KEGG   ENZYME: 3.5.1.84
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
Sysname
biuret amidohydrolase
Reaction(IUBMB)
biuret + H2O = urea-1-carboxylate + NH3 [RN:R05563]
Reaction(KEGG)
R05563
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
ECG: E2348C_4143
EUN: UMNK88_4650
ECP: ECP_4038
ENA: ECNA114_4133
ECOS: EC958_4305
ECV: APECO1_2632
ECM: EcSMS35_4203 EcSMS35_A0155
ECQ: ECED1_4526
EBR: ECB_03716
EBL: ECD_03716
EBE: B21_03665(ybl189)
EBD: ECBD_4201
ECC: c4769
ESE: ECSF_3681
ELC: i14_4363
ELD: i02_4363
ELF: LF82_595
ECOI: ECOPMV1_04182(rutB_2)
ECOJ: P423_21260
SEC: SCH_002
CLAP: NCTC11466_00993(rutB_1)
AHN: NCTC12129_00167(rutB)
SERF: L085_16915
EBI: EbC_35210
PAM: PANA_2400(ycdL)
PAJ: PAJ_1702(ycdL)
PVA: Pvag_1866
ETE: ETEE_3355
LRI: NCTC12151_01413(rutB)
MHQ: D650_5190
MHAT: B824_5980
MHAE: F382_05455
MHAM: J450_04800
MHAO: J451_05695
MHAL: N220_11595
MHAQ: WC39_02620
MHAY: VK67_02625
PSB: Psyr_1165
PSA: PST_1997
PKC: PKB_2171
PSEM: TO66_11265
PSET: THL1_1510
PSIL: PMA3_11175
ABY: ABAYE3593
CPS: CPS_1616
PSPO: PSPO_b1364
TNI: TVNIR_1391(ycdL_[C])
RFO: REIFOR_00277(entB)
SALN: SALB1_0448
NWE: SAMEA3174300_0048(rutB)
NZO: SAMEA4504057_1545(rutB)
LHK: LHK_01309
BMAL: DM55_3537
BMAE: DM78_4620
BMAQ: DM76_4234
BMAI: DM57_14470
BMAF: DM51_3932
BMAZ: BM44_3499
BMAB: BM45_4335
BPSE: BDL_5315
BPSM: BBQ_4221
BPSU: BBN_5374
BPSD: BBX_4480
BPK: BBK_4648
BPSH: DR55_5825
BPSA: BBU_4100
BPSO: X996_5623
BUT: X994_5186
BTQ: BTQ_3760
BTJ: BTJ_4791
BTZ: BTL_5577
BTD: BTI_5081
BTV: BTHA_4626
BTHE: BTN_5248
BTHM: BTRA_5518
BTHA: DR62_5377
BTHL: BG87_5593
BOK: DM82_6199
BOC: BG90_4465
BCJ: BCAL1772
BCEW: DM40_4913
BCEO: I35_1686
BCED: DM42_3489
BLAT: WK25_27040
BUL: BW21_4616
BXE: Bxe_B1371
CABA: SBC2_35050(rutB_1)
AMIM: MIM_c34160
AFQ: AFA_06545
RFR: Rfer_4193
AAA: Acav_3960
VEI: Veis_0839
HPSE: HPF_00345(rutB)
THI: THI_3633
AZO: azo1121
AOA: dqs_1232
ADE: Adeh_1030
HOH: Hoch_2400
MLO: mlr7064
SMER: DU99_14345
SMD: Smed_5340
SFD: USDA257_c27430(rutB)
AVI: Avi_5654
RLE: pRL100352
SHZ: shn_23570
BJA: blr6151
BRA: BRADO4247
BRS: S23_21430
AOL: S58_33410
BRAD: BF49_5478
RPT: Rpal_2912
VGO: GJW-30_1_00300(rutB)
SNO: Snov_2437
MDI: METDI2379
MEX: Mext_1705
MCH: Mchl_2024
META: Y590_08185
MAQU: Maq22A_c21355(pncA)
RVA: Rvan_3040
BVR: BVIR_3004
PLEO: OHA_1_04334(rutB_1) OHA_1_04337(rutB_2)
HDI: HDIA_3387(rutB_1)
JAN: Jann_1289
PSF: PSE_p0174
PPIC: PhaeoP14_01657(yecD)
RHC: RGUI_3084
ROH: FIU89_05155(rutB2)
LVS: LOKVESSMR4R_03011(nicF)
HBA: Hbal_2536
SMAZ: LH19_02950
SWI: Swit_1766
SPHD: HY78_16755
SPHI: TS85_05050
SPHT: K426_15875
AAY: WYH_00063(rutB_1)
ASZ: ASN_1282
SHUM: STHU_31960
RRF: F11_15420
TMO: TMO_0423(ywoC) TMO_1190(rutB) TMO_1192
PSYO: PB01_16430
BSE: Bsel_0158
EAC: EAL2_808p07130(rutB)
BPRM: CL3_04340
MPA: MAP_2378
MAO: MAP4_1445
MAVI: RC58_07165
MAVU: RE97_07165
MAV: MAV_1602
MIT: OCO_16710
MIA: OCU_16910
MID: MIP_02305
MIR: OCQ_14390
MMI: MMAR_2657
MMM: W7S_07025
MVA: Mvan_2011
MPHL: MPHLCCUG_01978(rutB)
MTHN: 4412656_01449(rutB)
MHAS: MHAS_00726(yecD_1)
MAB: MAB_3431c
MABB: MASS_3376
MCHE: BB28_17445
MSTE: MSTE_03446
MTER: 4434518_03345(yecD)
ASD: AS9A_2457
NSR: NS506_07749(rutB)
GRU: GCWB2_11585(yecD1)
GOM: D7316_02023(yecD_2)
SFA: Sfla_3437
SALS: SLNWT_1114
STRP: F750_3296
SLD: T261_7825
SMAL: SMALA_1218
SRJ: SRO_6780
CMI: CMM_2825
CMS: CMS2996
CMC: CMN_02790
NCA: Noca_0201
NDK: I601_2764(yecD)
GOB: Gobs_1017
KRA: Krad_3109
AMQ: AMETH_3961(pncA)
PSEH: XF36_01010
AMI: Amir_2477
AFS: AFR_34355
AEQ: AEQU_0892
CYA: CYA_1918
CYB: CYB_0796
LET: O77CONTIG1_01702(rutB_1) O77CONTIG1_01704(rutB_2)
HHG: XM38_018770(rutB_1) XM38_027850(rutB_2)
CTHE: Chro_4745
METM: MSMTP_1659
NEV: NTE_00794
 » show all
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)
DOI:10.1021/cs200295n
  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)
DOI:10.1074/jbc.RA118.001996
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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