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Conserved domains on  [gi|1084785129|gb|OGQ23678|]
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orotidine 5'-phosphate decarboxylase [Deltaproteobacteria bacterium RIFCSPHIGHO2_02_FULL_44_16]

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

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List of domain hits

Name Accession Description Interval E-value
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
9-237 8.69e-91

orotidine-5'-phosphate decarboxylase;


:

Pssm-ID: 234695  Cd Length: 230  Bit Score: 267.00  E-value: 8.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129   9 RDRLIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGV 88
Cdd:PRK00230    2 DDRLIVALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVAKAVRALAKLGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  89 AMLTVHATGGTEMLRRAAHAAedaagSKTEMPLLLAVTVLTSM--ETLADVGVQFEVREQVVRLAQLAKKCGFQGVVASP 166
Cdd:PRK00230   82 DMVNVHASGGPRMMKAAREAL-----EPKSRPLLIAVTVLTSMdeEDLAELGINLSLEEQVLRLAKLAQEAGLDGVVCSA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084785129 167 LEIKPVRKACGERFLIVTTGVRPLGSAPLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQILKEI 237
Cdd:PRK00230  157 QEAAAIREATGPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEI 227
 
Name Accession Description Interval E-value
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
9-237 8.69e-91

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 267.00  E-value: 8.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129   9 RDRLIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGV 88
Cdd:PRK00230    2 DDRLIVALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVAKAVRALAKLGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  89 AMLTVHATGGTEMLRRAAHAAedaagSKTEMPLLLAVTVLTSM--ETLADVGVQFEVREQVVRLAQLAKKCGFQGVVASP 166
Cdd:PRK00230   82 DMVNVHASGGPRMMKAAREAL-----EPKSRPLLIAVTVLTSMdeEDLAELGINLSLEEQVLRLAKLAQEAGLDGVVCSA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084785129 167 LEIKPVRKACGERFLIVTTGVRPLGSAPLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQILKEI 237
Cdd:PRK00230  157 QEAAAIREATGPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEI 227
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
9-237 1.15e-79

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: 238.46  E-value: 1.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129   9 RDRLIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGV 88
Cdd:COG0284     2 RSPLIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKERGLPVFLDLKRHDIPNTVAAAARAAAELGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  89 AMLTVHATGGTEMLRRAAHaaedaaGSKTEMPLLLAVTVLTSM--ETLADVGVQFEVREQVVRLAQLAKKCGFQGVVASP 166
Cdd:COG0284    82 DAVTVHAYGGRDMLEPALE------AADESGKGVFAVTVLTSPgaADLQELGIEGPLYEVVLRLAKLAKEAGLDGVVCSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084785129 167 LEIKPVRKACGERFLIVTTGVRPLGSAPLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQILKEI 237
Cdd:COG0284   156 TEAAALRAALGPDFLLLTPGIRPQGGDAGDQKRVGTPAEAIAAGADYLVVGRPITYAGDPRAAAEAIREEI 226
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
12-233 5.75e-61

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: 190.46  E-value: 5.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  12 LIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGVAML 91
Cdd:cd04725     1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELGFLVFLDLKLGDIPNTVAAAAEALLGLGADAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  92 TVHATGGTEMLRRaahaaeDAAGSKTEMPLLLAVTVLTSMETLADV-GVQFEVREQVVRLAQLAKKCGFQGVVASPLEIK 170
Cdd:cd04725    81 TVHPYGGSDMLKA------ALEAAEEKGKGLFAVTVLSSPGALDLQeGIPGSLEDLVERLAKLAREAGVDGVVCGATEPE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084785129 171 PVRKACGERFLIVTTGVRPLGSApLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQI 233
Cdd:cd04725   155 ALRRALGPDFLILTPGIGAQGSG-DDQKRGGTPEDAIRAGADYIVVGRPITQAADPVAAAEAI 216
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
11-233 5.13e-59

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: 185.45  E-value: 5.13e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129   11 RLIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHD-HQCKVFLDLKYHDIPSTVELAVRHATKLGVA 89
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKElFGFPVFLDLKLHDIPNTVARAARAAAELGAD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129   90 MLTVHATGGTEMLRraahaaEDAAGSKTEMPLLLAVTVLTSM--ETLADVGVQfEVREQVVRLAQLAKKCGFQGVVASPL 167
Cdd:smart00934  81 AVTVHAYAGSDMIE------AALEAAKKYGPGLLAVTVLTSPgaEDLQELGDE-SLEEQVLRLAKLAKEAGLDGVVCSAT 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084785129  168 EIKPVRKACGERFLIVTTGVRplgsaplDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQI 233
Cdd:smart00934 154 EPELIRRALGPDFLILTPGIG-------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
10-233 1.88e-46

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: 153.57  E-value: 1.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  10 DRLIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGVA 89
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKHGFLIFLDLKFADIGNTVAKQAKYKAKLGAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  90 MLTVHATGGTEMLRraahaaEDAAGSKTEMPLLLAVTVLTSM--ETLADVGVQFEVREQVVRLAQLAkkCGFQGVVASPL 167
Cdd:pfam00215  81 IVTVHAYAGEGTLK------AAKEAAEEYGRGLLLVAELSSKgsLDLQEEGDLGYTQEIVHRAADLA--AGVDGVVASAT 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084785129 168 EIkpvRKACGERFLIVTTGVRPLGSAPLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQI 233
Cdd:pfam00215 153 EA---LREILPDFLILTPGIGLQGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
12-234 2.08e-45

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: 150.97  E-value: 2.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  12 LIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGVAML 91
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNKLIFLDLKFADIPNTVKLQYESKIKLGADMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  92 TVHATGGTEMLRRAAHAAedaagSKTEMPLLLAVTVLTSMETladVGVQFEVREQVVRLAQLAKKCGFQGVVASPLEIKP 171
Cdd:TIGR01740  81 NVHGFAGSESVEAAKEAA-----SEFGRRGLLAVTELTSMGS---EEYGEDTMEKVVEYAKEAKEFGLIGPVCSAEEAKE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084785129 172 VRKACGeRFLIVTTGVRPLGSAPLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQIL 234
Cdd:TIGR01740 153 IRKATG-DFLILTPGIRLDSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
 
Name Accession Description Interval E-value
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
9-237 8.69e-91

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 267.00  E-value: 8.69e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129   9 RDRLIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGV 88
Cdd:PRK00230    2 DDRLIVALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVAKAVRALAKLGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  89 AMLTVHATGGTEMLRRAAHAAedaagSKTEMPLLLAVTVLTSM--ETLADVGVQFEVREQVVRLAQLAKKCGFQGVVASP 166
Cdd:PRK00230   82 DMVNVHASGGPRMMKAAREAL-----EPKSRPLLIAVTVLTSMdeEDLAELGINLSLEEQVLRLAKLAQEAGLDGVVCSA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084785129 167 LEIKPVRKACGERFLIVTTGVRPLGSAPLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQILKEI 237
Cdd:PRK00230  157 QEAAAIREATGPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEI 227
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
9-237 1.15e-79

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: 238.46  E-value: 1.15e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129   9 RDRLIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGV 88
Cdd:COG0284     2 RSPLIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKERGLPVFLDLKRHDIPNTVAAAARAAAELGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  89 AMLTVHATGGTEMLRRAAHaaedaaGSKTEMPLLLAVTVLTSM--ETLADVGVQFEVREQVVRLAQLAKKCGFQGVVASP 166
Cdd:COG0284    82 DAVTVHAYGGRDMLEPALE------AADESGKGVFAVTVLTSPgaADLQELGIEGPLYEVVLRLAKLAKEAGLDGVVCSA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084785129 167 LEIKPVRKACGERFLIVTTGVRPLGSAPLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQILKEI 237
Cdd:COG0284   156 TEAAALRAALGPDFLLLTPGIRPQGGDAGDQKRVGTPAEAIAAGADYLVVGRPITYAGDPRAAAEAIREEI 226
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
12-233 5.75e-61

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: 190.46  E-value: 5.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  12 LIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGVAML 91
Cdd:cd04725     1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELGFLVFLDLKLGDIPNTVAAAAEALLGLGADAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  92 TVHATGGTEMLRRaahaaeDAAGSKTEMPLLLAVTVLTSMETLADV-GVQFEVREQVVRLAQLAKKCGFQGVVASPLEIK 170
Cdd:cd04725    81 TVHPYGGSDMLKA------ALEAAEEKGKGLFAVTVLSSPGALDLQeGIPGSLEDLVERLAKLAREAGVDGVVCGATEPE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084785129 171 PVRKACGERFLIVTTGVRPLGSApLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQI 233
Cdd:cd04725   155 ALRRALGPDFLILTPGIGAQGSG-DDQKRGGTPEDAIRAGADYIVVGRPITQAADPVAAAEAI 216
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
11-233 5.13e-59

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: 185.45  E-value: 5.13e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129   11 RLIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHD-HQCKVFLDLKYHDIPSTVELAVRHATKLGVA 89
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKElFGFPVFLDLKLHDIPNTVARAARAAAELGAD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129   90 MLTVHATGGTEMLRraahaaEDAAGSKTEMPLLLAVTVLTSM--ETLADVGVQfEVREQVVRLAQLAKKCGFQGVVASPL 167
Cdd:smart00934  81 AVTVHAYAGSDMIE------AALEAAKKYGPGLLAVTVLTSPgaEDLQELGDE-SLEEQVLRLAKLAKEAGLDGVVCSAT 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084785129  168 EIKPVRKACGERFLIVTTGVRplgsaplDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQI 233
Cdd:smart00934 154 EPELIRRALGPDFLILTPGIG-------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
10-233 1.88e-46

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: 153.57  E-value: 1.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  10 DRLIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGVA 89
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKHGFLIFLDLKFADIGNTVAKQAKYKAKLGAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  90 MLTVHATGGTEMLRraahaaEDAAGSKTEMPLLLAVTVLTSM--ETLADVGVQFEVREQVVRLAQLAkkCGFQGVVASPL 167
Cdd:pfam00215  81 IVTVHAYAGEGTLK------AAKEAAEEYGRGLLLVAELSSKgsLDLQEEGDLGYTQEIVHRAADLA--AGVDGVVASAT 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084785129 168 EIkpvRKACGERFLIVTTGVRPLGSAPLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQI 233
Cdd:pfam00215 153 EA---LREILPDFLILTPGIGLQGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
12-234 2.08e-45

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: 150.97  E-value: 2.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  12 LIVALLADRMRDAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQCKVFLDLKYHDIPSTVELAVRHATKLGVAML 91
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNKLIFLDLKFADIPNTVKLQYESKIKLGADMV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  92 TVHATGGTEMLRRAAHAAedaagSKTEMPLLLAVTVLTSMETladVGVQFEVREQVVRLAQLAKKCGFQGVVASPLEIKP 171
Cdd:TIGR01740  81 NVHGFAGSESVEAAKEAA-----SEFGRRGLLAVTELTSMGS---EEYGEDTMEKVVEYAKEAKEFGLIGPVCSAEEAKE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084785129 172 VRKACGeRFLIVTTGVRPLGSAPLDQRRFAAPVMAIAAGADYLVIGRPVVQAKDPHAVVQQIL 234
Cdd:TIGR01740 153 IRKATG-DFLILTPGIRLDSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
11-238 2.81e-37

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 129.72  E-value: 2.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  11 RLIVAL-LADRMRdAEKMVKLLKKEVHIFEIGLPTYTALGPDVIKMVHDHQcKVFLDLKYHDIPSTVELAVRHATKLGVA 89
Cdd:PRK13813    5 RIILALdVTDRER-ALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYA-PVIADLKVADIPNTNRLICEAVFEAGAW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084785129  90 MLTVHATGGTEMLRRAAHAAEDAAGsktemplllAVTVLTSMetlADVGVQFEVREQVVRLAQLAKKCGFQGVVASPLEI 169
Cdd:PRK13813   83 GIIVHGFTGRDSLKAVVEAAAESGG---------KVFVVVEM---SHPGALEFIQPHADKLAKLAQEAGAFGVVAPATRP 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084785129 170 KPV---RKACGERFLIVTTGVRPLGSAPLDqrrfaapvmAIAAGADYLVIGRPVVQAKDPHAVVQQILKEIS 238
Cdd:PRK13813  151 ERVryiRSRLGDELKIISPGIGAQGGKAAD---------AIKAGADYVIVGRSIYNAADPREAAKAINEEIR 213
 
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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