| Entry |
|
| Name |
urea carboxylase;
urease (ATP-hydrolysing);
urea carboxylase (hydrolysing);
ATP---urea amidolyase;
urea amidolyase;
UALase;
UCA |
| Class |
Ligases;
Forming carbon-nitrogen bonds;
Other carbon-nitrogen ligases
 |
| Sysname |
urea:carbon-dioxide ligase (ADP-forming) |
| Reaction(IUBMB) |
ATP + urea + HCO3- = ADP + phosphate + urea-1-carboxylate
[RN:R00774] |
| Reaction(KEGG) |
R00774
 |
| Substrate |
ATP [CPD:C00002];
urea [CPD:C00086];
HCO3- [CPD:C00288] |
| Product |
ADP [CPD:C00008];
phosphate [CPD:C00009];
urea-1-carboxylate [CPD:C01010] |
| Cofactor |
Biotin [CPD:C00120] |
| Comment |
A biotinyl-protein. The yeast enzyme (but not that from green algae)
also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase,
thus bringing about the hydrolysis of urea to CO2 and NH3.
Previously also listed as EC 3.5.1.45. The enzyme from the
prokaryotic bacterium Oleomonas sagaranensis can also use acetamide
and formamide as substrates [4]. |
| Pathway |
PATH: ec00330 Arginine and proline metabolism
PATH: ec01100 Metabolic pathways |
| Orthology |
KO: K01941 urea carboxylase |
| Genes |
SCE: YBR208C(DUR1)
AGO: AGOS_ADR051C
KLA: KLLA0E08107g
DHA: DEHA0D07777g
PIC: PICST_28452(DUR1)
VPO: Kpol_299p2
CAL: CaO19.780(DUR1)
CGR: CAGL0M05533g
YLI: YALI0E07271g
MGR: MGG_04386
FGR: FG10913.1
ECA: ECA2142
PCT: PC1_2163
ETA: ETA_06880(uahA)
ESA: ESA_01768
SPE: Spro_1419
DZE: Dd1591_2748
XAC: XAC4326(uahA)
PSP: PSPPH_3975
PMY: Pmen_0703
CJA: CJA_1243
SAZ: Sama_0022
SLO: Shew_0007
BMA: BMAA1883
BMV: BMASAVP1_0896
BML: BMA10229_1182
BMN: BMA10247_A2159
BPS: BPSS0195
BPM: BURPS1710b_A1720
BPL: BURPS1106A_A0271
BPD: BURPS668_A0363
BCM: Bcenmc03_2954
BPT: Bpet0293
VEI: Veis_0373 Veis_4580 Veis_4581
NET: Neut_2475
RLE: pRL120151 pRL90293
BBT: BBta_2438
RPE: RPE_1219 RPE_1220
SIT: TM1040_3255
GBE: GbCGDNIH1_1745
MSM: MSMEG_2187
RHA: RHA1_ro02135
AAU: AAur_0187(uca)
ACE: Acel_0594
SUS: Acid_3428
GVI: gll0958
TTH: TTC0624
 |
Reference Authors Title Journal
|
1
Roon, R.J. and Levenberg, B.
ATP-Urea amidolyase (ADP) (Candida utilis).
Methods Enzymol. 17A (1970) 317-324. |
Reference Authors Title Journal Organism
|
2 [PMID:4556303]
Roon RJ, Levenberg B.
Urea amidolyase. I. Properties of the enzyme from Candida utilis.
J. Biol. Chem. 247 (1972) 4107-13.
Candida utilis |
Reference Authors Title
Journal Organism
|
3 [PMID:6124544]
Sumrada RA, Cooper TG.
Urea carboxylase and allophanate hydrolase are components of a
multifunctional protein in yeast.
J. Biol. Chem. 257 (1982) 9119-27.
Candida utilis, Saccharomyces cerevisiae [GN:sce] |
Reference Authors Title Journal Organism Sequence
|
4 [PMID:15090492]
Kanamori T, Kanou N, Atomi H, Imanaka T.
Enzymatic characterization of a prokaryotic urea carboxylase.
J. Bacteriol. 186 (2004) 2532-9.
Oleomonas sagaranensis
NCBI-GI: 46409051 |
| Other DBs |
ExplorEnz - The Enzyme Database: 6.3.4.6
IUBMB Enzyme Nomenclature: 6.3.4.6
ExPASy - ENZYME nomenclature database: 6.3.4.6
BRENDA, the Enzyme Database: 6.3.4.6
CAS: 9058-98-4 |