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Q5WKB5 (KYNU_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:ABC0651
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length427 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 – 427427Kynureninase HAMAP-Rule MF_01970
PRO_0000356993

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
Q5WKB5 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 19F67CEC50D893AC

FASTA42748,667
        10         20         30         40         50         60 
MPCFDSVYTK EYAQQLDAVD PLARFRNEFY IDEDSIYLDG NSLGLLSTRA EQSLLDVLDS 

        70         80         90        100        110        120 
WKQYGIDGWT KGKHPWFYLS ESLGEKMASL VGAKAEEVIV TGSTTTNLHQ LVSSFFRPEG 

       130        140        150        160        170        180 
KKTKILADEL NFPSDIYALK SQLHLQGFDP EEHLIQVKSD NGHLLNEEDI IAEMKEDIAL 

       190        200        210        220        230        240 
IVLPSVLYRS GQILDMERLT TAAHQRNILI GFDLCHSIGA IPHQLRKWDV DFAFWCTYKH 

       250        260        270        280        290        300 
VNGGPGSVAA LFVNEKHFGR RPGLAGWFSS NKQKQFDMEH TLTPAEHAGA FQIGTPHIFS 

       310        320        330        340        350        360 
IAPLIGSLAI FAEAGIEQIR KKSLKLTDYM MTLIEHELSD YQFTIQNPRD ERRGAHLYIE 

       370        380        390        400        410        420 
HDEAARICKA LKEENVIPDF RSPKGIRLAP VALYNTFKEV WNTIQVLKFI MKEERYKKFK 


NERDVVA 

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References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD63190.1.
RefSeqYP_174151.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WKB5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC0651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD63190; BAD63190; ABC0651.
GeneID3204717.
KEGGbcl:ABC0651.
PATRIC18920560. VBIBacCla58185_0685.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBCLA66692:GHMP-681-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_BACSK
AccessionPrimary (citable) accession number: Q5WKB5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 66 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