uridine 5'-monophosphate synthase catalyzes the last two steps of the UMP biosynthesis, the addition of ribose-P to orotate by orotate phosphoribosyltransferase, to form orotidine-5'-monophosphate (OMP), and the decarboxylation of OMP by orotidine-5'-phosphate decarboxylase to form uridine monophosphate (UMP); in bacteria, these two domains/functions are located in separate proteins
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
2-205
1.07e-68
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
The actual alignment was detected with superfamily member PRK13809:
Pssm-ID: 444823 Cd Length: 206 Bit Score: 218.55 E-value: 1.07e-68
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
249-463
9.24e-68
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: 216.36 E-value: 9.24e-68
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
249-463
9.24e-68
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: 216.36 E-value: 9.24e-68
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
10-203
2.19e-67
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 215.02 E-value: 2.19e-67
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
251-463
3.83e-53
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: 178.52 E-value: 3.83e-53
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
251-464
2.75e-52
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: 176.01 E-value: 2.75e-52
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: 144.62 E-value: 2.21e-40
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
16-177
5.41e-35
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 129436 [Multi-domain] Cd Length: 173 Bit Score: 128.70 E-value: 5.41e-35
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
54-176
2.67e-18
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 80.90 E-value: 2.67e-18
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
251-466
4.36e-17
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: 80.15 E-value: 4.36e-17
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
44-167
4.09e-09
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 55.45 E-value: 4.09e-09
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
249-463
9.24e-68
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: 216.36 E-value: 9.24e-68
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
10-203
2.19e-67
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 215.02 E-value: 2.19e-67
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
251-463
3.83e-53
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: 178.52 E-value: 3.83e-53
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
251-464
2.75e-52
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: 176.01 E-value: 2.75e-52
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: 144.62 E-value: 2.21e-40
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
16-177
5.41e-35
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 129436 [Multi-domain] Cd Length: 173 Bit Score: 128.70 E-value: 5.41e-35
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
54-176
2.67e-18
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 80.90 E-value: 2.67e-18
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
251-466
4.36e-17
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: 80.15 E-value: 4.36e-17
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
44-167
4.09e-09
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 55.45 E-value: 4.09e-09
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
29-177
2.47e-07
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 440269 Cd Length: 171 Bit Score: 50.46 E-value: 2.47e-07
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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