KEGG   ENZYME: 3.5.1.84Help
Entry
EC 3.5.1.84                 Enzyme                                 

Name
biuret amidohydrolase;
biuH (gene name)
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
biuret amidohydrolase
Reaction(IUBMB)
biuret + H2O = urea-1-carboxylate + NH3 [RN:R05563]
Reaction(KEGG)
Substrate
biuret [CPD:C06555];
H2O [CPD:C00001]
Product
urea-1-carboxylate [CPD:C01010];
NH3 [CPD:C00014]
Comment
The enzyme, characterized from the bacterium Rhizobium leguminosarum bv. viciae 3841, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The substrate, biuret, forms by the spontaneous decarboxylation of 1-carboxybiuret in the absence of EC 3.5.1.131, 1-carboxybiuret hydrolase.
History
EC 3.5.1.84 created 2000, modified 2008, modified 2019
Pathway
ec00791  Atrazine degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K23359  biuret amidohydrolase
Genes
ECLI: ECNIH5_22650
ECLA: ECNIH3_22220
KMI: VW41_17100
GQU: AWC35_04090
CNT: JT31_17815
CEM: LH23_23140
CEN: LH86_21660
CLAP: NCTC11466_00993(rutB_1)
PSTS: E05_13680
EBI: EbC_35210
PAM: PANA_2400(ycdL)
PAJ: PAJ_1702(ycdL)
PVA: Pvag_1866
PPSE: BN5_3203
PSB: Psyr_1165
PSYR: N018_19825
PKC: PKB_2171
ADI: B5T_00748
AXE: P40_03520
RFO: REIFOR_00277(entB)
SALN: SALB1_0448
BGO: BM43_116
BXE: Bxe_B1371
BXB: DR64_6677
BFN: OI25_7099
VEI: Veis_0839
MPT: Mpe_A0766
LCH: Lcho_3023
THI: THI_3633
SCL: sce4414
MLO: mlr7064
EAD: OV14_3714
AVI: Avi_5654
RLE: pRL100352
RLG: Rleg_6453
BJA: blr6151
BRA: BRADO4247
BBT: BBta_4623
BRS: S23_21430
AOL: S58_33410
BRAD: BF49_5478
VGO: GJW-30_1_00300(rutB)
MEX: Mext_1705
MDI: METDI2379
MCH: Mchl_2024
MPO: Mpop_1111
META: Y590_08185
MAQU: Maq22A_c21355(pncA)
BBAR: RHAL1_1365
PLEO: OHA_1_04334(rutB_1)
HDI: HDIA_3387(rutB_1)
CID: P73_1299
SMAZ: LH19_02950
TMO: TMO_1192
MAGQ: MGMAQ_2602
MAB: MAB_3431c
MABB: MASS_3376
MCHE: BB28_17445
MSTE: MSTE_03446
MSAL: DSM43276_03234(rutB)
NSR: NS506_07749(rutB)
SALS: SLNWT_1114
SMAL: SMALA_1218
CMI: CMM_2825
CMS: CMS2996
CMC: CMN_02790
FAL: FRAAL6406
PSEH: XF36_01010
AFS: AFR_34355
CAI: Caci_6450
CYA: CYA_1918
LET: O77CONTIG1_01702(rutB_1)
HHG: XM38_027850(rutB_2)
METM: MSMTP_1659
NEV: NTE_00794
 » show all
Taxonomy
Reference
1  [PMID:21897878]
  Authors
Cameron SM, Durchschein K, Richman JE, Sadowsky MJ, Wackett LP
  Title
A New Family of Biuret Hydrolases Involved in S-Triazine Ring Metabolism.
  Journal
ACS Catal 2011:1075-1082 (2011)
  Sequence
[rle:pRL100352]
Reference
2  [PMID:29425231]
  Authors
Esquirol L, Peat TS, Wilding M, Lucent D, French NG, Hartley CJ, Newman J, Scott C
  Title
Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841.
  Journal
PLoS One 13:e0192736 (2018)
DOI:10.1371/journal.pone.0192736
  Sequence
[rle:pRL100352]
Reference
3  [PMID:29523689]
  Authors
Esquirol L, Peat TS, Wilding M, Liu JW, French NG, Hartley CJ, Onagi H, Nebl T, Easton CJ, Newman J, Scott C
  Title
An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme.
  Journal
J Biol Chem 293:7880-7891 (2018)
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.84
IUBMB Enzyme Nomenclature: 3.5.1.84
ExPASy - ENZYME nomenclature database: 3.5.1.84
UM-BBD (Biocatalysis/Biodegradation Database): 3.5.1.84
BRENDA, the Enzyme Database: 3.5.1.84
CAS: 95567-88-7
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