFED 

       430        440 
VWNAVEHMRQ VLESGEWQKA EFNQTHAVT 

« Hide

References

[1]"Complete Genome Sequence of Acidovorax sp. Strain KKS102, a Polychlorinated-Biphenyl Degrader."
Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.
J. Bacteriol. 194:6970-6971(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: KKS102 EMBL AFU47438.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003872 Genomic DNA. Translation: AFU47438.1.
RefSeqYP_006856076.1. NC_018708.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFU47438; AFU47438; C380_18720.
GeneID13788168.
KEGGack:C380_18720.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01556.

Enzyme and pathway databases

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 nameK0HWX1_9BURK
AccessionPrimary (citable) accession number: K0HWX1
Entry history
Integrated into UniProtKB/TrEMBL: November 28, 2012
Last sequence update: November 28, 2012
Last modified: February 19, 2014
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)