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Conserved domains on  [gi|15598072|ref|NP_251566|]
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orotidine 5'-phosphate decarboxylase [Pseudomonas aeruginosa PAO1]

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;
4-231 2.03e-129

orotidine-5'-phosphate decarboxylase;


:

Pssm-ID: 234695  Cd Length: 230  Bit Score: 364.46  E-value: 2.03e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072    4 CQSPIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMG 83
Cdd:PRK00230   1 MDDRLIVALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVAKAVRALAKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072   84 VWMVNVHCSGGLRMMAACRETLEAFSgpRPLLIGVTVLTSMEREDLAGIGLDIEPQEQVLRLAALAQKAGMDGLVCSAQE 163
Cdd:PRK00230  81 VDMVNVHASGGPRMMKAAREALEPKS--RPLLIAVTVLTSMDEEDLAELGINLSLEEQVLRLAKLAQEAGLDGVVCSAQE 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598072  164 APALKAAH-PGLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPISQAADPAKALAAIVAEL 231
Cdd:PRK00230 159 AAAIREATgPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEI 227
 
Name Accession Description Interval E-value
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
4-231 2.03e-129

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 364.46  E-value: 2.03e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072    4 CQSPIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMG 83
Cdd:PRK00230   1 MDDRLIVALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVAKAVRALAKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072   84 VWMVNVHCSGGLRMMAACRETLEAFSgpRPLLIGVTVLTSMEREDLAGIGLDIEPQEQVLRLAALAQKAGMDGLVCSAQE 163
Cdd:PRK00230  81 VDMVNVHASGGPRMMKAAREALEPKS--RPLLIAVTVLTSMDEEDLAELGINLSLEEQVLRLAKLAQEAGLDGVVCSAQE 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598072  164 APALKAAH-PGLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPISQAADPAKALAAIVAEL 231
Cdd:PRK00230 159 AAAIREATgPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEI 227
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
5-216 1.27e-102

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: 296.63  E-value: 1.27e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072   5 QSPIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMGV 84
Cdd:COG0284   2 RSPLIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKERGLPVFLDLKRHDIPNTVAAAARAAAELGV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072  85 WMVNVHCSGGLRMMAACRETLEAfsgPRPLLIGVTVLTSMEREDLAGIGLDIEPQEQVLRLAALAQKAGMDGLVCSAQEA 164
Cdd:COG0284  82 DAVTVHAYGGRDMLEPALEAADE---SGKGVFAVTVLTSPGAADLQELGIEGPLYEVVLRLAKLAKEAGLDGVVCSATEA 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15598072 165 PALKAAHP-GLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPISQ 216
Cdd:COG0284 159 AALRAALGpDFLLLTPGIRPQGGDAGDQKRVGTPAEAIAAGADYLVVGRPITY 211
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
8-216 3.52e-78

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: 233.99  E-value: 3.52e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072   8 IIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMGVWMV 87
Cdd:cd04725   1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELGFLVFLDLKLGDIPNTVAAAAEALLGLGADAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072  88 NVHCSGGLRMMAACRETLEAfsgPRPLLIGVTVLTSMEREDLAGiGLDIEPQEQVLRLAALAQKAGMDGLVCSAQEAPAL 167
Cdd:cd04725  81 TVHPYGGSDMLKAALEAAEE---KGKGLFAVTVLSSPGALDLQE-GIPGSLEDLVERLAKLAREAGVDGVVCGATEPEAL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15598072 168 K-AAHPGLQLVTPGIRPAGSAqDDQRRILTPRQALDAGSDYLVIGRPISQ 216
Cdd:cd04725 157 RrALGPDFLILTPGIGAQGSG-DDQKRGGTPEDAIRAGADYIVVGRPITQ 205
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
7-214 5.37e-76

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: 228.59  E-value: 5.37e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072      7 PIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGK-GFEVFLDLKFHDIPNTTAMAVKAAAEMGVW 85
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELfGFPVFLDLKLHDIPNTVARAARAAAELGAD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072     86 MVNVHCSGGLRMMAACRETLEAFsgpRPLLIGVTVLTSMEREDLAGIGlDIEPQEQVLRLAALAQKAGMDGLVCSAQEAP 165
Cdd:smart00934  81 AVTVHAYAGSDMIEAALEAAKKY---GPGLLAVTVLTSPGAEDLQELG-DESLEEQVLRLAKLAKEAGLDGVVCSATEPE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 15598072    166 ALK-AAHPGLQLVTPGIRpagsaqdDQRRILTPRQALDAGSDYLVIGRPI 214
Cdd:smart00934 157 LIRrALGPDFLILTPGIG-------DQGRVATPAVAIGAGADIIVVGRPI 199
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
6-214 1.74e-71

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: 217.13  E-value: 1.74e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072     6 SPIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMGVW 85
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKHGFLIFLDLKFADIGNTVAKQAKYKAKLGAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072    86 MVNVHCSGGLRMMAACRETLEAFSgprPLLIGVTVLTSMEREDLAGIGLDIEPQEQVLRLAALAqkAGMDGLVCSAQEap 165
Cdd:pfam00215  81 IVTVHAYAGEGTLKAAKEAAEEYG---RGLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADLA--AGVDGVVASATE-- 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15598072   166 ALKAAHPGLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPI 214
Cdd:pfam00215 154 ALREILPDFLILTPGIGLQGGDAGGQQRVTTPAVAKEAGADIIIVGRGI 202
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
9-214 1.80e-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: 184.10  E-value: 1.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072     9 IVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMGVWMVN 88
Cdd:TIGR01740   2 IVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNKLIFLDLKFADIPNTVKLQYESKIKLGADMVN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072    89 VHCSGGLRMMAACRETLEAFsgPRPLLIGVTVLTSMEREdlagiGLDIEPQEQVLRLAALAQKAGMDGLVCSAQEAPALK 168
Cdd:TIGR01740  82 VHGFAGSESVEAAKEAASEF--GRRGLLAVTELTSMGSE-----EYGEDTMEKVVEYAKEAKEFGLIGPVCSAEEAKEIR 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 15598072   169 AAHPGLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPI 214
Cdd:TIGR01740 155 KATGDFLILTPGIRLDSKDADDQKRVVTLEEAKEAGADVIIVGRGI 200
 
Name Accession Description Interval E-value
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
4-231 2.03e-129

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 364.46  E-value: 2.03e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072    4 CQSPIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMG 83
Cdd:PRK00230   1 MDDRLIVALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQRGFKVFLDLKLHDIPNTVAKAVRALAKLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072   84 VWMVNVHCSGGLRMMAACRETLEAFSgpRPLLIGVTVLTSMEREDLAGIGLDIEPQEQVLRLAALAQKAGMDGLVCSAQE 163
Cdd:PRK00230  81 VDMVNVHASGGPRMMKAAREALEPKS--RPLLIAVTVLTSMDEEDLAELGINLSLEEQVLRLAKLAQEAGLDGVVCSAQE 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598072  164 APALKAAH-PGLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPISQAADPAKALAAIVAEL 231
Cdd:PRK00230 159 AAAIREATgPDFLLVTPGIRPAGSDAGDQKRVMTPAQAIAAGSDYIVVGRPITQAADPAAAYEAILAEI 227
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
5-216 1.27e-102

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: 296.63  E-value: 1.27e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072   5 QSPIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMGV 84
Cdd:COG0284   2 RSPLIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKERGLPVFLDLKRHDIPNTVAAAARAAAELGV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072  85 WMVNVHCSGGLRMMAACRETLEAfsgPRPLLIGVTVLTSMEREDLAGIGLDIEPQEQVLRLAALAQKAGMDGLVCSAQEA 164
Cdd:COG0284  82 DAVTVHAYGGRDMLEPALEAADE---SGKGVFAVTVLTSPGAADLQELGIEGPLYEVVLRLAKLAKEAGLDGVVCSATEA 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15598072 165 PALKAAHP-GLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPISQ 216
Cdd:COG0284 159 AALRAALGpDFLLLTPGIRPQGGDAGDQKRVGTPAEAIAAGADYLVVGRPITY 211
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
8-216 3.52e-78

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: 233.99  E-value: 3.52e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072   8 IIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMGVWMV 87
Cdd:cd04725   1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELGFLVFLDLKLGDIPNTVAAAAEALLGLGADAV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072  88 NVHCSGGLRMMAACRETLEAfsgPRPLLIGVTVLTSMEREDLAGiGLDIEPQEQVLRLAALAQKAGMDGLVCSAQEAPAL 167
Cdd:cd04725  81 TVHPYGGSDMLKAALEAAEE---KGKGLFAVTVLSSPGALDLQE-GIPGSLEDLVERLAKLAREAGVDGVVCGATEPEAL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15598072 168 K-AAHPGLQLVTPGIRPAGSAqDDQRRILTPRQALDAGSDYLVIGRPISQ 216
Cdd:cd04725 157 RrALGPDFLILTPGIGAQGSG-DDQKRGGTPEDAIRAGADYIVVGRPITQ 205
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
7-214 5.37e-76

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: 228.59  E-value: 5.37e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072      7 PIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGK-GFEVFLDLKFHDIPNTTAMAVKAAAEMGVW 85
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELfGFPVFLDLKLHDIPNTVARAARAAAELGAD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072     86 MVNVHCSGGLRMMAACRETLEAFsgpRPLLIGVTVLTSMEREDLAGIGlDIEPQEQVLRLAALAQKAGMDGLVCSAQEAP 165
Cdd:smart00934  81 AVTVHAYAGSDMIEAALEAAKKY---GPGLLAVTVLTSPGAEDLQELG-DESLEEQVLRLAKLAKEAGLDGVVCSATEPE 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 15598072    166 ALK-AAHPGLQLVTPGIRpagsaqdDQRRILTPRQALDAGSDYLVIGRPI 214
Cdd:smart00934 157 LIRrALGPDFLILTPGIG-------DQGRVATPAVAIGAGADIIVVGRPI 199
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
6-214 1.74e-71

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: 217.13  E-value: 1.74e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072     6 SPIIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMGVW 85
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKHGFLIFLDLKFADIGNTVAKQAKYKAKLGAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072    86 MVNVHCSGGLRMMAACRETLEAFSgprPLLIGVTVLTSMEREDLAGIGLDIEPQEQVLRLAALAqkAGMDGLVCSAQEap 165
Cdd:pfam00215  81 IVTVHAYAGEGTLKAAKEAAEEYG---RGLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADLA--AGVDGVVASATE-- 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 15598072   166 ALKAAHPGLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPI 214
Cdd:pfam00215 154 ALREILPDFLILTPGIGLQGGDAGGQQRVTTPAVAKEAGADIIIVGRGI 202
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
9-214 1.80e-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: 184.10  E-value: 1.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072     9 IVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGFEVFLDLKFHDIPNTTAMAVKAAAEMGVWMVN 88
Cdd:TIGR01740   2 IVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNKLIFLDLKFADIPNTVKLQYESKIKLGADMVN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072    89 VHCSGGLRMMAACRETLEAFsgPRPLLIGVTVLTSMEREdlagiGLDIEPQEQVLRLAALAQKAGMDGLVCSAQEAPALK 168
Cdd:TIGR01740  82 VHGFAGSESVEAAKEAASEF--GRRGLLAVTELTSMGSE-----EYGEDTMEKVVEYAKEAKEFGLIGPVCSAEEAKEIR 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 15598072   169 AAHPGLQLVTPGIRPAGSAQDDQRRILTPRQALDAGSDYLVIGRPI 214
Cdd:TIGR01740 155 KATGDFLILTPGIRLDSKDADDQKRVVTLEEAKEAGADVIIVGRGI 200
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
8-232 1.24e-57

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 181.72  E-value: 1.24e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072    8 IIVALDFPTREAALALADQLDPKLCRVKVGKELFTSCAAGIVETLRGKGfEVFLDLKFHDIPNTTAMAVKAAAEMGVWMV 87
Cdd:PRK13813   6 IILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYA-PVIADLKVADIPNTNRLICEAVFEAGAWGI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598072   88 NVHCSGGLRMMAACREtLEAFSGPRPLLIgvtvlTSMEREdlaGIGLDIEPqeQVLRLAALAQKAGMDGLVCSAQEAPAL 167
Cdd:PRK13813  85 IVHGFTGRDSLKAVVE-AAAESGGKVFVV-----VEMSHP---GALEFIQP--HADKLAKLAQEAGAFGVVAPATRPERV 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598072  168 ----KAAHPGLQLVTPGIRPAGSAqddqrriltPRQALDAGSDYLVIGRPISQAADPAKALAAIVAELG 232
Cdd:PRK13813 154 ryirSRLGDELKIISPGIGAQGGK---------AADAIKAGADYVIVGRSIYNAADPREAAKAINEEIR 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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