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B7H888 (B7H888_BACC4) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 36. 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 EMBL ACK62025.1
Ordered Locus Names:BCB4264_A2766 EMBL ACK62025.1
OrganismBacillus cereus (strain B4264) [Complete proteome] [HAMAP] EMBL ACK62025.1
Taxonomic identifier405532 [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. 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
B7H888 [UniParc].

Last modified February 10, 2009. 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 

« Hide

References

[1]"Genome sequence of Bacillus cereus B4264."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B4264 EMBL ACK62025.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001176 Genomic DNA. Translation: ACK62025.1.
RefSeqYP_002367474.1. NC_011725.1.

3D structure databases

ProteinModelPortalB7H888.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405532.BCB4264_A2766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK62025; ACK62025; BCB4264_A2766.
GeneID7097643.
KEGGbcb:BCB4264_A2766.
PATRIC18877455. VBIBacCer117876_2634.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.
ProtClustDBCLSK904618.

Enzyme and pathway databases

BioCycBCER405532:GI1K-2741-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 nameB7H888_BACC4
AccessionPrimary (citable) accession number: B7H888
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)