C1D325
C1D325_DEIDV
Kynureninase
3.7.1.3
L-kynurenine hydrolase
kynU
Deide_2p01450
Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115)
Bacteria
Deinococcota
Deinococci
Deinococcales
Deinococcaceae
Deinococcus
pDeide2
Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti.
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
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.
3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) + L-alanine
H2O + L-kynurenine = anthranilate + H(+) + L-alanine
pyridoxal 5'-phosphate
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.
Homodimer.
Belongs to the kynureninase family.
Hydrolase
Plasmid
Pyridine nucleotide biosynthesis
Pyridoxal phosphate
Reference proteome
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
MTTPVLSAKPALSTLLDLDARDPLQHKKAQFVLPEGVIYLDGNSLGALPATVPARLERVIHQEWGDALIRSWTAHAQEGRDWMALPDRVAAKLAPLIGAEASEISVGDSTSVNLFKALTAALDVASPGRRVILTDADNFPTDLYVAQGLNGLLDGRYELRRVPAAELSAHLTTDVAAMMVTEVDYRTGERLDMASLTAQAHAQGIVTIWDLAHSAGAFEVDLTAARADFAVGCGYKYLNGGPGAPGYLFVASRHLQARVALSGWMGHADPFEMARDYTPAKDARRFIVGTPTVLSLSALDTALDVFADVDLKQLRAKSLALTDTFMALVAGDPDLTLVTPLDHARRGSQVSFRHPQAREAMRRLVERGVIGDFRTPDILRFGFTPLYVSYADVYRAAQAVLDVAGELRA
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