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Conserved domains on  [gi|13278066|gb|AAH03887|]
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Uridine monophosphate synthetase [Mus musculus]

Protein Classification

uridine 5'-monophosphate synthase( domain architecture ID 10785486)

uridine 5'-monophosphate synthase catalyzes the last two steps of the UMP biosynthesis, the addition of ribose-P to orotate by orotate phosphoribosyltransferase, to form orotidine-5'-monophosphate (OMP), and the decarboxylation of OMP by orotidine-5'-phosphate decarboxylase to form uridine monophosphate (UMP); in bacteria, these two domains/functions are located in separate proteins

CATH:  3.20.20.70|3.40.50.2020
EC:  2.4.2.10|4.1.1.23
Gene Ontology:  GO:0004590|GO:0019856|GO:0004588
PubMed:  11751055|12045113|12727511|12206759|11257493
SCOP:  4003062|4000253

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 252-466 6.60e-72

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: 226.76  E-value: 6.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   252 TNLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELtalaKRHEFLIFEDRKFADIGNTVKKQYEsgtF 331
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAEL----RKHGFLIFLDLKFADIGNTVAKQAK---Y 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   332 KIASWADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSLATGN-----YTKAAVGMAEEHCEFVIGFISGSRV 406
Cdd:pfam00215  74 KAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLVAELSSKGSLDLQEegdlgYTQEIVHRAADLAAGVDGVVASATE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13278066   407 SMK---PEFLHLTPGVQLEtGGDHLGQQYNSPQEVIGKRGSDVIIVGRGILAAANRLEAAEMY 466
Cdd:pfam00215 154 ALReilPDFLILTPGIGLQ-GGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 11-203 5.93e-65

Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


:

Pssm-ID: 440229  Cd Length: 201  Bit Score: 208.47  E-value: 5.93e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  11 LVTELYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATVICSANH 90
Cdd:COG0461   7 LAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  91 IPMLIRRKETKDYGTKRLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAQGIRL 170
Cdd:COG0461  87 LPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLEEAGVPL 166

                       170       180       190
                ....*....|....*....|....*....|...
gi 13278066 171 HAVCTLSQMLEILQQQEKIDADMVGRVKRFIQE 203
Cdd:COG0461 167 HSLLTLDDLLELLKEKGYIDPEELEALEAYREK 199
 
Name Accession Description Interval E-value
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 252-466 6.60e-72

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: 226.76  E-value: 6.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   252 TNLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELtalaKRHEFLIFEDRKFADIGNTVKKQYEsgtF 331
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAEL----RKHGFLIFLDLKFADIGNTVAKQAK---Y 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   332 KIASWADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSLATGN-----YTKAAVGMAEEHCEFVIGFISGSRV 406
Cdd:pfam00215  74 KAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLVAELSSKGSLDLQEegdlgYTQEIVHRAADLAAGVDGVVASATE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13278066   407 SMK---PEFLHLTPGVQLEtGGDHLGQQYNSPQEVIGKRGSDVIIVGRGILAAANRLEAAEMY 466
Cdd:pfam00215 154 ALReilPDFLILTPGIGLQ-GGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 11-203 5.93e-65

Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440229  Cd Length: 201  Bit Score: 208.47  E-value: 5.93e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  11 LVTELYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATVICSANH 90
Cdd:COG0461   7 LAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  91 IPMLIRRKETKDYGTKRLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAQGIRL 170
Cdd:COG0461  87 LPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLEEAGVPL 166

                       170       180       190
                ....*....|....*....|....*....|...
gi 13278066 171 HAVCTLSQMLEILQQQEKIDADMVGRVKRFIQE 203
Cdd:COG0461 167 HSLLTLDDLLELLKEKGYIDPEELEALEAYREK 199
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
 254-467 4.82e-64

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: 206.44  E-value: 4.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   254 LCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELTALAKRheflIFEDRKFADIGNTVKKQYESgtfKI 333
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNKL----IFLDLKFADIPNTVKLQYES---KI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   334 ASWADIVNAHVVPGSGVVKGLQEVGLPLHRACLL-IAEMSSAGSLATGNYT-KAAVGMAEEHCEF-VIGFI-SGSRVSMK 409
Cdd:TIGR01740  74 KLGADMVNVHGFAGSESVEAAKEAASEFGRRGLLaVTELTSMGSEEYGEDTmEKVVEYAKEAKEFgLIGPVcSAEEAKEI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13278066   410 ----PEFLHLTPGVQLEtGGDHLGQQYNSPQEVIGKRGSDVIIVGRGILAAANRLEAAEMYR 467
Cdd:TIGR01740 154 rkatGDFLILTPGIRLD-SKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 9-204 1.58e-60

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 196.98  E-value: 1.58e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    9 GPLVTELYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKnagiSFDS--VCGVPYTALPLATVIC 86
Cdd:PRK13809  11 DQAVAILYQIGAIKFGKFILASGEETPIYVDMRLVISSPEVLQTIATLIWRLRP----SFNSslLCGVPYTALTLATSIS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   87 SANHIPMLIRRKETKDYGTKR--LVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQ 164
Cdd:PRK13809  87 LKYNIPMVLRRKELKNVDPSDaiKVEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGACQPLG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 13278066  165 AQGIRLHAVCTLSQMLEILQQQEKIDADMVGRVKRFIQEN 204
Cdd:PRK13809 167 PQGIKLSSVFTVPDLIKSLISYGKLSSGDLTLANKIIKIL 206
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 254-466 1.10e-59

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: 195.09  E-value: 1.10e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066 254 LCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELTALAkrheFLIFEDRKFADIGNTVKKQYESGTFKi 333
Cdd:cd04725   1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELG----FLVFLDLKLGDIPNTVAAAAEALLGL- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066 334 asWADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSL--------ATGNYTKAAVGMAEEHCefVIGFISGS- 404
Cdd:cd04725  76 --GADAVTVHPYGGSDMLKAALEAAEEKGKGLFAVTVLSSPGALdlqegipgSLEDLVERLAKLAREAG--VDGVVCGAt 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13278066 405 -----RVSMKPEFLHLTPGVQLEtGGDHLGQQYNSPQEVIgKRGSDVIIVGRGILAAANRLEAAEMY 466
Cdd:cd04725 152 epealRRALGPDFLILTPGIGAQ-GSGDDQKRGGTPEDAI-RAGADYIVVGRPITQAADPVAAAEAI 216
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 253-466 2.11e-43

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: 152.32  E-value: 2.11e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    253 NLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELtalAKRHEFLIFEDRKFADIGNTVKKqyesGTFK 332
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKEL---KELFGFPVFLDLKLHDIPNTVAR----AARA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    333 IAS-WADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSLATGN----YTKAAVG-MAEEHCE-FVIGFISGS- 404
Cdd:smart00934  74 AAElGADAVTVHAYAGSDMIEAALEAAKKYGPGLLAVTVLTSPGAEDLQElgdeSLEEQVLrLAKLAKEaGLDGVVCSAt 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13278066    405 -----RVSMKPEFLHLTPGVQletggdhlGQQYNSPQEVIGKRGSDVIIVGRGILAAANRLEAAEMY 466
Cdd:smart00934 154 epeliRRALGPDFLILTPGIG--------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 15-179 1.01e-34

orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 129436 [Multi-domain]  Cd Length: 173  Bit Score: 127.93  E-value: 1.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    15 LYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNaGISFDSVCGVPYTALPLATVIC--SANH-- 90
Cdd:TIGR00336   3 LLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKS-HLEFDVIAGPALGGIPIATAVSvkLAKPgg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    91 -IPMLIRRKETKDYGTKRLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQ--GGKDKLQAQG 167
Cdd:TIGR00336  82 dIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQErsAGQEFEKEYG 161

                         170
                  ....*....|..
gi 13278066   168 IRLHAVCTLSQM 179
Cdd:TIGR00336 162 LPVISLITLKDL 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 53-175 7.31e-21

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 88.22  E-value: 7.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  53 VADILFQTAKNAGISFDSVCGVPYTALPLATVICSANHIPMLIRRKETKDYGTKR-------LVEGEINPGQTCLVIEDV 125
Cdd:cd06223   1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGKRVLLVDDV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 13278066 126 VTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAQGIRLHAVCT 175
Cdd:cd06223  81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDPVYSLFT 130
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 249-464 1.85e-20

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 89.66  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  249 KKETNLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELTALAKrheflIFEDRKFADIGNTVKKQYES 328
Cdd:PRK13813   1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP-----VIADLKVADIPNTNRLICEA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  329 gTFKIASWAdiVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSLATGN-YTKAAVGMAEEhcEFVIGFIS----G 403
Cdd:PRK13813  76 -VFEAGAWG--IIVHGFTGRDSLKAVVEAAAESGGKVFVVVEMSHPGALEFIQpHADKLAKLAQE--AGAFGVVApatrP 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13278066  404 SRVSM-----KPEFLHLTPGVqletggdhlGQQYNSPQEVIgKRGSDVIIVGRGILAAANRLEAAE 464
Cdd:PRK13813 151 ERVRYirsrlGDELKIISPGI---------GAQGGKAADAI-KAGADYVIVGRSIYNAADPREAAK 206
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
 254-469 4.35e-17

Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5'-phosphate decarboxylase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440053  Cd Length: 228  Bit Score: 80.15  E-value: 4.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066 254 LCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELtalaKRHEFLIFEDRKFADIGNTVKKQYESgtfkI 333
Cdd:COG0284   5 LIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEAL----KERGLPVFLDLKRHDIPNTVAAAARA----A 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066 334 ASW-ADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSS-----------AGSLAtgNYTKAAVGMAEEHCefVIGFI 401
Cdd:COG0284  77 AELgVDAVTVHAYGGRDMLEPALEAADESGKGVFAVTVLTSpgaadlqelgiEGPLY--EVVLRLAKLAKEAG--LDGVV 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13278066 402 SGS------RVSMKPEFLHLTPGVQLEtGGDhLGQQ--YNSPQEVIgKRGSDVIIVGRGILAAANRLEAAEMYRKA 469
Cdd:COG0284 153 CSAteaaalRAALGPDFLLLTPGIRPQ-GGD-AGDQkrVGTPAEAI-AAGADYLVVGRPITYAGDPRAAAEAIREE 225
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 43-162 5.52e-09

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 54.68  E-value: 5.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    43 IVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATVICSANHIPM---LIRRKETKDYGTKRLVEGEINP-GQT 118
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLafvRKVSYNPDTSEVMKTSSALPDLkGKT 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 13278066   119 CLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDK 162
Cdd:pfam00156  85 VLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPK 128
 
Name Accession Description Interval E-value
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 252-466 6.60e-72

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: 226.76  E-value: 6.60e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   252 TNLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELtalaKRHEFLIFEDRKFADIGNTVKKQYEsgtF 331
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAEL----RKHGFLIFLDLKFADIGNTVAKQAK---Y 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   332 KIASWADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSLATGN-----YTKAAVGMAEEHCEFVIGFISGSRV 406
Cdd:pfam00215  74 KAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLVAELSSKGSLDLQEegdlgYTQEIVHRAADLAAGVDGVVASATE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13278066   407 SMK---PEFLHLTPGVQLEtGGDHLGQQYNSPQEVIGKRGSDVIIVGRGILAAANRLEAAEMY 466
Cdd:pfam00215 154 ALReilPDFLILTPGIGLQ-GGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 11-203 5.93e-65

Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440229  Cd Length: 201  Bit Score: 208.47  E-value: 5.93e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  11 LVTELYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATVICSANH 90
Cdd:COG0461   7 LAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  91 IPMLIRRKETKDYGTKRLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAQGIRL 170
Cdd:COG0461  87 LPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLEEAGVPL 166

                       170       180       190
                ....*....|....*....|....*....|...
gi 13278066 171 HAVCTLSQMLEILQQQEKIDADMVGRVKRFIQE 203
Cdd:COG0461 167 HSLLTLDDLLELLKEKGYIDPEELEALEAYREK 199
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
 254-467 4.82e-64

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: 206.44  E-value: 4.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   254 LCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELTALAKRheflIFEDRKFADIGNTVKKQYESgtfKI 333
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNKL----IFLDLKFADIPNTVKLQYES---KI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   334 ASWADIVNAHVVPGSGVVKGLQEVGLPLHRACLL-IAEMSSAGSLATGNYT-KAAVGMAEEHCEF-VIGFI-SGSRVSMK 409
Cdd:TIGR01740  74 KLGADMVNVHGFAGSESVEAAKEAASEFGRRGLLaVTELTSMGSEEYGEDTmEKVVEYAKEAKEFgLIGPVcSAEEAKEI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13278066   410 ----PEFLHLTPGVQLEtGGDHLGQQYNSPQEVIGKRGSDVIIVGRGILAAANRLEAAEMYR 467
Cdd:TIGR01740 154 rkatGDFLILTPGIRLD-SKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 9-204 1.58e-60

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 196.98  E-value: 1.58e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    9 GPLVTELYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKnagiSFDS--VCGVPYTALPLATVIC 86
Cdd:PRK13809  11 DQAVAILYQIGAIKFGKFILASGEETPIYVDMRLVISSPEVLQTIATLIWRLRP----SFNSslLCGVPYTALTLATSIS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   87 SANHIPMLIRRKETKDYGTKR--LVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQ 164
Cdd:PRK13809  87 LKYNIPMVLRRKELKNVDPSDaiKVEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGACQPLG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 13278066  165 AQGIRLHAVCTLSQMLEILQQQEKIDADMVGRVKRFIQEN 204
Cdd:PRK13809 167 PQGIKLSSVFTVPDLIKSLISYGKLSSGDLTLANKIIKIL 206
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 254-466 1.10e-59

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: 195.09  E-value: 1.10e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066 254 LCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELTALAkrheFLIFEDRKFADIGNTVKKQYESGTFKi 333
Cdd:cd04725   1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELG----FLVFLDLKLGDIPNTVAAAAEALLGL- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066 334 asWADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSL--------ATGNYTKAAVGMAEEHCefVIGFISGS- 404
Cdd:cd04725  76 --GADAVTVHPYGGSDMLKAALEAAEEKGKGLFAVTVLSSPGALdlqegipgSLEDLVERLAKLAREAG--VDGVVCGAt 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13278066 405 -----RVSMKPEFLHLTPGVQLEtGGDHLGQQYNSPQEVIgKRGSDVIIVGRGILAAANRLEAAEMY 466
Cdd:cd04725 152 epealRRALGPDFLILTPGIGAQ-GSGDDQKRGGTPEDAI-RAGADYIVVGRPITQAADPVAAAEAI 216
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
11-192 3.57e-50

bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 177.95  E-value: 3.57e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   11 LVTELYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNagISFDSVCGVPYTALPLATVICSANH 90
Cdd:PRK05500 290 LILQLYDIGCLLFGEYVQASGATFSYYIDLRKIISNPQLFHQVLSAYAEILKN--LTFDRIAGIPYGSLPTATGLALHLH 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   91 IPMLIRRKETKDYGTKRLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAQGIRL 170
Cdd:PRK05500 368 HPMIFPRKEVKAHGTRRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVFIDHEQGVKDKLQSHGYQA 447

                        170       180
                 ....*....|....*....|..
gi 13278066  171 HAVCTLSQMLEILQQQEKIDAD 192
Cdd:PRK05500 448 YSVLTISEITETLYQAGRINEE 469
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 14-204 1.51e-49

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 168.03  E-value: 1.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   14 ELYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATVICSANHIPM 93
Cdd:PRK00455  11 FLLEIGALLFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAAAVARALDLPA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   94 LIRRKETKDYGTKRLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAQGIRLHAV 173
Cdd:PRK00455  91 IFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQSAAQEVFADAGVPLISL 170

                        170       180       190
                 ....*....|....*....|....*....|.
gi 13278066  174 CTLSQMLEILQQQEkIDADMVGRVKRFIQEN 204
Cdd:PRK00455 171 ITLDDLLEYAEEGP-LCKEGLPAVKAYRRNY 200
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 253-466 2.11e-43

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: 152.32  E-value: 2.11e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    253 NLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELtalAKRHEFLIFEDRKFADIGNTVKKqyesGTFK 332
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKEL---KELFGFPVFLDLKLHDIPNTVAR----AARA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    333 IAS-WADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSLATGN----YTKAAVG-MAEEHCE-FVIGFISGS- 404
Cdd:smart00934  74 AAElGADAVTVHAYAGSDMIEAALEAAKKYGPGLLAVTVLTSPGAEDLQElgdeSLEEQVLrLAKLAKEaGLDGVVCSAt 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13278066    405 -----RVSMKPEFLHLTPGVQletggdhlGQQYNSPQEVIGKRGSDVIIVGRGILAAANRLEAAEMY 466
Cdd:smart00934 154 epeliRRALGPDFLILTPGIG--------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 15-179 1.01e-34

orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 129436 [Multi-domain]  Cd Length: 173  Bit Score: 127.93  E-value: 1.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    15 LYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNaGISFDSVCGVPYTALPLATVIC--SANH-- 90
Cdd:TIGR00336   3 LLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKS-HLEFDVIAGPALGGIPIATAVSvkLAKPgg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    91 -IPMLIRRKETKDYGTKRLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQ--GGKDKLQAQG 167
Cdd:TIGR00336  82 dIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQErsAGQEFEKEYG 161

                         170
                  ....*....|..
gi 13278066   168 IRLHAVCTLSQM 179
Cdd:TIGR00336 162 LPVISLITLKDL 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 53-175 7.31e-21

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 88.22  E-value: 7.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  53 VADILFQTAKNAGISFDSVCGVPYTALPLATVICSANHIPMLIRRKETKDYGTKR-------LVEGEINPGQTCLVIEDV 125
Cdd:cd06223   1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGKRVLLVDDV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 13278066 126 VTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAQGIRLHAVCT 175
Cdd:cd06223  81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDPVYSLFT 130
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 249-464 1.85e-20

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 89.66  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  249 KKETNLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELTALAKrheflIFEDRKFADIGNTVKKQYES 328
Cdd:PRK13813   1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP-----VIADLKVADIPNTNRLICEA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  329 gTFKIASWAdiVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSLATGN-YTKAAVGMAEEhcEFVIGFIS----G 403
Cdd:PRK13813  76 -VFEAGAWG--IIVHGFTGRDSLKAVVEAAAESGGKVFVVVEMSHPGALEFIQpHADKLAKLAQE--AGAFGVVApatrP 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13278066  404 SRVSM-----KPEFLHLTPGVqletggdhlGQQYNSPQEVIgKRGSDVIIVGRGILAAANRLEAAE 464
Cdd:PRK13813 151 ERVRYirsrlGDELKIISPGI---------GAQGGKAADAI-KAGADYVIVGRSIYNAADPREAAK 206
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 12-160 2.95e-19

orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of orotate phosphoribosyltransferases. Members include the experimentally determined example from Thermus aquaticus and additional examples from Caulobacter crescentus, Helicobacter pylori, Mesorhizobium loti, and related species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273579  Cd Length: 187  Bit Score: 85.22  E-value: 2.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    12 VTELY-DVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATVICSANH 90
Cdd:TIGR01367   2 VLDIYkQAGALHEGHFLLSSGKHSPYFLQSATLLEHPEALMELGGELAQKILDYGLKVDFIVGPAMGGVILGYEVARQLS 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13278066    91 IPMLIRRKETkdyGTKRLVEG-EINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGK 160
Cdd:TIGR01367  82 VRSIFAEREG---GGMKLRRGfAVKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLACIIDRSQGGK 149
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
 254-469 4.35e-17

Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5'-phosphate decarboxylase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440053  Cd Length: 228  Bit Score: 80.15  E-value: 4.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066 254 LCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELtalaKRHEFLIFEDRKFADIGNTVKKQYESgtfkI 333
Cdd:COG0284   5 LIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEAL----KERGLPVFLDLKRHDIPNTVAAAARA----A 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066 334 ASW-ADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSS-----------AGSLAtgNYTKAAVGMAEEHCefVIGFI 401
Cdd:COG0284  77 AELgVDAVTVHAYGGRDMLEPALEAADESGKGVFAVTVLTSpgaadlqelgiEGPLY--EVVLRLAKLAKEAG--LDGVV 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13278066 402 SGS------RVSMKPEFLHLTPGVQLEtGGDhLGQQ--YNSPQEVIgKRGSDVIIVGRGILAAANRLEAAEMYRKA 469
Cdd:COG0284 153 CSAteaaalRAALGPDFLLLTPGIRPQ-GGD-AGDQkrVGTPAEAI-AAGADYLVVGRPITYAGDPRAAAEAIREE 225
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
254-464 1.80e-09

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 57.84  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  254 LCLSADVSEARELLQLADALGPSICMLKthvdI-LNDFTLDVMEELTALAKRHeFLIFEDRKFADIGNTVKKQYESgtfk 332
Cdd:PRK00230   5 LIVALDFPSKEEALAFLDQLDPAVLFVK----VgMELFTAGGPQFVRELKQRG-FKVFLDLKLHDIPNTVAKAVRA---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  333 IASW-ADIVNAHVVPGSGVVKGLQEVGLPLHRACLL------------IAEMSSAGSLATG--NYTKAA----------- 386
Cdd:PRK00230  76 LAKLgVDMVNVHASGGPRMMKAAREALEPKSRPLLIavtvltsmdeedLAELGINLSLEEQvlRLAKLAqeagldgvvcs 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  387 ---VGMAEEHCEfvigfisgsrvsmkPEFLHLTPGVQLEtgGDHLGQQYN--SPQEVIgKRGSDVIIVGRGILAAANRLE 461
Cdd:PRK00230 156 aqeAAAIREATG--------------PDFLLVTPGIRPA--GSDAGDQKRvmTPAQAI-AAGSDYIVVGRPITQAADPAA 218


                 ...
gi 13278066  462 AAE 464
Cdd:PRK00230 219 AYE 221
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 36-154 3.56e-09

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 56.42  E-value: 3.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   36 VYIDLRGIVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATvicsanhipmLIRRKETKD---YGTKRLVEGE 112
Cdd:PRK02277  54 IHIDWSSIGSSSSRLRYIASAMADMLEKEDEEVDVVVGIAKSGVPLAT----------LVADELGKDlaiYHPKKWDHGE 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13278066  113 INP-------------GQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLD 154
Cdd:PRK02277 124 GEKktgsfsrnfasveGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLID 178
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 43-162 5.52e-09

Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.


Pssm-ID: 425489 [Multi-domain]  Cd Length: 150  Bit Score: 54.68  E-value: 5.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066    43 IVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATVICSANHIPM---LIRRKETKDYGTKRLVEGEINP-GQT 118
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLafvRKVSYNPDTSEVMKTSSALPDLkGKT 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 13278066   119 CLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDK 162
Cdd:pfam00156  85 VLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPK 128
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 27-176 6.85e-08

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 52.00  E-value: 6.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  27 VLKSGLsspVYIDLRGIVSRPRLLSQVADILFQTAKNAGIsfDSVCGVPYTALPLATVICSANHIPMLIRRKETK----- 101
Cdd:COG0503  13 FPKPGI---LFRDITPLLGDPELFRAAGDELAERFADKGI--DKVVGIEARGFILAAALAYALGVPFVPARKPGKlpget 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066 102 -------DYGTKRLVE---GEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLD-REQGGKDKLqaQGIRL 170
Cdd:COG0503  88 vseeydlEYGTGDTLElhkDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIElGFLGGREKL--RDYPV 165


                ....*.
gi 13278066 171 HAVCTL 176
Cdd:COG0503 166 ESLLTL 171
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 46-166 1.40e-06

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 48.63  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   46 RPRLLSQVAdilFQTAKNAGISFDSVCGVPYTALPLATVICSANHIPMLIRRK----------ETKDYGTKRLvEGE--- 112
Cdd:PRK12560  33 RPKVLKETA---KEIIKYIDKDIDKIVTEEDKGAPLATPVSLLSGKPLAMARWypyslselnyNVVEIGSEYF-EGVvyl 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13278066  113 --INPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQ-GGKDKLQAQ 166
Cdd:PRK12560 109 ngIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQnNGRKKLFTQ 165
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 81-152 7.75e-05

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 43.66  E-value: 7.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066  81 LATVICSANHIPM----LIRRKETKDYGTK-------------RLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEG 143
Cdd:COG1040 103 LARALARALGIPVlpdlLRRVRATPSQAGLsraerrrnlrgafAVRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAG 182


                ....*....
gi 13278066 144 LKVTDAIVL 152
Cdd:COG1040 183 AARVDVLVL 191
PLN02293 PLN02293
adenine phosphoribosyltransferase
 39-164 1.39e-03

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 39.66  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13278066   39 DLRGIVSRPRLLSQVADILFQTAKNAGIsfDSVCGVPYTAL----PLATVIcSANHIPM---------LIRRKETKDYGT 105
Cdd:PLN02293  36 DITTLLLDPKAFKDTIDLFVERYRDMGI--SVVAGIEARGFifgpPIALAI-GAKFVPLrkpgklpgeVISEEYVLEYGT 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13278066  106 KRLV--EGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTD-AIVLLDREQGGKDKLQ 164
Cdd:PLN02293 113 DCLEmhVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVEcACVIELPELKGREKLN 174
 
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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