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Q6HHX7 (KYNU_BACHK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:BT9727_2523
OrganismBacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]
Taxonomic identifier281309 [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_0000356992

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
Q6HHX7 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: DB3E0D0AE1A3FC91

FASTA42848,659
        10         20         30         40         50         60 
MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA EKSLLTLLDS 

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

       130        140        150        160        170        180 
IRTKILADEL TFPSDIYALQ SQIRLKGLDP DEHLVRVKSR DGRTLSEDDI IQAMTDDIAL 

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

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

       310        320        330        340        350        360 
TAPLIGSLEI FKDAGIERLR EKSLHITRYM LNLIDHELKD FGFAIGNPLE DEKRGGHIYL 

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


ENKREVVA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017355 Genomic DNA. Translation: AAT60051.1.
RefSeqYP_036849.1. NC_005957.1.

3D structure databases

ProteinModelPortalQ6HHX7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281309.BT9727_2523.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT60051; AAT60051; BT9727_2523.
GeneID2855106.
KEGGbtk:BT9727_2523.
PATRIC18985889. VBIBacThu119411_2671.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAHVAYRSA.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycBTHU281309:GJID-2603-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_BACHK
AccessionPrimary (citable) accession number: Q6HHX7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 70 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