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Conserved domains on  [gi|15220047|ref|NP_178122|]
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adenine phosphoribosyl transferase 2 [Arabidopsis thaliana]

Protein Classification

adenine phosphoribosyltransferase( domain architecture ID 10791313)

adenine phosphoribosyltransferase catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02293 PLN02293
adenine phosphoribosyltransferase
 1-187 6.11e-127

adenine phosphoribosyltransferase


:

Pssm-ID: 177930  Cd Length: 187  Bit Score: 354.75  E-value: 6.11e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    1 MFAVENGLQGDPRLKAISDAIRVIPHFPKTGIMFQDITTLLLDPVAFKHVVDIFVDRYKHMNISLVAGVEARGFIFGPPI 80
Cdd:PLN02293   1 MFAMENGDQGDPRLQGISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   81 ALAIGAKFVPLRKPGKLPGRVISEEYELEYGRDCLEMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECAC 160
Cdd:PLN02293  81 ALAIGAKFVPLRKPGKLPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECAC 160

                        170       180
                 ....*....|....*....|....*..
gi 15220047  161 VVGLPKFKGQCKLKGKPLYVLVEPNQF 187
Cdd:PLN02293 161 VIELPELKGREKLNGKPLFVLVESRGI 187
 
Name Accession Description Interval E-value
PLN02293 PLN02293
adenine phosphoribosyltransferase
 1-187 6.11e-127

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 354.75  E-value: 6.11e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    1 MFAVENGLQGDPRLKAISDAIRVIPHFPKTGIMFQDITTLLLDPVAFKHVVDIFVDRYKHMNISLVAGVEARGFIFGPPI 80
Cdd:PLN02293   1 MFAMENGDQGDPRLQGISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   81 ALAIGAKFVPLRKPGKLPGRVISEEYELEYGRDCLEMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECAC 160
Cdd:PLN02293  81 ALAIGAKFVPLRKPGKLPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECAC 160

                        170       180
                 ....*....|....*....|....*..
gi 15220047  161 VVGLPKFKGQCKLKGKPLYVLVEPNQF 187
Cdd:PLN02293 161 VIELPELKGREKLNGKPLFVLVESRGI 187
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 15-183 1.22e-70

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: 211.86  E-value: 1.22e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047  15 KAISDAIRVIPHFPKTGIMFQDITTLLLDPVAFKHVVDIFVDRYKHMNISLVAGVEARGFIFGPPIALAIGAKFVPLRKP 94
Cdd:COG0503   1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047  95 GKLPGRVISEEYELEYG-RDCLEMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVVGLPKFKGQCKL 173
Cdd:COG0503  81 GKLPGETVSEEYDLEYGtGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL 160

                       170
                ....*....|
gi 15220047 174 KGKPLYVLVE 183
Cdd:COG0503 161 RDYPVESLLT 170
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 19-183 3.10e-70

adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273437  Cd Length: 169  Bit Score: 210.60  E-value: 3.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    19 DAIRVIPHFPKTGIMFQDITTLLLDPVAFKHVVDIFVDRYKHMNISLVAGVEARGFIFGPPIALAIGAKFVPLRKPGKLP 98
Cdd:TIGR01090   3 QAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGKLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    99 GRVISEEYELEYGRDCLEMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVVGLPKFKGQCKLKGK-P 177
Cdd:TIGR01090  83 GETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPNvP 162


                  ....*.
gi 15220047   178 LYVLVE 183
Cdd:TIGR01090 163 VFSLLE 168
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 50-183 2.23e-23

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: 90.15  E-value: 2.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047  50 VVDIFVDRYKHM--NISLVAGVEARGFIFGPPIALAIGAKFVPLRKPGKLPGRVISEEYELEygrdcleMSVEAVKSEER 127
Cdd:cd06223   1 AGRLLAEEIREDllEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLE-------LPLGGDVKGKR 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15220047 128 ALIIDDLVATGGTLSASINLLERAGAEVVECACVVGLPKFKG-QCKLKGKPLYVLVE 183
Cdd:cd06223  74 VLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGArELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 36-162 7.78e-11

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: 57.76  E-value: 7.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    36 DITTLLLDPVAFKHVVDIFVDRYKHMNIS--LVAGVEARGFIFGPPIALAIGAKFVPLRKPGKLPGRVISEEYeleygrd 113
Cdd:pfam00156   1 SVDEILDNPAILKAVARLAAQINEDYGGKpdVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15220047   114 cleMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVV 162
Cdd:pfam00156  74 ---SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLI 119
 
Name Accession Description Interval E-value
PLN02293 PLN02293
adenine phosphoribosyltransferase
 1-187 6.11e-127

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 354.75  E-value: 6.11e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    1 MFAVENGLQGDPRLKAISDAIRVIPHFPKTGIMFQDITTLLLDPVAFKHVVDIFVDRYKHMNISLVAGVEARGFIFGPPI 80
Cdd:PLN02293   1 MFAMENGDQGDPRLQGISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   81 ALAIGAKFVPLRKPGKLPGRVISEEYELEYGRDCLEMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECAC 160
Cdd:PLN02293  81 ALAIGAKFVPLRKPGKLPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECAC 160

                        170       180
                 ....*....|....*....|....*..
gi 15220047  161 VVGLPKFKGQCKLKGKPLYVLVEPNQF 187
Cdd:PLN02293 161 VIELPELKGREKLNGKPLFVLVESRGI 187
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 14-183 3.49e-79

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 233.43  E-value: 3.49e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   14 LKAISDAIRVIPHFPKTGIMFQDITTLLLDPVAFKHVVDIFVDRYKHMNISLVAGVEARGFIFGPPIALAIGAKFVPLRK 93
Cdd:PRK02304   3 LEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   94 PGKLPGRVISEEYELEYGRDCLEMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVVGLPKFKGQCKL 173
Cdd:PRK02304  83 PGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKL 162

                        170
                 ....*....|
gi 15220047  174 KGKPLYVLVE 183
Cdd:PRK02304 163 EGYPVKSLVK 172
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 15-183 1.22e-70

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: 211.86  E-value: 1.22e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047  15 KAISDAIRVIPHFPKTGIMFQDITTLLLDPVAFKHVVDIFVDRYKHMNISLVAGVEARGFIFGPPIALAIGAKFVPLRKP 94
Cdd:COG0503   1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047  95 GKLPGRVISEEYELEYG-RDCLEMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVVGLPKFKGQCKL 173
Cdd:COG0503  81 GKLPGETVSEEYDLEYGtGDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKL 160

                       170
                ....*....|
gi 15220047 174 KGKPLYVLVE 183
Cdd:COG0503 161 RDYPVESLLT 170
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 19-183 3.10e-70

adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273437  Cd Length: 169  Bit Score: 210.60  E-value: 3.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    19 DAIRVIPHFPKTGIMFQDITTLLLDPVAFKHVVDIFVDRYKHMNISLVAGVEARGFIFGPPIALAIGAKFVPLRKPGKLP 98
Cdd:TIGR01090   3 QAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGKLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    99 GRVISEEYELEYGRDCLEMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVVGLPKFKGQCKLKGK-P 177
Cdd:TIGR01090  83 GETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPNvP 162


                  ....*.
gi 15220047   178 LYVLVE 183
Cdd:TIGR01090 163 VFSLLE 168
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 14-174 5.92e-28

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 103.33  E-value: 5.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   14 LKAISDAIRVIPHFPKTGIM--FQDITTLLlDPVAFKHVVdIFVDRYKHMNISLVAGVEARGFIFGPPIALaIGakFVPL 91
Cdd:PRK12560   3 LKNLYKNARVVNSGKALTTVneFTDQLPAL-RPKVLKETA-KEIIKYIDKDIDKIVTEEDKGAPLATPVSL-LS--GKPL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   92 RKPGKLPGRVISEEY-ELEYGRDCLEMSV--EAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVVGLPKFK 168
Cdd:PRK12560  78 AMARWYPYSLSELNYnVVEIGSEYFEGVVylNGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNN 157


                 ....*.
gi 15220047  169 GQCKLK 174
Cdd:PRK12560 158 GRKKLF 163
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 50-183 2.23e-23

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: 90.15  E-value: 2.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047  50 VVDIFVDRYKHM--NISLVAGVEARGFIFGPPIALAIGAKFVPLRKPGKLPGRVISEEYELEygrdcleMSVEAVKSEER 127
Cdd:cd06223   1 AGRLLAEEIREDllEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLE-------LPLGGDVKGKR 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15220047 128 ALIIDDLVATGGTLSASINLLERAGAEVVECACVVGLPKFKG-QCKLKGKPLYVLVE 183
Cdd:cd06223  74 VLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGArELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 36-162 7.78e-11

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: 57.76  E-value: 7.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    36 DITTLLLDPVAFKHVVDIFVDRYKHMNIS--LVAGVEARGFIFGPPIALAIGAKFVPLRKPGKLPGRVISEEYeleygrd 113
Cdd:pfam00156   1 SVDEILDNPAILKAVARLAAQINEDYGGKpdVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15220047   114 cleMSVEAVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVV 162
Cdd:pfam00156  74 ---SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLI 119
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 40-162 1.64e-10

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 57.47  E-value: 1.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047  40 LLLDPVAFKHVVDIFVDRYKH--MNISLVAGVEARGFIFGPPIALAIGAKFVPLRKPGKlpgrviseeyelEYGRDCLem 117
Cdd:COG0461  39 VLSYPEALELLGEALAELIKElgPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAK------------DHGTGGQ-- 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15220047 118 sVE-AVKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVV 162
Cdd:COG0461 105 -IEgGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIV 149
purR_Bsub TIGR01743
pur operon repressor, Bacillus subtilis type; This model represents the puring operon ...
 17-156 6.46e-08

pur operon repressor, Bacillus subtilis type; This model represents the puring operon repressor PurR of low-GC Gram-positive bacteria. This homodimeric repressor contains a large region homologous to phosphoribosyltransferases and is inhibited by 5-phosphoribosyl 1-pyrophosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis, Regulatory functions, DNA interactions]


Pssm-ID: 130804 [Multi-domain]  Cd Length: 268  Bit Score: 50.94  E-value: 6.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    17 ISDAIRVIPhfpkTGIMFqdITTLLLDPVAFKHVVDIFVDRYKHMNISLVAGVEARGFifgpPIALA----IGAKFVPLR 92
Cdd:TIGR01743  89 LSEPERILP----GGYLY--LTDILGKPSILSKIGKILASVFAEREIDAVMTVATKGI----PLAYAvasvLNVPLVIVR 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15220047    93 KPGKLP-GRVISEEYELEYGRDCLEMSV--EAVKSEERALIIDDLVATGGTLSASINLLERAGAEVV 156
Cdd:TIGR01743 159 KDSKVTeGSTVSINYVSGSSNRIQTMSLakRSLKTGSKVLIIDDFMKAGGTINGMINLLDEFDAEVA 225
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 42-162 1.75e-07

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 49.01  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   42 LDPVAFKHVVDIFVDRYKHMNISLVAGVEARGfifgppIALAI--GAKF-VPL-----RKPGKLPGRVIS---------E 104
Cdd:PRK09219  30 VDPKLMNEIGKEFARRFKDEGITKILTIEASG------IAPAVmaALALgVPVvfakkKKSLTLTDDVYTatvysftkqV 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15220047  105 EYELEYGRDCLemsveavKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVV 162
Cdd:PRK09219 104 TSTVSVSKKFL-------SEGDRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVI 154
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 127-161 9.22e-06

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 45.05  E-value: 9.22e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 15220047 127 RALIIDDLVATGGTLSASINLLERAGAEVVECACV 161
Cdd:COG0462 213 TCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAAAT 247
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 64-156 1.17e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 44.21  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   64 SLVAGVEARGFIF------------GPPIALAIGAKF---VPLRKPGKLPGrviSEEYELEYGRD------CLEMSVEAV 122
Cdd:PRK08558  97 RLIAPVVAERFMGlrvdvvltaatdGIPLAVAIASYFgadLVYAKKSKETG---VEKFYEEYQRLasgievTLYLPASAL 173

                         90       100       110
                 ....*....|....*....|....*....|....
gi 15220047  123 KSEERALIIDDLVATGGTLSASINLLERAGAEVV 156
Cdd:PRK08558 174 KKGDRVLIVDDIIRSGETQRALLDLARQAGADVV 207
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 100-164 2.28e-05

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 43.75  E-value: 2.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220047  100 RVISEEYELEY--------GRDCLEMSVEAVKSEER-ALIIDDLVATGGTLSASINLLERAGAEVVECACVVGL 164
Cdd:PRK00934 170 KEAAEILGCEYdylektriSPTEVEIAPKNLDVKGKdVLIVDDIISTGGTMATAIKILKEQGAKKVYVACVHPV 243
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 128-164 2.34e-05

ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 43.81  E-value: 2.34e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 15220047   128 ALIIDDLVATGGTLSASINLLERAGAEVVECACVVGL 164
Cdd:TIGR01251 213 VVIVDDIIDTGGTIAKAAEILKSAGAKRVIAAATHGV 249
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 36-162 3.01e-05

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 42.84  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   36 DITTLLLDPVAFKHVVDIFVDRYK--HMNISLVAGVEARGFIFGPPIALAIGAKFVPLRKPGKLPGrvisEEYELEyGRD 113
Cdd:PRK00455  36 DCRKLLSYPEALALLGRFLAEAIKdsGIEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAKDHG----EGGQIE-GRR 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15220047  114 clemsveavKSEERALIIDDLVATGGTLSASINLLERAGAEVVECACVV 162
Cdd:PRK00455 111 ---------LFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIV 150
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 119-156 5.99e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 41.89  E-value: 5.99e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15220047  119 VEAVKSEeRALIIDDLVATGGTLSASINLLERAGAEVV 156
Cdd:PRK07322 115 AEKLKGK-RVAIVDDVVSTGGTLTALERLVERAGGQVV 151
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 129-161 7.72e-05

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 41.73  E-value: 7.72e-05
                        10        20        30
                ....*....|....*....|....*....|...
gi 15220047 129 LIIDDLVATGGTLSASINLLERAGAEVVECACV 161
Cdd:COG1040 159 LLVDDVLTTGATLAEAARALKAAGAARVDVLVL 191
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 124-165 8.54e-05

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 41.61  E-value: 8.54e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15220047  124 SEERALIIDDLVATGGTLSASINLLERAGAEVVECACVVGLP 165
Cdd:PRK00129 123 DERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCLVAAP 164
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 126-182 1.23e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 38.31  E-value: 1.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15220047  126 ERALIIDDLVATGGTLSASINLLERAGAEVVecACVVGLPKfKGQCKLKGKPLYVLV 182
Cdd:PRK02277 141 KRCVIVDDVITSGTTMKETIEYLKEHGGKPV--AVVVLIDK-SGIDEIDGVPVYSLI 194
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 61-156 1.28e-03

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 38.20  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047   61 MNISLVAGVEARGFIFGPPIALAIG-AKFVPLRKPGKLpgrviseeyeleYGRDCLEMSVEAVKSE-------------- 125
Cdd:PRK06031  83 FDPDVVAGLPTLGLTLAAAVARKLGhTRYVPLGTSRKF------------WYRDELSVPLSSITTPdqgkrlyidprmlp 150

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15220047  126 ----ERALIIDDLVATGGTLSASINLLERAGAEVV 156
Cdd:PRK06031 151 llegRRVALIDDVISSGASIVAGLRLLAACGIEPA 185
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
128-161 3.95e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 37.22  E-value: 3.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 15220047  128 ALIIDDLVATGGTLSASINLLERAGAEVVECACV 161
Cdd:PRK07199 214 PVLVDDIVSTGRTLIEAARQLRAAGAASPDCVVV 247
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 75-162 6.31e-03

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: 35.87  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220047    75 IFGP-----PIALAIGAKfvpLRKPGKLPGRVISEEYELEYGRDCLemSVEAVKSEERALIIDDLVATGGTLSASINLLE 149
Cdd:TIGR00336  58 IAGPalggiPIATAVSVK---LAKPGGDIPLCFNRKEAKDHGEGGN--IEGELLEGDKVVVVEDVITTGTSILEAVEIIQ 132

                          90
                  ....*....|...
gi 15220047   150 RAGAEVVECACVV 162
Cdd:TIGR00336 133 AAGGQVAGVIIAV 145
 
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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