Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

G8U7W8 (G8U7W8_BACCE) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 18. 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:bcf_13480 EMBL AEW55818.1
OrganismBacillus cereus F837/76 [Complete proteome] EMBL AEW55818.1
Taxonomic identifier347495 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length428 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 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

Region132 – 1354Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site1041Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1051Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2131Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2161Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2381Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2671Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2951Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2391N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
G8U7W8 [UniParc].

Last modified February 22, 2012. Version 1.
Checksum: A880205EBFA30139

FASTA42848,782
        10         20         30         40         50         60 
MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA EKSLFTLLDS 

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

       130        140        150        160        170        180 
IRIKILADEL TFPSDIYALQ SQIRLKGLDP DEHLVRVKSR DGRTLSEDDI IHAMTDDVAL 

       190        200        210        220        230        240 
ILLPSVLYRS GQILDMKRLT AEAHKRGIHI GFDLCHSIGS IPHHFKEWDV DFAIWCNYKY 

       250        260        270        280        290        300 
LNAGPGGVAG LYVNKKHFNR LPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHVLS 

       310        320        330        340        350        360 
TAPLIGSLEM FKDAGIERLR EKSLHITRYM LNLIDHELKD FGFTIGNPFE DEKRGGHIYL 

       370        380        390        400        410        420 
EHAEAARICK ALKANGVIPD FRAPNGVRLA PVALYNTYEE VWQSVMILKK IMKDEEYKQF 


ENKREVVA 

« Hide

References

[1]"Complete Genome Sequence of the Highly Hemolytic Strain Bacillus cereus F837/76."
Auger S., Galleron N., Segurens B., Dossat C., Bolotin A., Wincker P., Sorokin A.
J. Bacteriol. 194:1630-1630(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: F837/76 EMBL AEW55818.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003187 Genomic DNA. Translation: AEW55818.1.
RefSeqYP_005119331.1. NC_016779.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEW55818; AEW55818; bcf_13480.
GeneID11679037.
KEGGbcf:bcf_13480.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01556.

Enzyme and pathway databases

BioCycBCER347495:GHGC-2696-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 nameG8U7W8_BACCE
AccessionPrimary (citable) accession number: G8U7W8
Entry history
Integrated into UniProtKB/TrEMBL: February 22, 2012
Last sequence update: February 22, 2012
Last modified: July 9, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)