KEGG   ENZYME: 3.5.2.15Help
Entry
EC 3.5.2.15                 Enzyme                                 

Name
cyanuric acid amidohydrolase;
AtzD
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In cyclic amides
BRITE hierarchy
Sysname
cyanuric acid amidohydrolase
Reaction(IUBMB)
cyanuric acid + H2O = biuret + CO2 [RN:R07305]
Reaction(KEGG)
R07305;
(other) R05561
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Substrate
cyanuric acid [CPD:C06554];
H2O [CPD:C00001]
Product
biuret [CPD:C06555];
CO2 [CPD:C00011]
Comment
Along with EC 3.5.1.54 (allophanate hydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. This is a key enzyme in the pathway, catalysing the ring cleavage of cyanuric acid. The enzyme is specific for cyanuric acid as substrate as neither the structurally related compounds ammeline (2,4-diamino-6-hydroxy-s-triazine) and ammelide (2-amino-4,6-dihydroxy-s-triazine) nor a number of pyrimidine compounds, such as uracil and cytosine, can act as substrates [3].
History
EC 3.5.2.15 created 2000, modified 2008
Pathway
ec00791  Atrazine degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K03383  cyanuric acid amidohydrolase
Genes
PPSE: BN5_3198(trzD)
ADI: B5T_00742
AXE: P40_03495
ACII: C4901_13330
VPD: VAPA_1c50370
VAA: AX767_09230
CSER: CCO03_17450
HYB: Q5W_10340
RGU: A4W93_01790
AVI: Avi_5653
RLE: pRL100353(atzD)
RLG: Rleg_6452
RHL: LPU83_pLPU83c0721(atzD)
BJA: blr7281(atzD)
BRA: BRADO6319(atzD)
BBT: BBta_1315(atzD)
BRS: S23_59060(atzD)
AOL: S58_64660
BRAD: BF49_2819
BRO: BRAD285_6240(atzD)
MET: M446_3816
MOR: MOC_0480
HDI: HDIA_3388(trzD)
CID: P73_3150
AFR: AFE_0779
ACU: Atc_m024
SAY: TPY_1352
MTA: Moth_2120
GOR: KTR9_4373
PDX: Psed_3188
 » show all
Taxonomy
Reference
1  [PMID:1991731]
  Authors
Eaton RW, Karns JS.
  Title
Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine-degrading bacterial strains.
  Journal
J Bacteriol 173:1363-6 (1991)
DOI:10.1128/JB.173.3.1363-1366.1991
  Sequence
Reference
2  [PMID:1846859]
  Authors
Eaton RW, Karns JS.
  Title
Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227.
  Journal
J Bacteriol 173:1215-22 (1991)
DOI:10.1128/JB.173.3.1215-1222.1991
  Sequence
Reference
3  [PMID:10427042]
  Authors
Karns JS.
  Title
Gene sequence and properties of an s-triazine ring-cleavage enzyme from Pseudomonas sp. strain NRRLB-12227.
  Journal
Appl Environ Microbiol 65:3512-7 (1999)
  Sequence
Reference
4  [PMID:12788776]
  Authors
Fruchey I, Shapir N, Sadowsky MJ, Wackett LP.
  Title
On the origins of cyanuric acid hydrolase: purification, substrates, and prevalence of AtzD from Pseudomonas sp. strain ADP.
  Journal
Appl Environ Microbiol 69:3653-7 (2003)
DOI:10.1128/AEM.69.6.3653-3657.2003
Other DBs
ExplorEnz - The Enzyme Database: 3.5.2.15
IUBMB Enzyme Nomenclature: 3.5.2.15
ExPASy - ENZYME nomenclature database: 3.5.2.15
UM-BBD (Biocatalysis/Biodegradation Database): 3.5.2.15
BRENDA, the Enzyme Database: 3.5.2.15
CAS: 132965-78-7

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