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Conserved domains on  [gi|4502171|ref|NP_000476|]
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adenine phosphoribosyltransferase isoform a [Homo sapiens]

Protein Classification

adenine phosphoribosyltransferase( domain architecture ID 10795679)

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
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 9-179 1.10e-92

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: 266.84  E-value: 1.10e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171      9 VEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHggrIDYIAGLDSRGFLFGPSLAQELGLGCVLIRK 88
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDAN---IDYIVGPEARGFIFGAALAYKLGVGFVPVRK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     89 RGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKL 168
Cdd:TIGR01090  78 PGKLPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKL 157

                         170
                  ....*....|..
gi 4502171    169 AP-VPFFSLLQY 179
Cdd:TIGR01090 158 EPnVPVFSLLEY 169
 
Name Accession Description Interval E-value
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 9-179 1.10e-92

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: 266.84  E-value: 1.10e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171      9 VEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHggrIDYIAGLDSRGFLFGPSLAQELGLGCVLIRK 88
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDAN---IDYIVGPEARGFIFGAALAYKLGVGFVPVRK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     89 RGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKL 168
Cdd:TIGR01090  78 PGKLPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKL 157

                         170
                  ....*....|..
gi 4502171    169 AP-VPFFSLLQY 179
Cdd:TIGR01090 158 EPnVPVFSLLEY 169
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 6-180 1.76e-87

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 253.85  E-value: 1.76e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     6 LQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKathGGRIDYIAGLDSRGFLFGPSLAQELGLGCVL 85
Cdd:PRK02304   3 LEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYK---DADIDKIVGIEARGFIFGAALAYKLGIGFVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    86 IRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGR 165
Cdd:PRK02304  80 VRKPGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGR 159

                        170
                 ....*....|....*
gi 4502171   166 EKLAPVPFFSLLQYE 180
Cdd:PRK02304 160 EKLEGYPVKSLVKFD 174
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 7-179 1.17e-75

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: 223.80  E-value: 1.17e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    7 QLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKathGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLI 86
Cdd:COG0503   1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFA---DKGIDKVVGIEARGFILAAALAYALGVPFVPA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171   87 RKRGKLPGPTLWASYSLEYGK-AELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGR 165
Cdd:COG0503  78 RKPGKLPGETVSEEYDLEYGTgDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGR 157

                       170
                ....*....|....
gi 4502171  166 EKLAPVPFFSLLQY 179
Cdd:COG0503 158 EKLRDYPVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 42-177 6.02e-28

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: 101.32  E-value: 6.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171   42 AIGLLARHLKAtHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYsleygkaELEIQKDALEPGQ 121
Cdd:cd06223   1 AGRLLAEEIRE-DLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY-------GLELPLGGDVKGK 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4502171  122 RVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAP-VPFFSLL 177
Cdd:cd06223  73 RVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPgDPVYSLF 129
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 32-158 4.28e-19

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: 78.95  E-value: 4.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     32 VLKDPASFRAAIGLLARHLKaTHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYsleygkaele 111
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINE-DYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT---------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 4502171    112 IQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVE 158
Cdd:pfam00156  74 SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
58-158 3.61e-11

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 58.78  E-value: 3.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    58 IDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRG-KLPGpTLWASYSLEYGKAELEIqkDALEPGQRVVVVDDLLATGGTM 136
Cdd:NF040646  54 VDKIVTVEAMGIPIATALSLKTDIPLVIIRKRKyGLPG-EVEVHQSTGYSKGELYI--NGINKGDRVLIVDDVISTGGTL 130

                         90       100
                 ....*....|....*....|..
gi 4502171   137 NAACELLGRLQAEVLECVSLVE 158
Cdd:NF040646 131 IAVIKALEKAGAEIKDVVVVIE 152
 
Name Accession Description Interval E-value
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 9-179 1.10e-92

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: 266.84  E-value: 1.10e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171      9 VEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHggrIDYIAGLDSRGFLFGPSLAQELGLGCVLIRK 88
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDAN---IDYIVGPEARGFIFGAALAYKLGVGFVPVRK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     89 RGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKL 168
Cdd:TIGR01090  78 PGKLPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKL 157

                         170
                  ....*....|..
gi 4502171    169 AP-VPFFSLLQY 179
Cdd:TIGR01090 158 EPnVPVFSLLEY 169
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 6-180 1.76e-87

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 253.85  E-value: 1.76e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     6 LQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKathGGRIDYIAGLDSRGFLFGPSLAQELGLGCVL 85
Cdd:PRK02304   3 LEDLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYK---DADIDKIVGIEARGFIFGAALAYKLGIGFVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    86 IRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGR 165
Cdd:PRK02304  80 VRKPGKLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGR 159

                        170
                 ....*....|....*
gi 4502171   166 EKLAPVPFFSLLQYE 180
Cdd:PRK02304 160 EKLEGYPVKSLVKFD 174
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 7-179 1.17e-75

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: 223.80  E-value: 1.17e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    7 QLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKathGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLI 86
Cdd:COG0503   1 EDLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFA---DKGIDKVVGIEARGFILAAALAYALGVPFVPA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171   87 RKRGKLPGPTLWASYSLEYGK-AELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGR 165
Cdd:COG0503  78 RKPGKLPGETVSEEYDLEYGTgDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGR 157

                       170
                ....*....|....
gi 4502171  166 EKLAPVPFFSLLQY 179
Cdd:COG0503 158 EKLRDYPVESLLTL 171
PLN02293 PLN02293
adenine phosphoribosyltransferase
 2-180 3.94e-61

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 187.57  E-value: 3.94e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     2 ADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKathGGRIDYIAGLDSRGFLFGPSLAQELGL 81
Cdd:PLN02293  10 GDPRLQGISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYR---DMGISVVAGIEARGFIFGPPIALAIGA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    82 GCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTS 161
Cdd:PLN02293  87 KFVPLRKPGKLPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPE 166

                        170
                 ....*....|....*....
gi 4502171   162 LKGREKLAPVPFFSLLQYE 180
Cdd:PLN02293 167 LKGREKLNGKPLFVLVESR 185
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 42-177 6.02e-28

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: 101.32  E-value: 6.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171   42 AIGLLARHLKAtHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYsleygkaELEIQKDALEPGQ 121
Cdd:cd06223   1 AGRLLAEEIRE-DLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPY-------GLELPLGGDVKGK 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4502171  122 RVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAP-VPFFSLL 177
Cdd:cd06223  73 RVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPgDPVYSLF 129
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 9-168 1.50e-23

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 91.77  E-value: 1.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     9 VEQRIRSFPDFPTPGVV--FRDISPVLKdPASFRAAIGLLARHLKAthggRIDYIAGLDSRGFLFGPSLAQelgLGCVLI 86
Cdd:PRK12560   6 LYKNARVVNSGKALTTVneFTDQLPALR-PKVLKETAKEIIKYIDK----DIDKIVTEEDKGAPLATPVSL---LSGKPL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    87 RKRGKLPGPTLWASYS-LEYGKAELE--IQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLK 163
Cdd:PRK12560  78 AMARWYPYSLSELNYNvVEIGSEYFEgvVYLNGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNN 157


                 ....*
gi 4502171   164 GREKL 168
Cdd:PRK12560 158 GRKKL 162
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 32-158 4.28e-19

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: 78.95  E-value: 4.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     32 VLKDPASFRAAIGLLARHLKaTHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYsleygkaele 111
Cdd:pfam00156   5 ILDNPAILKAVARLAAQINE-DYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKT---------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 4502171    112 IQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVE 158
Cdd:pfam00156  74 SSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLID 120
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 28-180 1.49e-14

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 68.26  E-value: 1.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171   28 DISPVLKDPASFRAAIGLLARHLKAtHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKlpgptlwasyslEYGK 107
Cdd:COG0461  35 DCRLVLSYPEALELLGEALAELIKE-LGPEFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAK------------DHGT 101

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4502171  108 -AELEiqkDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSlKGREKLAP--VPFFSLLQYE 180
Cdd:COG0461 102 gGQIE---GGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE-GAAENLEEagVPLHSLLTLD 173
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 31-180 6.66e-12

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 61.33  E-value: 6.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    31 PVLKDPASFRAAIGLLARHLKAtHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKlpgptlwasyslEYGK-AE 109
Cdd:PRK00455  39 KLLSYPEALALLGRFLAEAIKD-SGIEFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK------------DHGEgGQ 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4502171   110 LEIqkdALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVE-LTSLKGREKLAPVPFFSLLQYE 180
Cdd:PRK00455 106 IEG---RRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDrQSAAQEVFADAGVPLISLITLD 174
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
58-158 3.61e-11

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 58.78  E-value: 3.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    58 IDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRG-KLPGpTLWASYSLEYGKAELEIqkDALEPGQRVVVVDDLLATGGTM 136
Cdd:NF040646  54 VDKIVTVEAMGIPIATALSLKTDIPLVIIRKRKyGLPG-EVEVHQSTGYSKGELYI--NGINKGDRVLIVDDVISTGGTL 130

                         90       100
                 ....*....|....*....|..
gi 4502171   137 NAACELLGRLQAEVLECVSLVE 158
Cdd:NF040646 131 IAVIKALEKAGAEIKDVVVVIE 152
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 116-179 3.15e-07

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: 47.81  E-value: 3.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502171    116 ALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLV---ELTSLKGREKLAPVPFFSLLQY 179
Cdd:TIGR00336 104 ELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVdrqERSAGQEFEKEYGLPVISLITL 170
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 13-150 2.66e-06

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 45.35  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    13 IRSFPDFPTPGVVFrdispvLKDPASFRAAIGLLARHLKAthggRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGK- 91
Cdd:PRK07322  18 IRVGPDLAIALFVI------LGDTELTEAAAEALAKRLPT----EVDVLVTPETKGIPLAHALSRRLGKPYVVARKSRKp 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4502171    92 -LPGPTLWASYSLEYGKAELEI--QKDA-LEPGQRVVVVDDLLATGGTMNAACELLGRLQAEV 150
Cdd:PRK07322  88 yMQDPIIQEVVSITTGKPQLLVldGADAeKLKGKRVAIVDDVVSTGGTLTALERLVERAGGQV 150
purR_Bsub TIGR01743
pur operon repressor, Bacillus subtilis type; This model represents the puring operon ...
 58-150 9.44e-06

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: 44.39  E-value: 9.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     58 IDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLP-GPTLWASY-SLEYGKAE-LEIQKDALEPGQRVVVVDDLLATGG 134
Cdd:TIGR01743 129 IDAVMTVATKGIPLAYAVASVLNVPLVIVRKDSKVTeGSTVSINYvSGSSNRIQtMSLAKRSLKTGSKVLIIDDFMKAGG 208

                          90
                  ....*....|....*.
gi 4502171    135 TMNAACELLGRLQAEV 150
Cdd:TIGR01743 209 TINGMINLLDEFDAEV 224
pyrE_Therm TIGR01367
orotate phosphoribosyltransferase, Thermus family; This model represents a distinct clade of ...
 32-180 5.78e-05

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: 41.70  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     32 VLKDPASFRAAIGLLARHLKAThGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKlpGPTLWASYsleygkaele 111
Cdd:TIGR01367  34 LLEHPEALMELGGELAQKILDY-GLKVDFIVGPAMGGVILGYEVARQLSVRSIFAEREGG--GMKLRRGF---------- 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4502171    112 iqkdALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTslKGREKLAPVPFFSLLQYE 180
Cdd:TIGR01367 101 ----AVKPGEKFVAVEDVVTTGGSLLEAIRAIEGQGGQVVGLACIIDRS--QGGKPDSGVPLMSLKELE 163
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 120-157 7.36e-05

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 41.61  E-value: 7.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 4502171   120 GQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLV 157
Cdd:PRK00129 124 ERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCLV 161
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 7-176 8.88e-05

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 41.31  E-value: 8.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     7 QLVEQRIRSfpdfptPGVVFRDisPVLK---------DPASFRAaIG-LLARHLKATHggrIDYIAGLDSRGFlfGPSL- 75
Cdd:PRK09219   2 KLLEERILK------DGKVLSG--NILKvdsflnhqvDPKLMNE-IGkEFARRFKDEG---ITKILTIEASGI--APAVm 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    76 -AQELGLGCVLIRKRGK--LPGPTLWAS-YSLEYGKA-ELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEV 150
Cdd:PRK09219  68 aALALGVPVVFAKKKKSltLTDDVYTATvYSFTKQVTsTVSVSKKFLSEGDRVLIIDDFLANGQAALGLIDIIEQAGAKV 147

                        170       180
                 ....*....|....*....|....*...
gi 4502171   151 LECVSLVELTSLKGREKL--APVPFFSL 176
Cdd:PRK09219 148 AGIGIVIEKSFQDGRKLLeeKGYRVESL 175
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 9-180 1.65e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 40.75  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171     9 VEQRIRsFPDFptpGVVfrDISPVLKDPASFRaaigLLARHLKATHGG-RIDYIAGLDSRGFLFGPSLAQELGLGCVlIR 87
Cdd:PRK08558  72 VKARIK-VDDE---GYV--DNSSVVFDPSFLR----LIAPVVAERFMGlRVDVVLTAATDGIPLAVAIASYFGADLV-YA 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    88 KRGKLPG-PTLWASY-SLEYG-KAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVEL--TSL 162
Cdd:PRK08558 141 KKSKETGvEKFYEEYqRLASGiEVTLYLPASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVgeVGI 220

                        170
                 ....*....|....*...
gi 4502171   163 KGREKLAPVPFFSLLQYE 180
Cdd:PRK08558 221 DRAREETDAPVDALYTLE 238
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
120-149 3.34e-04

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 39.67  E-value: 3.34e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 4502171  120 GQRVVVVDDLLATGGTMNAACELLGRLQAE 149
Cdd:COG1926 121 GRTVILVDDGIATGATMRAALRALRRQGPA 150
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 74-149 8.02e-04

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: 38.80  E-value: 8.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4502171     74 SLAQELGLGCVLIRKRGKlpgptlwasysleygKAELEIQKDALE---PGQRVVVVDDLLATGGTMNAACELLGRLQAE 149
Cdd:TIGR01251 176 KVADALGCPLAIIDKRRI---------------SATNEVEVMNLVgdvEGKDVVIVDDIIDTGGTIAKAAEILKSAGAK 239
PLN02541 PLN02541
uracil phosphoribosyltransferase
 115-143 1.22e-03

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 38.23  E-value: 1.22e-03
                         10        20
                 ....*....|....*....|....*....
gi 4502171   115 DALEPGQRVVVVDDLLATGGTMNAACELL 143
Cdd:PLN02541 152 DKFPEGSRVLVVDPMLATGGTIVAAIDEL 180
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 120-178 1.26e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 37.93  E-value: 1.26e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4502171   120 GQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVeltSLKGREKLAPVPFFSLLQ 178
Cdd:PRK02277 140 GKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLI---DKSGIDEIDGVPVYSLIR 195
PRK06031 PRK06031
phosphoribosyltransferase; Provisional
 37-169 2.08e-03

phosphoribosyltransferase; Provisional


Pssm-ID: 235678  Cd Length: 233  Bit Score: 37.43  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502171    37 ASFrAAIGLLARHLKATHGG-RIDYIAGLDSRGFLFGPSLAQELG------LGCVliRK---RGKLPGPTlwasYSLEYG 106
Cdd:PRK06031  64 ASF-EVLDALAEHLAEKARAfDPDVVAGLPTLGLTLAAAVARKLGhtryvpLGTS--RKfwyRDELSVPL----SSITTP 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502171   107 KAELEIQKD----ALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLeCVSLVELTSLKGREKLA 169
Cdd:PRK06031 137 DQGKRLYIDprmlPLLEGRRVALIDDVISSGASIVAGLRLLAACGIEPA-GIGAAMLQSERWRESLA 202
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 120-143 3.33e-03

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: 36.96  E-value: 3.33e-03
                        10        20
                ....*....|....*....|....
gi 4502171  120 GQRVVVVDDLLATGGTMNAACELL 143
Cdd:COG0462 211 GKTCIIVDDMIDTGGTLVEAAEAL 234
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 120-149 4.25e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 36.81  E-value: 4.25e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 4502171   120 GQRVVVVDDLLATGGTMNAACELLGRLQAE 149
Cdd:PRK00934 204 GKDVLIVDDIISTGGTMATAIKILKEQGAK 233
 
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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