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Reviewed, UniProtKB/Swiss-Prot B1YHD6 (KYNU_EXIS2)

Last modified November 3, 2009. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 lineageBacteriaFirmicutesBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

L-kynurenine + H2O = anthranilate + L-alanine.

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1.

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the kynureninase family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   LigandPyridoxal phosphate
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

tryptophan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionkynureninase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Kynureninase
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
B1YHD6-1 [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."
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].

Cross-references

Sequence databases

CP001022 Genomic DNA. Translation: ACB59668.1.
RefSeqYP_001812685.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6173872.
GenomeReviewsGene locus Exig_0182 in contig CP001022_GR.
KEGGesi:Exig_0182.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMANFPTDVY.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
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: November 3, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents