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Conserved domains on  [gi|90111088|ref|NP_414667|]
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hypoxanthine phosphoribosyltransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

type I phosphoribosyltransferase; uracil phosphoribosyltransferase( domain architecture ID 10794158)

type I phosphoribosyltransferase similar to phosphoribosyltransferases with specificities for hypoxanthine, guanine, and/or xanthine| uracil phosphoribosyltransferase catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 1-178 7.58e-118

hypoxanthine phosphoribosyltransferase; Provisional


:

Pssm-ID: 185321  Cd Length: 178  Bit Score: 330.83  E-value: 7.58e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:PRK15423   1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160

                        170
                 ....*....|....*...
gi 90111088  161 AQRYRHLPYIGKVILLDE 178
Cdd:PRK15423 161 AQRYRHLPYIGKVILLDE 178
 
Name Accession Description Interval E-value
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 1-178 7.58e-118

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 330.83  E-value: 7.58e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:PRK15423   1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160

                        170
                 ....*....|....*...
gi 90111088  161 AQRYRHLPYIGKVILLDE 178
Cdd:PRK15423 161 AQRYRHLPYIGKVILLDE 178
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 1-173 7.16e-98

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440399  Cd Length: 176  Bit Score: 280.37  E-value: 7.16e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   1 MKHTVEVMIPEAEIKARIAELGRQITERYKdsGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:COG0634   2 HDDIAEVLISEEEIQARVKELAAQITADYA--GKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:COG0634  80 RILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDY 159

                       170
                ....*....|...
gi 90111088 161 AQRYRHLPYIGKV 173
Cdd:COG0634 160 AEYYRNLPYIYAL 172
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 7-173 4.32e-93

hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine phosphoribosyltransferase. Sequence differences as small as a single residue can affect whether members of this family act on hypoxanthine and guanine or hypoxanthine only. The designation of this model as equivalog reflects hypoxanthine specificity and does not reflect whether or not guanine can replace hypoxanthine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273497  Cd Length: 166  Bit Score: 267.96  E-value: 4.32e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088     7 VMIPEAEIKARIAELGRQITERYKdsGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKDL 86
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYA--GKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    87 DEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYRH 166
Cdd:TIGR01203  79 DLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRN 158


                  ....*..
gi 90111088   167 LPYIGKV 173
Cdd:TIGR01203 159 LPYIGVL 165
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-136 1.12e-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: 82.44  E-value: 1.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088  18 IAELGRQITERYKDsgsDMVLVGLLRGSFMFMADLCREVQVshEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLI 97
Cdd:cd06223   2 GRLLAEEIREDLLE---PDVVVGILRGGLPLAAALARALGL--PLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLL 76

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 90111088  98 VEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRRE 136
Cdd:cd06223  77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA 115
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 13-160 2.23e-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: 79.72  E-value: 2.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    13 EIKARIAELGRQITEryKDSGSDMVLVGLLRGSFMFMADLCREVQVshEVDFMTASSYGSGMSTtrdVKILKDLDEDIRG 92
Cdd:pfam00156  10 AILKAVARLAAQINE--DYGGKPDVVVGILRGGLPFAGILARRLDV--PLAFVRKVSYNPDTSE---VMKTSSALPDLKG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    93 KDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREvnvPVEFIGFSIPD--EFVVGYGIDY 160
Cdd:pfam00156  83 KTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTE---PKDKYDKRVDDwiVFVVGFGLDE 149
 
Name Accession Description Interval E-value
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 1-178 7.58e-118

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 330.83  E-value: 7.58e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:PRK15423   1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160

                        170
                 ....*....|....*...
gi 90111088  161 AQRYRHLPYIGKVILLDE 178
Cdd:PRK15423 161 AQRYRHLPYIGKVILLDE 178
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 1-173 7.16e-98

Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440399  Cd Length: 176  Bit Score: 280.37  E-value: 7.16e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   1 MKHTVEVMIPEAEIKARIAELGRQITERYKdsGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:COG0634   2 HDDIAEVLISEEEIQARVKELAAQITADYA--GKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:COG0634  80 RILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDY 159

                       170
                ....*....|...
gi 90111088 161 AQRYRHLPYIGKV 173
Cdd:COG0634 160 AEYYRNLPYIYAL 172
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 7-173 4.32e-93

hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine phosphoribosyltransferase. Sequence differences as small as a single residue can affect whether members of this family act on hypoxanthine and guanine or hypoxanthine only. The designation of this model as equivalog reflects hypoxanthine specificity and does not reflect whether or not guanine can replace hypoxanthine. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273497  Cd Length: 166  Bit Score: 267.96  E-value: 4.32e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088     7 VMIPEAEIKARIAELGRQITERYKdsGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKDL 86
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYA--GKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    87 DEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYRH 166
Cdd:TIGR01203  79 DLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRN 158


                  ....*..
gi 90111088   167 LPYIGKV 173
Cdd:TIGR01203 159 LPYIGVL 165
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 2-171 3.67e-60

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 185.24  E-value: 3.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    2 KHTVEVMIPEAEIKARIAELGRQITERYkdSGSDMVLVGLLRGSFMFMADLCREVQVSH---EVDFMTASSYGSGMSTTR 78
Cdd:PLN02238   5 VDIEKVLWTAEDISARVAELAAQIASDY--AGKSPVVLGVATGAFMFLADLVRAIQPLPrglTVDFIRASSYGGGTESSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   79 DVKI-LKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPV-----EFIGFSIPDEF 152
Cdd:PLN02238  83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYELvgdgkEYVGFECPDEF 162

                        170
                 ....*....|....*....
gi 90111088  153 VVGYGIDYAQRYRHLPYIG 171
Cdd:PLN02238 163 VVGYGLDFAEKYRNLPYVG 181
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 4-167 1.22e-36

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 125.91  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    4 TVEVMIPEAEIKARIAELGRQITERYKD----SGSDMVLVGLLRGSFMFMADLCR---EVQVSHEVDFMTASSYGSGMST 76
Cdd:PTZ00271  23 SAHTLVTQEQVWAATAKCAKKIAEDYRSfkltTENPLYLLCVLKGSFIFTADLARflaDEGVPVKVEFICASSYGTGVET 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   77 TRDVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGY 156
Cdd:PTZ00271 103 SGQVRMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGY 182

                        170
                 ....*....|.
gi 90111088  157 GIDYAQRYRHL 167
Cdd:PTZ00271 183 GMDYAESYREL 193
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 7-178 3.87e-33

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 117.95  E-value: 3.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    7 VMIPEAEIKARIAELGRQITERYKDSgsDMVLVGLLRGSFMFMADLCREVQVSHEV------------DFMTASSYGSGM 74
Cdd:PTZ00149  56 ILLPNGLIKDRVEKLAYDIKQVYGNE--ELHILCILKGSRGFFSALVDYLNRIHNYsstespkppyqeHYVRVKSYCNDE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   75 STTRdVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVV 154
Cdd:PTZ00149 134 STGK-LEIVSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPDHFVV 212

                        170       180
                 ....*....|....*....|....
gi 90111088  155 GYGIDYAQRYRHLPYIgkVILLDE 178
Cdd:PTZ00149 213 GYCLDYNEHFRDLDHV--AVLNDE 234
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 6-170 1.80e-24

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 93.77  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    6 EVMIPEAEIKARIAELGRQITERYKDSGSdmVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKD 85
Cdd:PRK09162  14 DCLVSAAEVEAAIDRMADEITADLADENP--LVLCVMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNETTGGELVWKVKP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   86 lDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREV-NVPVEFIGFSIPDEFVVGYGIDYAQRY 164
Cdd:PRK09162  92 -RESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAkPLKADFVGLEVPDRYVFGYGMDYKGYW 170


                 ....*.
gi 90111088  165 RHLPYI 170
Cdd:PRK09162 171 RNLPGI 176
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-136 1.12e-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: 82.44  E-value: 1.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088  18 IAELGRQITERYKDsgsDMVLVGLLRGSFMFMADLCREVQVshEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLI 97
Cdd:cd06223   2 GRLLAEEIREDLLE---PDVVVGILRGGLPLAAALARALGL--PLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLL 76

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 90111088  98 VEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRRE 136
Cdd:cd06223  77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA 115
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 13-160 2.23e-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: 79.72  E-value: 2.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    13 EIKARIAELGRQITEryKDSGSDMVLVGLLRGSFMFMADLCREVQVshEVDFMTASSYGSGMSTtrdVKILKDLDEDIRG 92
Cdd:pfam00156  10 AILKAVARLAAQINE--DYGGKPDVVVGILRGGLPFAGILARRLDV--PLAFVRKVSYNPDTSE---VMKTSSALPDLKG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088    93 KDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREvnvPVEFIGFSIPD--EFVVGYGIDY 160
Cdd:pfam00156  83 KTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTE---PKDKYDKRVDDwiVFVVGFGLDE 149
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 18-135 1.91e-18

Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 441837 [Multi-domain]  Cd Length: 153  Bit Score: 77.19  E-value: 1.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088  18 IAELGRQITERYKDSGS--DMVlVGLLRGSfMFMAD-LCREVQVsHEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKD 94
Cdd:COG2236  14 IHELSRRLAEQILESGFrpDVI-VAIARGG-LVPARiLADALGV-PDLASIRVSSYTGTAKRLEEPVVKGPLDEDLAGKR 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 90111088  95 VLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRR 135
Cdd:COG2236  91 VLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSK 131
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 23-136 3.30e-08

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 50.25  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   23 RQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHeVDFMTASSYGSgmSTTRDVKILKDLDEDirGKDVLIVEDII 102
Cdd:PRK09177  20 RALAWRLLPAGQWKGIIAVTRGGLVPAAILARELGIRL-VDTVCISSYDH--DNQGELKVLKRAEGD--GEGFLVVDDLV 94

                         90       100       110
                 ....*....|....*....|....*....|....
gi 90111088  103 DSGNTLSKVREILslrePKSLaICTLLDKPSRRE 136
Cdd:PRK09177  95 DTGGTARAVREMY----PKAH-FATVYAKPAGRP 123
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
89-170 9.52e-06

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 44.34  E-value: 9.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111088   89 DIRGKDVLIVEDIIDSGNTLSKVREILSLREPKS-LAICT--LLDKPSrrevnvpVEFIGFSIPDEFVVGYGIDYAQRYR 165
Cdd:PRK01259 205 DVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSvYAYAThpVLSGGA-------IERIENSVIDELVVTDSIPLSEEAK 277


                 ....*
gi 90111088  166 HLPYI 170
Cdd:PRK01259 278 KCDKI 282
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 89-142 1.01e-05

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 44.09  E-value: 1.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 90111088   89 DIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREV-NVPVE 142
Cdd:PRK02277 137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDKSGIDEIdGVPVY 191
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 84-115 2.67e-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: 40.34  E-value: 2.67e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 90111088    84 KDLDEDIRGKDVLIVEDIIDSGNTLSKVREIL 115
Cdd:TIGR01251 202 MNLVGDVEGKDVVIVDDIIDTGGTIAKAAEIL 233
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 86-127 2.34e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 37.62  E-value: 2.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 90111088   86 LDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICT 127
Cdd:PRK06827 258 LGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAA 299
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 78-115 3.69e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 36.81  E-value: 3.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 90111088   78 RDVKIlKDLDEDIRGKDVLIVEDIIDSGNTLSKVREIL 115
Cdd:PRK00934 191 TEVEI-APKNLDVKGKDVLIVDDIISTGGTMATAIKIL 227
 
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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