orotidine 5'-phosphate decarboxylase (ODCase) decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
31-254
1.13e-43
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to pfam00834.
:
Pssm-ID: 395160 Cd Length: 215 Bit Score: 147.41 E-value: 1.13e-43
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
31-254
1.13e-43
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to pfam00834.
Pssm-ID: 395160 Cd Length: 215 Bit Score: 147.41 E-value: 1.13e-43
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
33-254
1.54e-42
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway. In mammals, UMP synthase contains two domains: the orotate phosphoribosyltransferase (OPRTase) domain that catalyzes the transfer of phosphoribosyl 5'-pyrophosphate (PRPP) to orotate to form OMP, and the orotidine-5'-phosphate decarboxylase (ODCase) domain that decarboxylates OMP to form UMP.
Pssm-ID: 240076 Cd Length: 216 Bit Score: 144.63 E-value: 1.54e-42
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
33-254
6.85e-37
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5'-monophosphate decarboxylase, the PyrF protein of pyrimidine nucleotide biosynthesis. In many eukaryotes, the region hit by this model is part of a multifunctional protein. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273785 Cd Length: 214 Bit Score: 129.78 E-value: 6.85e-37
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.
Pssm-ID: 214921 Cd Length: 212 Bit Score: 103.02 E-value: 1.30e-26
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
29-256
1.38e-24
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5'-phosphate decarboxylase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440053 Cd Length: 228 Bit Score: 97.86 E-value: 1.38e-24
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
31-254
1.13e-43
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to pfam00834.
Pssm-ID: 395160 Cd Length: 215 Bit Score: 147.41 E-value: 1.13e-43
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
33-254
1.54e-42
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway. In mammals, UMP synthase contains two domains: the orotate phosphoribosyltransferase (OPRTase) domain that catalyzes the transfer of phosphoribosyl 5'-pyrophosphate (PRPP) to orotate to form OMP, and the orotidine-5'-phosphate decarboxylase (ODCase) domain that decarboxylates OMP to form UMP.
Pssm-ID: 240076 Cd Length: 216 Bit Score: 144.63 E-value: 1.54e-42
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
33-254
6.85e-37
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5'-monophosphate decarboxylase, the PyrF protein of pyrimidine nucleotide biosynthesis. In many eukaryotes, the region hit by this model is part of a multifunctional protein. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273785 Cd Length: 214 Bit Score: 129.78 E-value: 6.85e-37
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.
Pssm-ID: 214921 Cd Length: 212 Bit Score: 103.02 E-value: 1.30e-26
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
29-256
1.38e-24
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5'-phosphate decarboxylase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440053 Cd Length: 228 Bit Score: 97.86 E-value: 1.38e-24
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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