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Conserved domains on  [gi|4507835|ref|NP_000364|]
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uridine 5'-monophosphate synthase [Homo sapiens]

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 1.61e-73

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: 231.00  E-value: 1.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    252 TNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELitlaKCHEFLIFEDRKFADIGNTVKKQYEggiF 331
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAEL----RKHGFLIFLDLKFADIGNTVAKQAK---Y 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    332 KIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLATGD-----YTRAAVRMAEEHSEFVVGFISGSRV 406
Cdd:pfam00215  74 KAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLVAELSSKGSLDLQEegdlgYTQEIVHRAADLAAGVDGVVASATE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507835    407 SMK---PEFLHLTPGVQLeAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMY 466
Cdd:pfam00215 154 ALReilPDFLILTPGIGL-QGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 15-203 2.02e-64

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


:

Pssm-ID: 440229  Cd Length: 201  Bit Score: 206.93  E-value: 2.02e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   15 LYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPML 94
Cdd:COG0461  11 LLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALGLPAI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   95 IRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVC 174
Cdd:COG0461  91 FVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLEEAGVPLHSLL 170

                       170       180
                ....*....|....*....|....*....
gi 4507835  175 TLSKMLEILEQQKKVDAETVGRVKRFIQE 203
Cdd:COG0461 171 TLDDLLELLKEKGYIDPEELEALEAYREK 199
 
Name Accession Description Interval E-value
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 252-466 1.61e-73

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: 231.00  E-value: 1.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    252 TNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELitlaKCHEFLIFEDRKFADIGNTVKKQYEggiF 331
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAEL----RKHGFLIFLDLKFADIGNTVAKQAK---Y 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    332 KIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLATGD-----YTRAAVRMAEEHSEFVVGFISGSRV 406
Cdd:pfam00215  74 KAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLVAELSSKGSLDLQEegdlgYTQEIVHRAADLAAGVDGVVASATE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507835    407 SMK---PEFLHLTPGVQLeAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMY 466
Cdd:pfam00215 154 ALReilPDFLILTPGIGL-QGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 15-203 2.02e-64

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 206.93  E-value: 2.02e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   15 LYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPML 94
Cdd:COG0461  11 LLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALGLPAI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   95 IRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVC 174
Cdd:COG0461  91 FVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLEEAGVPLHSLL 170

                       170       180
                ....*....|....*....|....*....
gi 4507835  175 TLSKMLEILEQQKKVDAETVGRVKRFIQE 203
Cdd:COG0461 171 TLDDLLELLKEKGYIDPEELEALEAYREK 199
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
 254-467 3.59e-62

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: 201.43  E-value: 3.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    254 LCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKchefLIFEDRKFADIGNTVKKQYEGgifKI 333
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNK----LIFLDLKFADIPNTVKLQYES---KI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    334 ASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLL-IAEMSSTGSLATGDYT-RAAVRMAEEHSEFVV-GFI-SGSRVSMK 409
Cdd:TIGR01740  74 KLGADMVNVHGFAGSESVEAAKEAASEFGRRGLLaVTELTSMGSEEYGEDTmEKVVEYAKEAKEFGLiGPVcSAEEAKEI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4507835    410 ----PEFLHLTPGVQLeAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMYR 467
Cdd:TIGR01740 154 rkatGDFLILTPGIRL-DSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 254-466 8.58e-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: 198.17  E-value: 8.58e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835  254 LCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAkcheFLIFEDRKFADIGNTVKKQYEGGIFKi 333
Cdd:cd04725   1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELG----FLVFLDLKLGDIPNTVAAAAEALLGL- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835  334 asWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSL--------ATGDYTRAAVRMAEEHSefVVGFISGS- 404
Cdd:cd04725  76 --GADAVTVHPYGGSDMLKAALEAAEEKGKGLFAVTVLSSPGALdlqegipgSLEDLVERLAKLAREAG--VDGVVCGAt 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507835  405 -----RVSMKPEFLHLTPGVQLEAGGDnLGQQYNSPQEVIgKRGSDIIIVGRGIISAADRLEAAEMY 466
Cdd:cd04725 152 epealRRALGPDFLILTPGIGAQGSGD-DQKRGGTPEDAI-RAGADYIVVGRPITQAADPVAAAEAI 216
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 9-204 1.55e-60

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 196.98  E-value: 1.55e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     9 GPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFqtaqNAGISF--DTVCGVPYTALPLATVIC 86
Cdd:PRK13809  11 DQAVAILYQIGAIKFGKFILASGEETPIYVDMRLVISSPEVLQTIATLIW----RLRPSFnsSLLCGVPYTALTLATSIS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    87 STNQIPMLIRRKETKDYGTKR--LVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQ 164
Cdd:PRK13809  87 LKYNIPMVLRRKELKNVDPSDaiKVEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGACQPLG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4507835   165 AHGIRLHSVCTLSKMLEILEQQKKVDAETVGRVKRFIQEN 204
Cdd:PRK13809 167 PQGIKLSSVFTVPDLIKSLISYGKLSSGDLTLANKIIKIL 206
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 253-466 7.85e-45

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: 156.17  E-value: 7.85e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     253 NLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELitlAKCHEFLIFEDRKFADIGNTVKKqyegGIFK 332
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKEL---KELFGFPVFLDLKLHDIPNTVAR----AARA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     333 IAS-WADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLA-----TGDYTRAAVRMAEEHSE-FVVGFISGS- 404
Cdd:smart00934  74 AAElGADAVTVHAYAGSDMIEAALEAAKKYGPGLLAVTVLTSPGAEDlqelgDESLEEQVLRLAKLAKEaGLDGVVCSAt 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507835     405 -----RVSMKPEFLHLTPGVQleaggdnlGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMY 466
Cdd:smart00934 154 epeliRRALGPDFLILTPGIG--------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 15-177 1.17e-33

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: 124.85  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     15 LYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILfQTAQNAGISFDTVCGVPYTALPLATVIC-----STN 89
Cdd:TIGR00336   3 LLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYA-AAIIKSHLEFDVIAGPALGGIPIATAVSvklakPGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     90 QIPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQ--GGKDKLQAHG 167
Cdd:TIGR00336  82 DIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQErsAGQEFEKEYG 161

                         170
                  ....*....|
gi 4507835    168 IRLHSVCTLS 177
Cdd:TIGR00336 162 LPVISLITLK 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 53-175 9.74e-20

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: 85.14  E-value: 9.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   53 VADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKR-------LVEGTINPGETCLIIEDV 125
Cdd:cd06223   1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGKRVLLVDDV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4507835  126 VTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCT 175
Cdd:cd06223  81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDPVYSLFT 130
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 249-464 9.94e-20

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 87.34  E-value: 9.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   249 KKETNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKcheflIFEDRKFADIGNTVKKQYEG 328
Cdd:PRK13813   1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP-----VIADLKVADIPNTNRLICEA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   329 gIFKIASWAdlVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLAT-GDYTRAAVRMAEEHSEFvvGFIS----G 403
Cdd:PRK13813  76 -VFEAGAWG--IIVHGFTGRDSLKAVVEAAAESGGKVFVVVEMSHPGALEFiQPHADKLAKLAQEAGAF--GVVApatrP 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507835   404 SRVSM-----KPEFLHLTPGVqleaggdnlGQQYNSPQEVIgKRGSDIIIVGRGIISAADRLEAAE 464
Cdd:PRK13813 151 ERVRYirsrlGDELKIISPGI---------GAQGGKAADAI-KAGADYVIVGRSIYNAADPREAAK 206
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
 254-469 2.99e-19

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: 86.31  E-value: 2.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835  254 LCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITlakcHEFLIFEDRKFADIGNTVKKqYEGGIFKI 333
Cdd:COG0284   5 LIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKE----RGLPVFLDLKRHDIPNTVAA-AARAAAEL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835  334 AswADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGS---------LATGDYTRAAVRMAEEHSefVVGFISGS 404
Cdd:COG0284  80 G--VDAVTVHAYGGRDMLEPALEAADESGKGVFAVTVLTSPGAadlqelgieGPLYEVVLRLAKLAKEAG--LDGVVCSA 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507835  405 ------RVSMKPEFLHLTPGVQLEagGDNLGQQ--YNSPQEVIgKRGSDIIIVGRGIISAADRLEAAEMYRKA 469
Cdd:COG0284 156 teaaalRAALGPDFLLLTPGIRPQ--GGDAGDQkrVGTPAEAI-AAGADYLVVGRPITYAGDPRAAAEAIREE 225
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 43-162 9.48e-10

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: 56.99  E-value: 9.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     43 IVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPM---LIRRKETKDYGTKRLVEGTINP-GET 118
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLafvRKVSYNPDTSEVMKTSSALPDLkGKT 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 4507835    119 CLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDK 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 1.61e-73

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: 231.00  E-value: 1.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    252 TNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELitlaKCHEFLIFEDRKFADIGNTVKKQYEggiF 331
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAEL----RKHGFLIFLDLKFADIGNTVAKQAK---Y 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    332 KIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLATGD-----YTRAAVRMAEEHSEFVVGFISGSRV 406
Cdd:pfam00215  74 KAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLVAELSSKGSLDLQEegdlgYTQEIVHRAADLAAGVDGVVASATE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507835    407 SMK---PEFLHLTPGVQLeAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMY 466
Cdd:pfam00215 154 ALReilPDFLILTPGIGL-QGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 15-203 2.02e-64

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 206.93  E-value: 2.02e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   15 LYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPML 94
Cdd:COG0461  11 LLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGPEFDAVAGPATGGIPLAAAVARALGLPAI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   95 IRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVC 174
Cdd:COG0461  91 FVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLEEAGVPLHSLL 170

                       170       180
                ....*....|....*....|....*....
gi 4507835  175 TLSKMLEILEQQKKVDAETVGRVKRFIQE 203
Cdd:COG0461 171 TLDDLLELLKEKGYIDPEELEALEAYREK 199
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
 254-467 3.59e-62

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: 201.43  E-value: 3.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    254 LCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKchefLIFEDRKFADIGNTVKKQYEGgifKI 333
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNK----LIFLDLKFADIPNTVKLQYES---KI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    334 ASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLL-IAEMSSTGSLATGDYT-RAAVRMAEEHSEFVV-GFI-SGSRVSMK 409
Cdd:TIGR01740  74 KLGADMVNVHGFAGSESVEAAKEAASEFGRRGLLaVTELTSMGSEEYGEDTmEKVVEYAKEAKEFGLiGPVcSAEEAKEI 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4507835    410 ----PEFLHLTPGVQLeAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMYR 467
Cdd:TIGR01740 154 rkatGDFLILTPGIRL-DSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 254-466 8.58e-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: 198.17  E-value: 8.58e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835  254 LCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAkcheFLIFEDRKFADIGNTVKKQYEGGIFKi 333
Cdd:cd04725   1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELG----FLVFLDLKLGDIPNTVAAAAEALLGL- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835  334 asWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSL--------ATGDYTRAAVRMAEEHSefVVGFISGS- 404
Cdd:cd04725  76 --GADAVTVHPYGGSDMLKAALEAAEEKGKGLFAVTVLSSPGALdlqegipgSLEDLVERLAKLAREAG--VDGVVCGAt 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507835  405 -----RVSMKPEFLHLTPGVQLEAGGDnLGQQYNSPQEVIgKRGSDIIIVGRGIISAADRLEAAEMY 466
Cdd:cd04725 152 epealRRALGPDFLILTPGIGAQGSGD-DQKRGGTPEDAI-RAGADYIVVGRPITQAADPVAAAEAI 216
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
 9-204 1.55e-60

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 196.98  E-value: 1.55e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     9 GPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFqtaqNAGISF--DTVCGVPYTALPLATVIC 86
Cdd:PRK13809  11 DQAVAILYQIGAIKFGKFILASGEETPIYVDMRLVISSPEVLQTIATLIW----RLRPSFnsSLLCGVPYTALTLATSIS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    87 STNQIPMLIRRKETKDYGTKR--LVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQ 164
Cdd:PRK13809  87 LKYNIPMVLRRKELKNVDPSDaiKVEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGACQPLG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4507835   165 AHGIRLHSVCTLSKMLEILEQQKKVDAETVGRVKRFIQEN 204
Cdd:PRK13809 167 PQGIKLSSVFTVPDLIKSLISYGKLSSGDLTLANKIIKIL 206
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
11-192 1.91e-49

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


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 176.03  E-value: 1.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    11 LVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNagISFDTVCGVPYTALPLATVICSTNQ 90
Cdd:PRK05500 290 LILQLYDIGCLLFGEYVQASGATFSYYIDLRKIISNPQLFHQVLSAYAEILKN--LTFDRIAGIPYGSLPTATGLALHLH 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    91 IPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRL 170
Cdd:PRK05500 368 HPMIFPRKEVKAHGTRRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVFIDHEQGVKDKLQSHGYQA 447

                        170       180
                 ....*....|....*....|..
gi 4507835   171 HSVCTLSKMLEILEQQKKVDAE 192
Cdd:PRK05500 448 YSVLTISEITETLYQAGRINEE 469
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 15-204 1.18e-48

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 165.71  E-value: 1.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    15 LYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPML 94
Cdd:PRK00455  12 LLEIGALLFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIEFDVVAGPATGGIPLAAAVARALDLPAI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    95 IRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVC 174
Cdd:PRK00455  92 FVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQSAAQEVFADAGVPLISLI 171

                        170       180       190
                 ....*....|....*....|....*....|
gi 4507835   175 TLSKMLEILEqQKKVDAETVGRVKRFIQEN 204
Cdd:PRK00455 172 TLDDLLEYAE-EGPLCKEGLPAVKAYRRNY 200
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 253-466 7.85e-45

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: 156.17  E-value: 7.85e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     253 NLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELitlAKCHEFLIFEDRKFADIGNTVKKqyegGIFK 332
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKEL---KELFGFPVFLDLKLHDIPNTVAR----AARA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     333 IAS-WADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLA-----TGDYTRAAVRMAEEHSE-FVVGFISGS- 404
Cdd:smart00934  74 AAElGADAVTVHAYAGSDMIEAALEAAKKYGPGLLAVTVLTSPGAEDlqelgDESLEEQVLRLAKLAKEaGLDGVVCSAt 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507835     405 -----RVSMKPEFLHLTPGVQleaggdnlGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMY 466
Cdd:smart00934 154 epeliRRALGPDFLILTPGIG--------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 15-177 1.17e-33

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: 124.85  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     15 LYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILfQTAQNAGISFDTVCGVPYTALPLATVIC-----STN 89
Cdd:TIGR00336   3 LLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYA-AAIIKSHLEFDVIAGPALGGIPIATAVSvklakPGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     90 QIPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQ--GGKDKLQAHG 167
Cdd:TIGR00336  82 DIPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQErsAGQEFEKEYG 161

                         170
                  ....*....|
gi 4507835    168 IRLHSVCTLS 177
Cdd:TIGR00336 162 LPVISLITLK 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 53-175 9.74e-20

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: 85.14  E-value: 9.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   53 VADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKR-------LVEGTINPGETCLIIEDV 125
Cdd:cd06223   1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGKRVLLVDDV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4507835  126 VTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCT 175
Cdd:cd06223  81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGDPVYSLFT 130
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 249-464 9.94e-20

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 87.34  E-value: 9.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   249 KKETNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKcheflIFEDRKFADIGNTVKKQYEG 328
Cdd:PRK13813   1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP-----VIADLKVADIPNTNRLICEA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   329 gIFKIASWAdlVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLAT-GDYTRAAVRMAEEHSEFvvGFIS----G 403
Cdd:PRK13813  76 -VFEAGAWG--IIVHGFTGRDSLKAVVEAAAESGGKVFVVVEMSHPGALEFiQPHADKLAKLAQEAGAF--GVVApatrP 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507835   404 SRVSM-----KPEFLHLTPGVqleaggdnlGQQYNSPQEVIgKRGSDIIIVGRGIISAADRLEAAE 464
Cdd:PRK13813 151 ERVRYirsrlGDELKIISPGI---------GAQGGKAADAI-KAGADYVIVGRSIYNAADPREAAK 206
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
 254-469 2.99e-19

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: 86.31  E-value: 2.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835  254 LCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITlakcHEFLIFEDRKFADIGNTVKKqYEGGIFKI 333
Cdd:COG0284   5 LIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKE----RGLPVFLDLKRHDIPNTVAA-AARAAAEL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835  334 AswADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGS---------LATGDYTRAAVRMAEEHSefVVGFISGS 404
Cdd:COG0284  80 G--VDAVTVHAYGGRDMLEPALEAADESGKGVFAVTVLTSPGAadlqelgieGPLYEVVLRLAKLAKEAG--LDGVVCSA 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4507835  405 ------RVSMKPEFLHLTPGVQLEagGDNLGQQ--YNSPQEVIgKRGSDIIIVGRGIISAADRLEAAEMYRKA 469
Cdd:COG0284 156 teaaalRAALGPDFLLLTPGIRPQ--GGDAGDQkrVGTPAEAI-AAGADYLVVGRPITYAGDPRAAAEAIREE 225
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 20-160 7.00e-18

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: 81.37  E-value: 7.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     20 AFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKE 99
Cdd:TIGR01367  11 ALHEGHFLLSSGKHSPYFLQSATLLEHPEALMELGGELAQKILDYGLKVDFIVGPAMGGVILGYEVARQLSVRSIFAERE 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507835    100 TKDYGTKRLVEgtINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGK 160
Cdd:TIGR01367  91 GGGMKLRRGFA--VKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLACIIDRSQGGK 149
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 36-154 2.29e-10

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 59.88  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    36 IYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKRLVEGTIN- 114
Cdd:PRK02277  54 IHIDWSSIGSSSSRLRYIASAMADMLEKEDEEVDVVVGIAKSGVPLATLVADELGKDLAIYHPKKWDHGEGEKKTGSFSr 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 4507835   115 -----PGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLD 154
Cdd:PRK02277 134 nfasvEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLID 178
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 43-162 9.48e-10

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: 56.99  E-value: 9.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835     43 IVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPM---LIRRKETKDYGTKRLVEGTINP-GET 118
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLafvRKVSYNPDTSEVMKTSSALPDLkGKT 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 4507835    119 CLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDK 162
Cdd:pfam00156  85 VLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPK 128
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
254-464 2.75e-08

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 54.37  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   254 LCLSADVSLARELLQLADALGPSICMLKthvdilndftldVMKELIT------LAKCHE--FLIFEDRKFADIGNTVKKQ 325
Cdd:PRK00230   5 LIVALDFPSKEEALAFLDQLDPAVLFVK------------VGMELFTaggpqfVRELKQrgFKVFLDLKLHDIPNTVAKA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   326 YEGgifkIASW-ADLVNAHVVPGSGVVKGLQEVGLPLHRGCLL------------IAEMSSTGSLATgdytrAAVRMAEE 392
Cdd:PRK00230  73 VRA----LAKLgVDMVNVHASGGPRMMKAAREALEPKSRPLLIavtvltsmdeedLAELGINLSLEE-----QVLRLAKL 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   393 HSEF----VVgfISGSRVSM-----KPEFLHLTPGVQLEagGDNLGQQYN--SPQEVIgKRGSDIIIVGRGIISAADRLE 461
Cdd:PRK00230 144 AQEAgldgVV--CSAQEAAAireatGPDFLLVTPGIRPA--GSDAGDQKRvmTPAQAI-AAGSDYIVVGRPITQAADPAA 218


                 ...
gi 4507835   462 AAE 464
Cdd:PRK00230 219 AYE 221
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 27-176 2.98e-07

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: 50.07  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   27 VLKSGLsspIYIDLRGIVSRPRLLSQVADILFQTAQNAGIsfDTVCGVPYTALPLATVICSTNQIPMLIRRKETK----- 101
Cdd:COG0503  13 FPKPGI---LFRDITPLLGDPELFRAAGDELAERFADKGI--DKVVGIEARGFILAAALAYALGVPFVPARKPGKlpget 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835  102 -------DYGTKRLVE---GTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLD-REQGGKDKLQAHgiRL 170
Cdd:COG0503  88 vseeydlEYGTGDTLElhkDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIElGFLGGREKLRDY--PV 165


                ....*.
gi 4507835  171 HSVCTL 176
Cdd:COG0503 166 ESLLTL 171
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 46-163 1.89e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 45.16  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835    46 RPRLLSQVAdilFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRK----------ETKDYGTKRLvEGT--- 112
Cdd:PRK12560  33 RPKVLKETA---KEIIKYIDKDIDKIVTEEDKGAPLATPVSLLSGKPLAMARWypyslselnyNVVEIGSEYF-EGVvyl 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4507835   113 --INPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQ-GGKDKL 163
Cdd:PRK12560 109 ngIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQnNGRKKL 162
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 81-152 1.05e-03

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 40.19  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507835   81 LATVICSTNQIPM----LIRRKETKDYGTK-------------RLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEG 143
Cdd:COG1040 103 LARALARALGIPVlpdlLRRVRATPSQAGLsraerrrnlrgafAVRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAG 182


                ....*....
gi 4507835  144 LKVTDAIVL 152
Cdd:COG1040 183 AARVDVLVL 191
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 113-179 5.79e-03

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 37.84  E-value: 5.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507835   113 INPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTD-AIVLLDREQGGKDKLQAHGIRLHSVCTLSKM 179
Cdd:PRK09219 114 LSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGiGIVIEKSFQDGRKLLEEKGYRVESLARIASL 181
 
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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