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C1D325 (C1D325_DEIDV) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 34. 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
Ordered Locus Names:Deide_2p01450 EMBL ACO47814.1
Encoded onPlasmid pDeide2
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP] EMBL ACO47814.1
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Region139 – 1424Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site1101Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1111Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1811Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2101Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2131Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2351Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2641Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2901Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2361N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
C1D325 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 4DFE06C0F2B2F327

FASTA40944,171
        10         20         30         40         50         60 
MTTPVLSAKP ALSTLLDLDA RDPLQHKKAQ FVLPEGVIYL DGNSLGALPA TVPARLERVI 

        70         80         90        100        110        120 
HQEWGDALIR SWTAHAQEGR DWMALPDRVA AKLAPLIGAE ASEISVGDST SVNLFKALTA 

       130        140        150        160        170        180 
ALDVASPGRR VILTDADNFP TDLYVAQGLN GLLDGRYELR RVPAAELSAH LTTDVAAMMV 

       190        200        210        220        230        240 
TEVDYRTGER LDMASLTAQA HAQGIVTIWD LAHSAGAFEV DLTAARADFA VGCGYKYLNG 

       250        260        270        280        290        300 
GPGAPGYLFV ASRHLQARVA LSGWMGHADP FEMARDYTPA KDARRFIVGT PTVLSLSALD 

       310        320        330        340        350        360 
TALDVFADVD LKQLRAKSLA LTDTFMALVA GDPDLTLVTP LDHARRGSQV SFRHPQAREA 

       370        380        390        400 
MRRLVERGVI GDFRTPDILR FGFTPLYVSY ADVYRAAQAV LDVAGELRA 

« Hide

References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Plasmid 2 and VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001116 Genomic DNA. Translation: ACO47814.1.
RefSeqYP_002787916.1. NC_012529.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING546414.Deide_2p01450.

Proteomic databases

PaxDbC1D325.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO47814; ACO47814; Deide_2p01450.
GeneID7740681.
KEGGddr:Deide_2p01450.
PATRIC21620493. VBIDeiDes121019_3511.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242437.
KOK01556.
OMAYACESHI.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycDDES546414:GHOM-3432-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 nameC1D325_DEIDV
AccessionPrimary (citable) accession number: C1D325
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: July 9, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)