Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q1LCS5 (Q1LCS5_RALME) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 40. 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·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Kynureninase PIRNR PIRNR038800
EC=3.7.1.3 PIRNR PIRNR038800
Gene names
Ordered Locus Names:Rmet_5192
Encoded onPlasmid megaplasmid CH34
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length409 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. PIRNR PIRNR038800

Catalytic activity

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. PIRNR PIRNR038800

L-kynurenine + H2O = anthranilate + L-alanine. PIRNR PIRNR038800

Cofactor

Pyridoxal phosphate By similarity. PIRNR PIRNR038800

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. PIRNR PIRNR038800

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. PIRNR PIRNR038800

Subunit structure

Homodimer By similarity. PIRNR PIRNR038800

Sequence similarities

Belongs to the kynureninase family. PIRNR PIRNR038800

Sequences

Sequence LengthMass (Da)Tools
Q1LCS5 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: D6AFFBC5AC4735C5

FASTA40944,655
        10         20         30         40         50         60 
MMIREDCAAL DAADKLAGCR ARFALPAGTI YLDGNSLGAM PANVPARMKV AIEQEWAEGL 

        70         80         90        100        110        120 
IRSWNDADWY PAPQRTGDRI ARLIGAGQGE VIVADSTSVN LFKVLVAATR MRPGRGVILA 

       130        140        150        160        170        180 
ERTNFPTDVY IAESVAEMTG CELRCVDPEE VMSAIDENVA IVSLTHVNYK TGKRYDMEAM 

       190        200        210        220        230        240 
TRRAHEAGAL VVWDLCHTAG AMPVYLNRCE VDFAVGCGYK YLNGGPGAPA FVFVASRHLE 

       250        260        270        280        290        300 
HVRQPLSGWH GHAQPFAFTH EYAPHAGIDR MLTGTAPQLG LISLESALEA FDGVDMEALR 

       310        320        330        340        350        360 
EKSVSLGDLF ITLAEQELAG LGFTLATPRD ADQRGSQVSL RHAEGYAIMQ ALIARNIIGD 

       370        380        390        400 
FRAPDILRFG FAALYVRHVD IWDTIAALKD IVTSEAWNTE AFRTRKSVT

« Hide

References

[1]"Complete sequence of the megaplasmid of Ralstonia metallidurans CH34."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000353 Genomic DNA. Translation: ABF12051.1.
RefSeqYP_587320.1. NC_007974.2.

3D structure databases

ProteinModelPortalQ1LCS5.
SMRQ1LCS5. Positions 3-397.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LCS5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4042053.
GenomeReviewsGene locus Rmet_5192 in contig CP000353_GR.
KEGGrme:Rmet_5192.
PATRIC20295144. VBIRalMet4734_5614.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHBG523016.
OMANFPTDVY.
PhylomeDBQ1LCS5.
ProtClustDBCLSK769898.

Enzyme and pathway databases

BioCycRMET266264:RMET_5192-MONOMER.

Family and domain databases

InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK01556.
PANTHERPTHR14084. Kynureninase. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. Kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ1LCS5_RALME
AccessionPrimary (citable) accession number: Q1LCS5
Entry history
Integrated into UniProtKB/TrEMBL: May 30, 2006
Last sequence update: May 30, 2006
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info