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B1YHD6 (KYNU_EXIS2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:Exig_0182
OrganismExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15) [Complete proteome] [HAMAP]
Taxonomic identifier262543 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length425 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 – 425425Kynureninase HAMAP-Rule MF_01970
PRO_0000357004

Regions

Region129 – 1324Pyridoxal phosphate binding By similarity

Sites

Binding site1011Pyridoxal phosphate; via amide nitrogen By similarity
Binding site1021Pyridoxal phosphate By similarity
Binding site2101Pyridoxal phosphate By similarity
Binding site2131Pyridoxal phosphate By similarity
Binding site2351Pyridoxal phosphate By similarity
Binding site2641Pyridoxal phosphate By similarity
Binding site2921Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2361N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1YHD6 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 8BDA1A8D2351607D

FASTA42547,194
        10         20         30         40         50         60 
MTLTAPRKHA IEQDQQDALA PYRNEFYLQE GSIYMDGNSL GLLSKRAEAT LLESLADWRE 

        70         80         90        100        110        120 
LGIDGWMKGR HPWFDLSEKL AALNAPLVGG RADEVMVTGS TTVNLHQLVA TFFAPSGRRT 

       130        140        150        160        170        180 
KILADSLTFP SDIYALQSQL RLRGLDPAEH LVQVESRDGR FLDEADIIAA MTDDIALIVL 

       190        200        210        220        230        240 
PTVLYRSGQI LDMERLTREA HARGILIGFD GCHSVGAIPH AFHDWGVDFA YWCNYKHLNG 

       250        260        270        280        290        300 
GPGTVGGLFV HERHFGTLPG LTGWFGSRKD KQFDMNHTMT PAENAAAFQI GTPHVLSLAP 

       310        320        330        340        350        360 
QIGALELFAE VGIDAVRAKS LALTDYMMTL VDQELTAYGF VIGNPRDAKR RGAHLSLEHP 

       370        380        390        400        410        420 
EAARICKALK AHQVIPDFRA PNIVRLAPVA LYNSFEDVYE VVSILKTIMD EKQYEQFKNE 


REVVA 

« Hide

References

[1]"Complete sequence of chromosome of Exiguobacterium sibiricum 255-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17290 / JCM 13490 / 255-15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001022 Genomic DNA. Translation: ACB59668.1.
RefSeqYP_001812685.1. NC_010556.1.

3D structure databases

ProteinModelPortalB1YHD6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262543.Exig_0182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB59668; ACB59668; Exig_0182.
GeneID6173872.
KEGGesi:Exig_0182.
PATRIC32133885. VBIExiSib53410_0194.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycESIB262543:GHBP-233-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_EXIS2
AccessionPrimary (citable) accession number: B1YHD6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 42 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