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Conserved domains on  [gi|1828881384|ref|WP_167729517|]
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orotidine-5'-phosphate decarboxylase [Thermococcus sp. 9N3]

Protein Classification

orotidine 5'-phosphate decarboxylase( domain architecture ID 10793876)

Orotidine 5'-phosphate decarboxylase (ODCase) decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 1-212 2.20e-121

orotidine 5'-phosphate decarboxylase; Provisional


:

Pssm-ID: 237520  Cd Length: 215  Bit Score: 342.73  E-value: 2.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   1 MAESRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEETglPVIADLKLADIPNTNRLIAGKVFE 80
Cdd:PRK13813    1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYA--PVIADLKVADIPNTNRLICEAVFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  81 AGADYIIAHGFVGSDSVEAVMEL-----GKTIIVVEMSHPGAREFIQPVTDRLIELANRLEPFGVIAPATRPERVNYIRS 155
Cdd:PRK13813   79 AGAWGIIVHGFTGRDSLKAVVEAaaesgGKVFVVVEMSHPGALEFIQPHADKLAKLAQEAGAFGVVAPATRPERVRYIRS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1828881384 156 RLKLGIKILTPGVGAQGGKAGEVLKAGADYIIVGRSIYASYNPRESARQIYEEVKAW 212
Cdd:PRK13813  159 RLGDELKIISPGIGAQGGKAADAIKAGADYVIVGRSIYNAADPREAAKAINEEIRGA 215
 
Name Accession Description Interval E-value
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 1-212 2.20e-121

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 342.73  E-value: 2.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   1 MAESRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEETglPVIADLKLADIPNTNRLIAGKVFE 80
Cdd:PRK13813    1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYA--PVIADLKVADIPNTNRLICEAVFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  81 AGADYIIAHGFVGSDSVEAVMEL-----GKTIIVVEMSHPGAREFIQPVTDRLIELANRLEPFGVIAPATRPERVNYIRS 155
Cdd:PRK13813   79 AGAWGIIVHGFTGRDSLKAVVEAaaesgGKVFVVVEMSHPGALEFIQPHADKLAKLAQEAGAFGVVAPATRPERVRYIRS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1828881384 156 RLKLGIKILTPGVGAQGGKAGEVLKAGADYIIVGRSIYASYNPRESARQIYEEVKAW 212
Cdd:PRK13813  159 RLGDELKIISPGIGAQGGKAADAIKAGADYVIVGRSIYNAADPREAAKAINEEIRGA 215
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 6-205 2.97e-65

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: 200.48  E-value: 2.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   6 LILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEEtGLPVIADLKLADIPNTNRLIAGKVFEAGADY 85
Cdd:cd04725     1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELREL-GFLVFLDLKLGDIPNTVAAAAEALLGLGADA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  86 IIAHGFVGSDSVEAVMELGKT-----IIVVEMSHPGAREF-------IQPVTDRLIELANRLEPFGVIAPATRPERvnyI 153
Cdd:cd04725    80 VTVHPYGGSDMLKAALEAAEEkgkglFAVTVLSSPGALDLqegipgsLEDLVERLAKLAREAGVDGVVCGATEPEA---L 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384 154 RSRLKLGIKILTPGVGAQ--------GGKAGEVLKAGADYIIVGRSIYASYNPRESARQI 205
Cdd:cd04725   157 RRALGPDFLILTPGIGAQgsgddqkrGGTPEDAIRAGADYIVVGRPITQAADPVAAAEAI 216
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-205 2.99e-64

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: 197.78  E-value: 2.99e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384    5 RLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEETGLPVIADLKLADIPNTNRLIAGKVFEAGAD 84
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELFGFPVFLDLKLHDIPNTVARAARAAAELGAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   85 YIIAHGFVGSDSVEAVMELG-----KTIIVVEMSHPGAREF-------IQPVTDRLIELANRLEPFGVIAPATRPERvny 152
Cdd:smart00934  81 AVTVHAYAGSDMIEAALEAAkkygpGLLAVTVLTSPGAEDLqelgdesLEEQVLRLAKLAKEAGLDGVVCSATEPEL--- 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1828881384  153 IRSRLKLGIKILTPGVGAQGGKAGEV--LKAGADYIIVGRSIYASYNPRESARQI 205
Cdd:smart00934 158 IRRALGPDFLILTPGIGDQGRVATPAvaIGAGADIIVVGRPITQAADPVEAAEAI 212
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
 6-205 1.88e-58

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: 183.33  E-value: 1.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   6 LILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEeTGLPVIADLKLADIPNTNRLIAGKVFEAGADY 85
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAK-LNKLIFLDLKFADIPNTVKLQYESKIKLGADM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  86 IIAHGFVGSDSVEAVME------LGKTIIVVEMSHPGAREFIQPVTDRLIELANRLEPFGVIAPATRPERVNYIRsRLKL 159
Cdd:TIGR01740  80 VNVHGFAGSESVEAAKEaasefgRRGLLAVTELTSMGSEEYGEDTMEKVVEYAKEAKEFGLIGPVCSAEEAKEIR-KATG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1828881384 160 GIKILTPGVGAQGGKAG---------EVLKAGADYIIVGRSIYASYNPRESARQI 205
Cdd:TIGR01740 159 DFLILTPGIRLDSKDADdqkrvvtleEAKEAGADVIIVGRGIYAAEDPVEAAKRI 213
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-205 5.43e-53

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: 169.37  E-value: 5.43e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   4 SRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEEtGLPVIADLKLADIPNTNRLIAGKVFEAGA 83
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH-GFLIFLDLKFADIGNTVAKQAKYKAKLGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  84 DYIIAHGFVGSDSVEAVMELGKT-----IIVVEMSHPGAREFI--------QPVTDRLIELANrlEPFGVIAPATRPERv 150
Cdd:pfam00215  80 DIVTVHAYAGEGTLKAAKEAAEEygrglLLVAELSSKGSLDLQeegdlgytQEIVHRAADLAA--GVDGVVASATEALR- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828881384 151 nyirsRLKLGIKILTPGVGAQGGKAG---------EVLKAGADYIIVGRSIYASYNPRESARQI 205
Cdd:pfam00215 157 -----EILPDFLILTPGIGLQGGDAGgqqrvttpaVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
 2-211 2.35e-47

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: 155.26  E-value: 2.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   2 AESRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEEtGLPVIADLKLADIPNTNRLIAGKVFEA 81
Cdd:COG0284     1 KRSPLIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKER-GLPVFLDLKRHDIPNTVAAAARAAAEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  82 GADYIIAHGFVGSDSVEAVMEL----GKTIIVV-EMSHPGAREF--------IQPVTDRLIELANRLEPFGVIAPATRPE 148
Cdd:COG0284    80 GVDAVTVHAYGGRDMLEPALEAadesGKGVFAVtVLTSPGAADLqelgiegpLYEVVLRLAKLAKEAGLDGVVCSATEAA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828881384 149 RvnyIRSRLKLGIKILTPGVGAQGGKAGEV---------LKAGADYIIVGRSIYASYNPRESARQIYEEVKA 211
Cdd:COG0284   160 A---LRAALGPDFLLLTPGIRPQGGDAGDQkrvgtpaeaIAAGADYLVVGRPITYAGDPRAAAEAIREEIAA 228
 
Name Accession Description Interval E-value
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 1-212 2.20e-121

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 342.73  E-value: 2.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   1 MAESRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEETglPVIADLKLADIPNTNRLIAGKVFE 80
Cdd:PRK13813    1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYA--PVIADLKVADIPNTNRLICEAVFE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  81 AGADYIIAHGFVGSDSVEAVMEL-----GKTIIVVEMSHPGAREFIQPVTDRLIELANRLEPFGVIAPATRPERVNYIRS 155
Cdd:PRK13813   79 AGAWGIIVHGFTGRDSLKAVVEAaaesgGKVFVVVEMSHPGALEFIQPHADKLAKLAQEAGAFGVVAPATRPERVRYIRS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1828881384 156 RLKLGIKILTPGVGAQGGKAGEVLKAGADYIIVGRSIYASYNPRESARQIYEEVKAW 212
Cdd:PRK13813  159 RLGDELKIISPGIGAQGGKAADAIKAGADYVIVGRSIYNAADPREAAKAINEEIRGA 215
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 6-205 2.97e-65

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: 200.48  E-value: 2.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   6 LILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEEtGLPVIADLKLADIPNTNRLIAGKVFEAGADY 85
Cdd:cd04725     1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELREL-GFLVFLDLKLGDIPNTVAAAAEALLGLGADA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  86 IIAHGFVGSDSVEAVMELGKT-----IIVVEMSHPGAREF-------IQPVTDRLIELANRLEPFGVIAPATRPERvnyI 153
Cdd:cd04725    80 VTVHPYGGSDMLKAALEAAEEkgkglFAVTVLSSPGALDLqegipgsLEDLVERLAKLAREAGVDGVVCGATEPEA---L 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384 154 RSRLKLGIKILTPGVGAQ--------GGKAGEVLKAGADYIIVGRSIYASYNPRESARQI 205
Cdd:cd04725   157 RRALGPDFLILTPGIGAQgsgddqkrGGTPEDAIRAGADYIVVGRPITQAADPVAAAEAI 216
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-205 2.99e-64

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: 197.78  E-value: 2.99e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384    5 RLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEETGLPVIADLKLADIPNTNRLIAGKVFEAGAD 84
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELFGFPVFLDLKLHDIPNTVARAARAAAELGAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   85 YIIAHGFVGSDSVEAVMELG-----KTIIVVEMSHPGAREF-------IQPVTDRLIELANRLEPFGVIAPATRPERvny 152
Cdd:smart00934  81 AVTVHAYAGSDMIEAALEAAkkygpGLLAVTVLTSPGAEDLqelgdesLEEQVLRLAKLAKEAGLDGVVCSATEPEL--- 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1828881384  153 IRSRLKLGIKILTPGVGAQGGKAGEV--LKAGADYIIVGRSIYASYNPRESARQI 205
Cdd:smart00934 158 IRRALGPDFLILTPGIGDQGRVATPAvaIGAGADIIVVGRPITQAADPVEAAEAI 212
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
 6-205 1.88e-58

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: 183.33  E-value: 1.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   6 LILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEeTGLPVIADLKLADIPNTNRLIAGKVFEAGADY 85
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAK-LNKLIFLDLKFADIPNTVKLQYESKIKLGADM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  86 IIAHGFVGSDSVEAVME------LGKTIIVVEMSHPGAREFIQPVTDRLIELANRLEPFGVIAPATRPERVNYIRsRLKL 159
Cdd:TIGR01740  80 VNVHGFAGSESVEAAKEaasefgRRGLLAVTELTSMGSEEYGEDTMEKVVEYAKEAKEFGLIGPVCSAEEAKEIR-KATG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1828881384 160 GIKILTPGVGAQGGKAG---------EVLKAGADYIIVGRSIYASYNPRESARQI 205
Cdd:TIGR01740 159 DFLILTPGIRLDSKDADdqkrvvtleEAKEAGADVIIVGRGIYAAEDPVEAAKRI 213
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-205 5.43e-53

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: 169.37  E-value: 5.43e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   4 SRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEEtGLPVIADLKLADIPNTNRLIAGKVFEAGA 83
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH-GFLIFLDLKFADIGNTVAKQAKYKAKLGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  84 DYIIAHGFVGSDSVEAVMELGKT-----IIVVEMSHPGAREFI--------QPVTDRLIELANrlEPFGVIAPATRPERv 150
Cdd:pfam00215  80 DIVTVHAYAGEGTLKAAKEAAEEygrglLLVAELSSKGSLDLQeegdlgytQEIVHRAADLAA--GVDGVVASATEALR- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1828881384 151 nyirsRLKLGIKILTPGVGAQGGKAG---------EVLKAGADYIIVGRSIYASYNPRESARQI 205
Cdd:pfam00215 157 -----EILPDFLILTPGIGLQGGDAGgqqrvttpaVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
 2-211 2.35e-47

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: 155.26  E-value: 2.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   2 AESRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEEtGLPVIADLKLADIPNTNRLIAGKVFEA 81
Cdd:COG0284     1 KRSPLIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKER-GLPVFLDLKRHDIPNTVAAAARAAAEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  82 GADYIIAHGFVGSDSVEAVMEL----GKTIIVV-EMSHPGAREF--------IQPVTDRLIELANRLEPFGVIAPATRPE 148
Cdd:COG0284    80 GVDAVTVHAYGGRDMLEPALEAadesGKGVFAVtVLTSPGAADLqelgiegpLYEVVLRLAKLAKEAGLDGVVCSATEAA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828881384 149 RvnyIRSRLKLGIKILTPGVGAQGGKAGEV---------LKAGADYIIVGRSIYASYNPRESARQIYEEVKA 211
Cdd:COG0284   160 A---LRAALGPDFLLLTPGIRPQGGDAGDQkrvgtpaeaIAAGADYLVVGRPITYAGDPRAAAEAIREEIAA 228
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-211 9.62e-23

3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];


Pssm-ID: 440039  Cd Length: 212  Bit Score: 90.99  E-value: 9.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   1 MAESRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEE-TGLPVIADLKLADipnTNRLIAGKVF 79
Cdd:COG0269     1 MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAfPDKIIVADLKTMD---AGALEAEMAF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  80 EAGADYI----IAHGFVGSDSVEAVMELGKTIIVvemshpgarEFIQpVTDRLiELANRLEPFGV------------IAP 143
Cdd:COG0269    78 KAGADIVtvlgAADDATIKGAVKAAKKYGKEVQV---------DLIG-VWDPV-ERAKELEELGVdivilhrgidaqAAG 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828881384 144 ATRPERVNYIRSRLKLGIKIlTPGVGAQggKAGEVLKAGADYIIVGRSIYASYNPRESARQIYEEVKA 211
Cdd:COG0269   147 GSPLDDLKKIKELVGVPVAV-AGGINPE--TLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDK 211
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
2-208 1.01e-20

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 86.34  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   2 AESRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEEtGLPVIADLKLADIPNTnrlIAGKVFEA 81
Cdd:PRK00230    1 MDDRLIVALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQR-GFKVFLDLKLHDIPNT---VAKAVRAL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  82 ---GADYIIAHGFVGSDSVEAVME-LGK----TIIVV----EMSHPGAREFI--QPVTDRLIELANR-----LEpfGVIA 142
Cdd:PRK00230   77 aklGVDMVNVHASGGPRMMKAAREaLEPksrpLLIAVtvltSMDEEDLAELGinLSLEEQVLRLAKLaqeagLD--GVVC 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828881384 143 patRPERVNYIRSRLKLGIKILTPGVGAQGGKAG---------EVLKAGADYIIVGRSIYASYNPRESARQIYEE 208
Cdd:PRK00230  155 ---SAQEAAAIREATGPDFLLVTPGIRPAGSDAGdqkrvmtpaQAIAAGSDYIVVGRPITQAADPAAAYEAILAE 226
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 8-205 6.85e-16

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 72.61  E-value: 6.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   8 LALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEE-TGLPVIADLKLADipnTNRLIAGKVFEAGADYI 86
Cdd:cd04726     5 VALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAfPDKIIVADLKTAD---AGALEAEMAFKAGADIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  87 IAHGFVGSDSVEAVMELGK---TIIVVEMShpGAREFIQpvtdrlielANRLEPFG---VIAPATRPERVNYIRSRLKLG 160
Cdd:cd04726    82 TVLGAAPLSTIKKAVKAAKkygKEVQVDLI--GVEDPEK---------RAKLLKLGvdiVILHRGIDAQAAGGWWPEDDL 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1828881384 161 IKILTPG---VGAQGG----KAGEVLKAGADYIIVGRSIYASYNPRESARQI 205
Cdd:cd04726   151 KKVKKLLgvkVAVAGGitpdTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
pyrF_sub2 TIGR02127
orotidine 5'-phosphate decarboxylase, subfamily 2; This model represents orotidine 5 ...
 15-206 4.37e-14

orotidine 5'-phosphate decarboxylase, subfamily 2; This model represents orotidine 5'-monophosphate decarboxylase, the PyrF protein of pyrimidine nucleotide biosynthesis. See TIGR01740 for a related but distinct subfamily of the same enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273987  Cd Length: 261  Bit Score: 68.97  E-value: 4.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  15 RERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKE------ETGLPVIADLKLADIPNTNRLIAGKVF-EAGADYII 87
Cdd:TIGR02127  40 QAFCLRIIDATAEYAAVVKPQVAFFERFGSEGFKALEEviaharSLGLPVLADVKRGDIGSTASAYAKAWLgHLHADALT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  88 AHGFVGSDS----VEAVMELGKTIIV-VEMSHPGAREF-----------IQPVTDRLIELAN---RLEPFGVIAPATRPE 148
Cdd:TIGR02127 120 VSPYLGLDSlrpfLEYARANGAGIFVlVKTSNPGGADLqdlrvsdgrtvYEEVAELAGELNEspgDCSSVGAVVGATSPG 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828881384 149 RVNYIRSRLKLGIkILTPGVGAQGGKAGEVLKA----GADYII-VGRSIYASYNPRESARQIY 206
Cdd:TIGR02127 200 DLLRLRIEMPTAP-FLVPGFGAQGAEAADLRGLfgadGSGLLInSSRGVLFAGPRSSALVAAG 261
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 1-210 8.24e-14

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 69.28  E-value: 8.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   1 MAESRLILALDVYERERALEIARET----ADYlwaIKVNWPLIIGSGLDIIPELKEE-TGLPVIADLKLADIPNTNRLIA 75
Cdd:PRK07028    1 MERPILQVALDLLELDRAVEIAKEAvaggADW---IEAGTPLIKSEGMNAIRTLRKNfPDHTIVADMKTMDTGAIEVEMA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  76 GKvfeAGADYII----AHGFVGSDSVEAVMELGKTIIVVEMSHPgarefiQPVtdrliELANRLEPFGviapatrperVN 151
Cdd:PRK07028   78 AK---AGADIVCilglADDSTIEDAVRAARKYGVRLMADLINVP------DPV-----KRAVELEELG----------VD 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828881384 152 YIR---------------SRLKLGIKILTPGVGAQGG----KAGEVLKAGADYIIVGRSIYASYNPRESARQIYEEVK 210
Cdd:PRK07028  134 YINvhvgidqqmlgkdplELLKEVSEEVSIPIAVAGGldaeTAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAID 211
pyrF PRK00125
orotidine 5'-phosphate decarboxylase; Reviewed
 53-211 3.61e-13

orotidine 5'-phosphate decarboxylase; Reviewed


Pssm-ID: 234651  Cd Length: 278  Bit Score: 66.42  E-value: 3.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  53 ETGLPVIADLKLADIPNTNRLIAGKVFEA--GADYIIAHGFVGSDSVEAVMEL----GKTIIV-VEMSHPGAR--EFI-- 121
Cdd:PRK00125   84 EAGVLVIADAKRGDIGSTAEAYAKAAFESplEADAVTVSPYMGFDSLEPYLEYaeehGKGVFVlCRTSNPGGSdlQFLrt 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384 122 ---QPVTDRLIELANRLE--------PFGVIAPATRPERVNYIRSRLKlGIKILTPGVGAQGGKAGEVLKAGADY----- 185
Cdd:PRK00125  164 adgRPLYQHVADLAAALNnlgncgygSIGLVVGATFPPELAAVRKILG-GMPLLIPGIGAQGGDAEATVRAGGAAgnggi 242

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1828881384 186 IIVGRSI-YASYNP------RESARQIYEEVKA 211
Cdd:PRK00125  243 PNSSRAIlYAGPGKdfaeaaRRAAERTRDAINA 275
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
6-210 9.44e-10

bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 57.33  E-value: 9.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   6 LILALDVYERERALEIARE--TADYLwAIKVNWPLIIGSGLDIIPELKEE-TGLPVIADLKLADipnTNRLIAGKVFEAG 82
Cdd:PRK13307  175 LQVALDLPDLEEVERVLSQlpKSDHI-IIEAGTPLIKKFGLEVISKIREVrPDAFIVADLKTLD---TGNLEARMAADAT 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  83 ADYIIAHGFVGSDSVE-AVMELGKTIIVVEMSHPGAREFIQpVTDRLIELANRLEPFGVIAPATRPERVNYIRSRLKLGI 161
Cdd:PRK13307  251 ADAVVISGLAPISTIEkAIHEAQKTGIYSILDMLNVEDPVK-LLESLKVKPDVVELHRGIDEEGTEHAWGNIKEIKKAGG 329

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1828881384 162 KILtpgVGAQGG----KAGEVLKAGADYIIVGRSIYASYNPRESARQIYEEVK 210
Cdd:PRK13307  330 KIL---VAVAGGvrveNVEEALKAGADILVVGRAITKSKDVRRAAEDFLNKLK 379
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 46-190 3.69e-05

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 42.96  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384  46 IIPELKEETGLPVIADLKLADIPNTNRLIAGKVFEAGADYIIAHGFVGSDS------VEAVMELGKTIIVVEMSHP-GAR 118
Cdd:cd04722    48 VLKEVAAETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYLAredlelIRELREAVPDVKVVVKLSPtGEL 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828881384 119 EFIQPVTDRLIE-LANRLEPFGVIAPATRPERVNYIRSRLKLGIKILTPGVGAQGGKAGEVLKAGADYIIVGR 190
Cdd:cd04722   128 AAAAAEEAGVDEvGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
1-86 2.91e-04

3-dehydro-L-gulonate-6-phosphate decarboxylase;


Pssm-ID: 237344  Cd Length: 216  Bit Score: 40.30  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881384   1 MAESRLILALDVYERERALEIARETADYLWAIKVNWPLIIGSGLDIIPELKEEtgLP---VIADLKLADipntnrliAGK 77
Cdd:PRK13306    1 MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRAL--YPdkiIVADTKIAD--------AGK 70

                          90
                  ....*....|....
gi 1828881384  78 V-----FEAGADYI 86
Cdd:PRK13306   71 IlakmaFEAGADWV 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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