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dCTP deaminase from Escherichia coli in complex with dUTP External Resource: Annotation Domain Annotation: SCOP2 Classification SCOP2 Database Homepage Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) A SCOP2 Family dUTPase-like 8031769 4002970 SCOP2 (2022-06-29) A SCOP2 Superfamily dUTPase-like 8044147 3001957 SCOP2 (2022-06-29) C SCOP2B Superfamily dUTPase-like 8044147 3001957 SCOP2B (2022-06-29) E SCOP2B Superfamily dUTPase-like 8044147 3001957 SCOP2B (2022-06-29) B SCOP2B Superfamily dUTPase-like 8044147 3001957 SCOP2B (2022-06-29) D SCOP2B Superfamily dUTPase-like 8044147 3001957 SCOP2B (2022-06-29) F SCOP2B Superfamily dUTPase-like 8044147 3001957 SCOP2B (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A PF22769 e1xs1A1 A: beta barrels X: beta-clip H: dUTPase-like (From Topology) T: dUTPase-like F: PF22769 ECOD (1.6) C PF22769 e1xs1C1 A: beta barrels X: beta-clip H: dUTPase-like (From Topology) T: dUTPase-like F: PF22769 ECOD (1.6) E PF22769 e1xs1E1 A: beta barrels X: beta-clip H: dUTPase-like (From Topology) T: dUTPase-like F: PF22769 ECOD (1.6) B PF22769 e1xs1B1 A: beta barrels X: beta-clip H: dUTPase-like (From Topology) T: dUTPase-like F: PF22769 ECOD (1.6) D PF22769 e1xs1D1 A: beta barrels X: beta-clip H: dUTPase-like (From Topology) T: dUTPase-like F: PF22769 ECOD (1.6) F PF22769 e1xs1F1 A: beta barrels X: beta-clip H: dUTPase-like (From Topology) T: dUTPase-like F: PF22769 ECOD (1.6)
Chains Accession Name Description Comments Source PF00692 dUTPase (dUTPase) dUTPase dUTPase hydrolyses dUTP to dUMP and pyrophosphate. Domain
Chains Polymer Molecular Function Biological Process Cellular Component Deoxycytidine triphosphate deaminase
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage Chains Enzyme Name Description Catalytic Residues dCTP deaminase
M-CSA #732 Deoxycytidine triphosphate deaminase (dCTP deaminase) from E. coli catalyses the deamination of dCTP producing ammonia and dUTP. The dUTP can be hydrolysed by dUTPase producing dUMP which is a precursor of dTTP. dCTP deaminase is inhibited by dTTP and by inorganic phosphate. Deamination of dCTP by dCTP deaminase provides about 80% of the dUMP used for dTMP synthesis in E. coli . The substrate of dCTP deaminase is the dCTP.Mg2+ complex but the magnesium does not have a catalytic role and no other metal ions are involved in catalysis.
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