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Q81CK0 (KYNU_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:BC_2759
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length428 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 – 428428Kynureninase HAMAP-Rule MF_01970
PRO_0000356990

Regions

Region132 – 1354Pyridoxal phosphate binding By similarity

Sites

Binding site1041Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1051Pyridoxal phosphate By similarity
Binding site2131Pyridoxal phosphate By similarity
Binding site2161Pyridoxal phosphate By similarity
Binding site2381Pyridoxal phosphate By similarity
Binding site2671Pyridoxal phosphate By similarity
Binding site2951Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2391N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81CK0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 39B9A789AE41714F

FASTA42848,754
        10         20         30         40         50         60 
MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA EKSLLTLLDS 

        70         80         90        100        110        120 
WKEYGIDGWT EGEHPWFFLS EKLGKLTAPL IGALPEETIV TGSTTTNIHQ VIATFYEPKG 

       130        140        150        160        170        180 
IRTKILADEL TFPSDIYALQ SQIRLKGLDP EEHLVRVKSR DGRTLSEEDI IHAMEDDIAL 

       190        200        210        220        230        240 
ILLPSVLYRS GQILDMKRLT TEAHKRGIHI GFDLCHSIGS IPHHFKDWDV DFAVWCNYKY 

       250        260        270        280        290        300 
LNAGPGSVAG LYVNSKHFNR LPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHVLS 

       310        320        330        340        350        360 
TAPLIGSLEI FKDAGIERLR EKSLHITRYM LNLIGHELKD FEFTIGNPLE DEKRGGHIYL 

       370        380        390        400        410        420 
EHAEAARICK ALKANGVIPD FRAPNGVRLA PVALYNTYEE VWKSVQILKK IMKNEEYKQF 


ENKREVVA 

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References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP09712.1.
RefSeqNP_832511.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ81CK0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC2759.

Proteomic databases

PRIDEQ81CK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP09712; AAP09712; BC_2759.
GeneID1205107.
KEGGbce:BC2759.
PATRIC32601419. VBIBacCer54481_2814.

Phylogenomic databases

eggNOGCOG3844.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycBCER226900:GJEU-2758-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_BACCR
AccessionPrimary (citable) accession number: Q81CK0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 72 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