KEGG   ENZYME: 3.5.1.54Help
Entry
EC 3.5.1.54                 Enzyme                                 

Name
allophanate hydrolase;
allophanate lyase;
AtzF;
TrzF
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
urea-1-carboxylate amidohydrolase
Reaction(IUBMB)
urea-1-carboxylate + H2O = 2 CO2 + 2 NH3 [RN:R00005]
Reaction(KEGG)
Substrate
urea-1-carboxylate [CPD:C01010];
H2O [CPD:C00001]
Product
CO2 [CPD:C00011];
NH3 [CPD:C00014]
Comment
Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) 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. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate [6].
History
EC 3.5.1.54 created 1986, modified 2008
Pathway
Arginine and proline metabolism
Atrazine degradation
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K01457  
allophanate hydrolase
K14541  
urea carboxylase / allophanate hydrolase
Genes
SCE: 
YBR208C(DUR1)
AGO: 
ERC: 
KLA: 
LTH: 
PPA: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0B02280(NCAS0B02280)
NDI: 
NDAI_0C05400(NDAI0C05400)
TPF: 
TPHA_0L01560(TPHA0L01560)
TDL: 
TDEL_0B03290(TDEL0B03290)
DHA: 
PIC: 
PGU: 
LEL: 
CAL: 
CaO19.780(DUR1) CaO19.8402(DUR1)
CTP: 
CDU: 
COT: 
YLI: 
CLU: 
FGR: 
NHE: 
VAL: 
SEX: 
ECA: 
PCT: 
PCC: 
PWA: 
PEC: 
ETA: 
EBI: 
ENC: 
ESA: 
CSK: 
CSZ: 
CTU: 
KPE: 
KPK_2627(atzF)
KVA: 
KOX: 
SPE: 
SRR: 
SRL: 
SRS: 
SRA: 
SMAF: 
SMW: 
SLQ: 
DDC: 
DDD: 
DZE: 
PLF: 
PAQ: 
PVA: 
Pvag_0053(uaha3)
PAO: 
RAH: 
RAQ: 
RAA: 
EBF: 
XAC: 
XAC4327(uahA)
XCI: 
XAO: 
PST: 
PSB: 
PSP: 
PFO: 
PEN: 
PMY: 
PMK: 
PSA: 
PFV: 
PRE: 
CJA: 
ACD: 
ACB: 
ABY: 
ABC: 
ABN: 
ABB: 
ABX: 
ABZ: 
ABR: 
ABD: 
ABH: 
ABAD: 
ABJ: 
ABAB: 
ABAJ: 
ACC: 
PHA: 
SDE: 
MAD: 
PIN: 
TTU: 
TCX: 
AEH: 
HHA: 
TGR: 
HNA: 
ABO: 
ADI: 
TOL: 
TAU: 
REU: 
BVI: 
BUR: 
BCH: 
BCM: 
BCJ: 
BXE: 
BPH: 
BPY: 
BUG: 
BGE: 
BGD: 
BPT: 
Bpet0294(uahA)
BAV: 
AXY: 
AXO: 
RFR: 
PNA: 
VEI: 
VAP: 
VPE: 
MPT: 
MMS: 
mma_3078(uahA)
HSE: 
LCH: 
NMU: 
AZO: 
DAR: 
MEH: 
MEP: 
MPQ_0993(gatA)
SLT: 
GCA: 
WSU: 
WS1118(gatA)
SKU: 
ANT: 
MLO: 
MOP: 
PLA: 
RHI: 
SFD: 
ARA: 
AVI: 
RET: 
REC: 
RLE: 
RLT: 
RLG: 
RTR: 
BJA: 
BJU: 
BRA: 
BBT: 
BRS: 
AOL: 
RPA: 
RPB: 
RPC: 
RPD: 
RPE: 
RPT: 
RPX: 
XAU: 
AZC: 
SNO: 
MEX: 
MEA: 
MDI: 
MCH: 
MRD: 
MET: 
MPO: 
MSL: 
PHL: 
CCR: 
CCS: 
CAK: 
AEX: 
RSP: 
JAN: 
RDE: 
RLI: 
HNE: 
NAR: 
SJP: 
GBE: 
ACR: 
APT: 
RRU: 
AZL: 
PGV: 
BMD: 
BMD_0981(atzF)
PJD: 
AAC: 
EHA: 
CLE: 
SGY: 
MSM: 
MVA: 
MAB: 
MMC: 
MKM: 
MJL: 
ASD: 
CEF: 
NFA: 
RHA: 
RER: 
ROP: 
REQ: 
GBR: 
TPR: 
SRT: 
SMA: 
SCB: 
CMI: 
CMS: 
ART: 
AAU: 
AAur_0186(atzF)
SKE: 
CFL: 
FRI: 
FAL: 
NML: 
KRA: 
AMD: 
AMED_2634(amiE)
PDX: 
CAI: 
CAA: 
ACM: 
SUS: 
CYN: 
GVI: 
 » show all
Taxonomy
Reference
1
  Authors
Maitz, G.S., Haas, E.M. and Castric, P.A.
  Title
Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii.
  Journal
Biochim. Biophys. Acta 714 (1982) 486-491.
Reference
2  [PMID:4556303]
  Authors
Roon RJ, Levenberg B.
  Title
Urea amidolyase. I. Properties of the enzyme from Candida utilis.
  Journal
J. Biol. Chem. 247 (1972) 4107-13.
  Organism
Candida utilis
Reference
3  [PMID:6124544]
  Authors
Sumrada RA, Cooper TG.
  Title
Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast.
  Journal
J. Biol. Chem. 257 (1982) 9119-27.
  Organism
Saccharomyces cerevisiae
Reference
4  [PMID:15796980]
  Authors
Kanamori T, Kanou N, Kusakabe S, Atomi H, Imanaka T.
  Title
Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea.
  Journal
FEMS. Microbiol. Lett. 245 (2005) 61-5.
  Organism
Oleomonas sagaranensis
Reference
5  [PMID:16085834]
  Authors
Cheng G, Shapir N, Sadowsky MJ, Wackett LP.
  Title
Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism.
  Journal
Appl. Environ. Microbiol. 71 (2005) 4437-45.
  Organism
Enterobacter cloacae, Pseudomonas huttiensis, Pseudomonas sp.
Reference
6  [PMID:15901697]
  Authors
Shapir N, Sadowsky MJ, Wackett LP.
  Title
Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP.
  Journal
J. Bacteriol. 187 (2005) 3731-8.
  Organism
Pseudomonas sp.
  Sequence
Reference
7  [PMID:16597948]
  Authors
Shapir N, Cheng G, Sadowsky MJ, Wackett LP.
  Title
Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth.
  Journal
Appl. Environ. Microbiol. 72 (2006) 2491-5.
  Organism
Enterobacter cloacae
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 
CAS: 
9076-72-6

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