NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488399994|ref|WP_002469379|]
View 

MULTISPECIES: orotidine-5'-phosphate decarboxylase [Staphylococcus]

Protein Classification

orotidine 5'-phosphate decarboxylase( domain architecture ID 10791852)

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

EC:  4.1.1.23
Gene Ontology:  GO:0004590

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
1-230 2.85e-134

orotidine-5'-phosphate decarboxylase;


:

Pssm-ID: 234695  Cd Length: 230  Bit Score: 376.78  E-value: 2.85e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   1 MRNLPIIALDFKSADEVHTFLNKFNEPLC-VKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLD 79
Cdd:PRK00230   1 MDDRLIVALDFPSKEEALAFLDQLDPAVLfVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVAKAVRALAKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  80 VDLVNVHAAGGIKMMEEAKKGLRKHNaDIKIIAVTQLTSTTERQLHEeQNIQTSIEEAVLNYARLTKKAGLDGVVCSPLE 159
Cdd:PRK00230  81 VDMVNVHASGGPRMMKAAREALEPKS-RPLLIAVTVLTSMDEEDLAE-LGINLSLEEQVLRLAKLAQEAGLDGVVCSAQE 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488399994 160 AEMISKELGTDFLKVTPGIRPKGAARNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKIKESWLS 230
Cdd:PRK00230 159 AAAIREATGPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEIAG 229
 
Name Accession Description Interval E-value
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
1-230 2.85e-134

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 376.78  E-value: 2.85e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   1 MRNLPIIALDFKSADEVHTFLNKFNEPLC-VKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLD 79
Cdd:PRK00230   1 MDDRLIVALDFPSKEEALAFLDQLDPAVLfVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVAKAVRALAKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  80 VDLVNVHAAGGIKMMEEAKKGLRKHNaDIKIIAVTQLTSTTERQLHEeQNIQTSIEEAVLNYARLTKKAGLDGVVCSPLE 159
Cdd:PRK00230  81 VDMVNVHASGGPRMMKAAREALEPKS-RPLLIAVTVLTSMDEEDLAE-LGINLSLEEQVLRLAKLAQEAGLDGVVCSAQE 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488399994 160 AEMISKELGTDFLKVTPGIRPKGAARNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKIKESWLS 230
Cdd:PRK00230 159 AAAIREATGPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEIAG 229
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
1-228 5.43e-104

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: 299.71  E-value: 5.43e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   1 MRNLPIIALDFKSADEVHTFLNKF-NEPLCVKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLD 79
Cdd:COG0284    1 KRSPLIVALDLPDAAEALAIVDALaDLVCAYKPGLALFEAYGPEGVEALKERGLPVFLDLKRHDIPNTVAAAARAAAELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  80 VDLVNVHAAGGIKMMEEAKKGLRKHnaDIKIIAVTQLTSTTERQLhEEQNIQTSIEEAVLNYARLTKKAGLDGVVCSPLE 159
Cdd:COG0284   81 VDAVTVHAYGGRDMLEPALEAADES--GKGVFAVTVLTSPGAADL-QELGIEGPLYEVVLRLAKLAKEAGLDGVVCSATE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488399994 160 AEMISKELGTDFLKVTPGIRPKGAARNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKIKESW 228
Cdd:COG0284  158 AAALRAALGPDFLLLTPGIRPQGGDAGDQKRVGTPAEAIAAGADYLVVGRPITYAGDPRAAAEAIREEI 226
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
6-224 4.86e-82

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: 244.01  E-value: 4.86e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   6 IIALDFKSADEVHTFLNKFNEPLC-VKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLDVDLVN 84
Cdd:cd04725    2 IVALDPPDEEFALALIDALGPYVCaVKVGLELFEAAGPEIVKELRELGFLVFLDLKLGDIPNTVAAAAEALLGLGADAVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  85 VHAAGGIKMMEEAKKGLRKHNAdiKIIAVTQLTSTTERQLHeeQNIQTSIEEAVLNYARLTKKAGLDGVVCSPLEAEMIS 164
Cdd:cd04725   82 VHPYGGSDMLKAALEAAEEKGK--GLFAVTVLSSPGALDLQ--EGIPGSLEDLVERLAKLAREAGVDGVVCGATEPEALR 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994 165 KELGTDFLKVTPGIRPKGAArNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKI 224
Cdd:cd04725  158 RALGPDFLILTPGIGAQGSG-DDQKRGGTPEDAIRAGADYIVVGRPITQAADPVAAAEAI 216
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
6-224 6.95e-81

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: 240.92  E-value: 6.95e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994     6 IIALDFKSADEVHTFLNKF-NEPLCVKIGMELFYQTGPALIKSIKKR-GHDIFLDLKLHDIPNTVSKAMEGLARLDVDLV 83
Cdd:smart00934   3 IVALDVPDLEEALELADALgDSVDIIKVGTELFLAEGPEGVKELKELfGFPVFLDLKLHDIPNTVARAARAAAELGADAV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994    84 NVHAAGGIKMMEEAKKGLRKHNAdiKIIAVTQLTSTTERQLHEEQNIqtSIEEAVLNYARLTKKAGLDGVVCSPLEAEMI 163
Cdd:smart00934  83 TVHAYAGSDMIEAALEAAKKYGP--GLLAVTVLTSPGAEDLQELGDE--SLEEQVLRLAKLAKEAGLDGVVCSATEPELI 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488399994   164 SKELGTDFLKVTPGIRpkgaarnDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKI 224
Cdd:smart00934 159 RRALGPDFLILTPGIG-------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
6-224 1.02e-67

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: 207.50  E-value: 1.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994    6 IIALDFKSADEVHTFLNKF-NEPLCVKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLDVDLVN 84
Cdd:pfam00215   4 CVALDVPTLEEALELADELgPYVDILKVGTPLFEAFGLKLVAELRKHGFLIFLDLKFADIGNTVAKQAKYKAKLGADIVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   85 VHAAGGIKMMEEAKKGLRKHNAdiKIIAVTQLTSTTERQLHEEQnIQTSIEEAVLNYARLtkKAGLDGVVCSPLEAEmis 164
Cdd:pfam00215  84 VHAYAGEGTLKAAKEAAEEYGR--GLLLVAELSSKGSLDLQEEG-DLGYTQEIVHRAADL--AAGVDGVVASATEAL--- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  165 KELGTDFLKVTPGIRPKGAARNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKI 224
Cdd:pfam00215 156 REILPDFLILTPGIGLQGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
5-225 1.01e-65

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: 202.20  E-value: 1.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994    5 PIIALDFKSADEVHTFLNKFNEPLC-VKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLDVDLV 83
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICvIKVGYDLLLSGGEKIIDELAKLNKLIFLDLKFADIPNTVKLQYESKIKLGADMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   84 NVHAAGGIKMMEEAKKGLRKHNaDIKIIAVTQLTSTterqlhEEQNIQTSIEEAVLNYARLTKKAGLDGVVCSPLEAEMI 163
Cdd:TIGR01740  81 NVHGFAGSESVEAAKEAASEFG-RRGLLAVTELTSM------GSEEYGEDTMEKVVEYAKEAKEFGLIGPVCSAEEAKEI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488399994  164 SKELGtDFLKVTPGIRPKGAARNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKIK 225
Cdd:TIGR01740 154 RKATG-DFLILTPGIRLDSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
 
Name Accession Description Interval E-value
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
1-230 2.85e-134

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 376.78  E-value: 2.85e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   1 MRNLPIIALDFKSADEVHTFLNKFNEPLC-VKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLD 79
Cdd:PRK00230   1 MDDRLIVALDFPSKEEALAFLDQLDPAVLfVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVAKAVRALAKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  80 VDLVNVHAAGGIKMMEEAKKGLRKHNaDIKIIAVTQLTSTTERQLHEeQNIQTSIEEAVLNYARLTKKAGLDGVVCSPLE 159
Cdd:PRK00230  81 VDMVNVHASGGPRMMKAAREALEPKS-RPLLIAVTVLTSMDEEDLAE-LGINLSLEEQVLRLAKLAQEAGLDGVVCSAQE 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488399994 160 AEMISKELGTDFLKVTPGIRPKGAARNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKIKESWLS 230
Cdd:PRK00230 159 AAAIREATGPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEIAG 229
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
1-228 5.43e-104

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: 299.71  E-value: 5.43e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   1 MRNLPIIALDFKSADEVHTFLNKF-NEPLCVKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLD 79
Cdd:COG0284    1 KRSPLIVALDLPDAAEALAIVDALaDLVCAYKPGLALFEAYGPEGVEALKERGLPVFLDLKRHDIPNTVAAAARAAAELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  80 VDLVNVHAAGGIKMMEEAKKGLRKHnaDIKIIAVTQLTSTTERQLhEEQNIQTSIEEAVLNYARLTKKAGLDGVVCSPLE 159
Cdd:COG0284   81 VDAVTVHAYGGRDMLEPALEAADES--GKGVFAVTVLTSPGAADL-QELGIEGPLYEVVLRLAKLAKEAGLDGVVCSATE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488399994 160 AEMISKELGTDFLKVTPGIRPKGAARNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKIKESW 228
Cdd:COG0284  158 AAALRAALGPDFLLLTPGIRPQGGDAGDQKRVGTPAEAIAAGADYLVVGRPITYAGDPRAAAEAIREEI 226
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
6-224 4.86e-82

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: 244.01  E-value: 4.86e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   6 IIALDFKSADEVHTFLNKFNEPLC-VKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLDVDLVN 84
Cdd:cd04725    2 IVALDPPDEEFALALIDALGPYVCaVKVGLELFEAAGPEIVKELRELGFLVFLDLKLGDIPNTVAAAAEALLGLGADAVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  85 VHAAGGIKMMEEAKKGLRKHNAdiKIIAVTQLTSTTERQLHeeQNIQTSIEEAVLNYARLTKKAGLDGVVCSPLEAEMIS 164
Cdd:cd04725   82 VHPYGGSDMLKAALEAAEEKGK--GLFAVTVLSSPGALDLQ--EGIPGSLEDLVERLAKLAREAGVDGVVCGATEPEALR 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994 165 KELGTDFLKVTPGIRPKGAArNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKI 224
Cdd:cd04725  158 RALGPDFLILTPGIGAQGSG-DDQKRGGTPEDAIRAGADYIVVGRPITQAADPVAAAEAI 216
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
6-224 6.95e-81

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: 240.92  E-value: 6.95e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994     6 IIALDFKSADEVHTFLNKF-NEPLCVKIGMELFYQTGPALIKSIKKR-GHDIFLDLKLHDIPNTVSKAMEGLARLDVDLV 83
Cdd:smart00934   3 IVALDVPDLEEALELADALgDSVDIIKVGTELFLAEGPEGVKELKELfGFPVFLDLKLHDIPNTVARAARAAAELGADAV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994    84 NVHAAGGIKMMEEAKKGLRKHNAdiKIIAVTQLTSTTERQLHEEQNIqtSIEEAVLNYARLTKKAGLDGVVCSPLEAEMI 163
Cdd:smart00934  83 TVHAYAGSDMIEAALEAAKKYGP--GLLAVTVLTSPGAEDLQELGDE--SLEEQVLRLAKLAKEAGLDGVVCSATEPELI 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488399994   164 SKELGTDFLKVTPGIRpkgaarnDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKI 224
Cdd:smart00934 159 RRALGPDFLILTPGIG-------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
6-224 1.02e-67

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: 207.50  E-value: 1.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994    6 IIALDFKSADEVHTFLNKF-NEPLCVKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLDVDLVN 84
Cdd:pfam00215   4 CVALDVPTLEEALELADELgPYVDILKVGTPLFEAFGLKLVAELRKHGFLIFLDLKFADIGNTVAKQAKYKAKLGADIVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   85 VHAAGGIKMMEEAKKGLRKHNAdiKIIAVTQLTSTTERQLHEEQnIQTSIEEAVLNYARLtkKAGLDGVVCSPLEAEmis 164
Cdd:pfam00215  84 VHAYAGEGTLKAAKEAAEEYGR--GLLLVAELSSKGSLDLQEEG-DLGYTQEIVHRAADL--AAGVDGVVASATEAL--- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  165 KELGTDFLKVTPGIRPKGAARNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKI 224
Cdd:pfam00215 156 REILPDFLILTPGIGLQGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
5-225 1.01e-65

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: 202.20  E-value: 1.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994    5 PIIALDFKSADEVHTFLNKFNEPLC-VKIGMELFYQTGPALIKSIKKRGHDIFLDLKLHDIPNTVSKAMEGLARLDVDLV 83
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICvIKVGYDLLLSGGEKIIDELAKLNKLIFLDLKFADIPNTVKLQYESKIKLGADMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   84 NVHAAGGIKMMEEAKKGLRKHNaDIKIIAVTQLTSTterqlhEEQNIQTSIEEAVLNYARLTKKAGLDGVVCSPLEAEMI 163
Cdd:TIGR01740  81 NVHGFAGSESVEAAKEAASEFG-RRGLLAVTELTSM------GSEEYGEDTMEKVVEYAKEAKEFGLIGPVCSAEEAKEI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488399994  164 SKELGtDFLKVTPGIRPKGAARNDQQRITTPEEAKTLGSTHIVVGRPITQSEHPIDSYHKIK 225
Cdd:TIGR01740 154 RKATG-DFLILTPGIRLDSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
6-227 1.42e-42

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 143.20  E-value: 1.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994   6 IIALDFKSADEVHTFLNKFNEPLC-VKIGMELFYQTGPALIKSIKKRGhDIFLDLKLHDIPNTVSKAMEGLARLDVDLVN 84
Cdd:PRK13813   7 ILALDVTDRERALKIAEELDDYVDaIKVGWPLVLASGLGIIEELKRYA-PVIADLKVADIPNTNRLICEAVFEAGAWGII 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488399994  85 VHAAGGIKMMEEAKKGLRKHNADIKIIAVTQltstterqlHEeqNIQTSIEEAVLNYARLTKKAGLDGVVCSPLEAE--- 161
Cdd:PRK13813  86 VHGFTGRDSLKAVVEAAAESGGKVFVVVEMS---------HP--GALEFIQPHADKLAKLAQEAGAFGVVAPATRPErvr 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488399994 162 MISKELGTDFLKVTPGIRPKGAArndqqrittPEEAKTLGSTHIVVGRPITQSEHPIDSYHKIKES 227
Cdd:PRK13813 155 YIRSRLGDELKIISPGIGAQGGK---------AADAIKAGADYVIVGRSIYNAADPREAAKAINEE 211
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH