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Conserved domains on  [gi|446603345|ref|WP_000680691|]
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hypoxanthine phosphoribosyltransferase [Escherichia coli]

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 9.45e-117

hypoxanthine phosphoribosyltransferase; Provisional


:

Pssm-ID: 185321  Cd Length: 178  Bit Score: 328.13  E-value: 9.45e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   1 MKHIVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:PRK15423   1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
                        170
                 ....*....|....*...
gi 446603345 161 AQRYRHLPYIGKVILLDE 178
Cdd:PRK15423 161 AQRYRHLPYIGKVILLDE 178
 
Name Accession Description Interval E-value
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
1-178 9.45e-117

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 328.13  E-value: 9.45e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   1 MKHIVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:PRK15423   1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
                        170
                 ....*....|....*...
gi 446603345 161 AQRYRHLPYIGKVILLDE 178
Cdd:PRK15423 161 AQRYRHLPYIGKVILLDE 178
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
1-173 6.70e-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: 6.70e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   1 MKHIVEVMIPEAEIKARIAELGRQITERYKdsGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:COG0634    2 HDDIAEVLISEEEIQARVKELAAQITADYA--GKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:COG0634   80 RILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDY 159
                        170
                 ....*....|...
gi 446603345 161 AQRYRHLPYIGKV 173
Cdd:COG0634  160 AEYYRNLPYIYAL 172
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
7-173 1.12e-92

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: 266.80  E-value: 1.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345    7 VMIPEAEIKARIAELGRQITERYKdsGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKDL 86
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYA--GKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   87 DEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYRH 166
Cdd:TIGR01203  79 DLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRN 158

                  ....*..
gi 446603345  167 LPYIGKV 173
Cdd:TIGR01203 159 LPYIGVL 165
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
18-136 1.98e-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: 82.06  E-value: 1.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  18 IAELGRQITERYKDsgsDMVLVGLLRGSFMFMADLCREVQVshEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLI 97
Cdd:cd06223    2 GRLLAEEIREDLLE---PDVVVGILRGGLPLAAALARALGL--PLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLL 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446603345  98 VEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRRE 136
Cdd:cd06223   77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA 115
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
13-160 3.68e-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: 79.33  E-value: 3.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   13 EIKARIAELGRQITEryKDSGSDMVLVGLLRGSFMFMADLCREVQVshEVDFMTASSYGSGMSTtrdVKILKDLDEDIRG 92
Cdd:pfam00156  10 AILKAVARLAAQINE--DYGGKPDVVVGILRGGLPFAGILARRLDV--PLAFVRKVSYNPDTSE---VMKTSSALPDLKG 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   93 KDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREvnvPVEFIGFSIPD--EFVVGYGIDY 160
Cdd:pfam00156  83 KTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTE---PKDKYDKRVDDwiVFVVGFGLDE 149
 
Name Accession Description Interval E-value
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
1-178 9.45e-117

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 328.13  E-value: 9.45e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   1 MKHIVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:PRK15423   1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
                        170
                 ....*....|....*...
gi 446603345 161 AQRYRHLPYIGKVILLDE 178
Cdd:PRK15423 161 AQRYRHLPYIGKVILLDE 178
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
1-173 6.70e-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: 6.70e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   1 MKHIVEVMIPEAEIKARIAELGRQITERYKdsGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:COG0634    2 HDDIAEVLISEEEIQARVKELAAQITADYA--GKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:COG0634   80 RILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDY 159
                        170
                 ....*....|...
gi 446603345 161 AQRYRHLPYIGKV 173
Cdd:COG0634  160 AEYYRNLPYIYAL 172
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
7-173 1.12e-92

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: 266.80  E-value: 1.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345    7 VMIPEAEIKARIAELGRQITERYKdsGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKDL 86
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYA--GKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   87 DEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYRH 166
Cdd:TIGR01203  79 DLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRN 158

                  ....*..
gi 446603345  167 LPYIGKV 173
Cdd:TIGR01203 159 LPYIGVL 165
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
2-171 3.55e-61

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 187.94  E-value: 3.55e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   2 KHIVEVMIPEAEIKARIAELGRQITERYkdSGSDMVLVGLLRGSFMFMADLCREVQVSH---EVDFMTASSYGSGMSTTR 78
Cdd:PLN02238   5 VDIEKVLWTAEDISARVAELAAQIASDY--AGKSPVVLGVATGAFMFLADLVRAIQPLPrglTVDFIRASSYGGGTESSG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  79 DVKI-LKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPV-----EFIGFSIPDEF 152
Cdd:PLN02238  83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYELvgdgkEYVGFECPDEF 162
                        170
                 ....*....|....*....
gi 446603345 153 VVGYGIDYAQRYRHLPYIG 171
Cdd:PLN02238 163 VVGYGLDFAEKYRNLPYVG 181
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
8-167 1.54e-36

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 125.91  E-value: 1.54e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   8 MIPEAEIKARIAELGRQITERYKD----SGSDMVLVGLLRGSFMFMADLCR---EVQVSHEVDFMTASSYGSGMSTTRDV 80
Cdd:PTZ00271  27 LVTQEQVWAATAKCAKKIAEDYRSfkltTENPLYLLCVLKGSFIFTADLARflaDEGVPVKVEFICASSYGTGVETSGQV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160
Cdd:PTZ00271 107 RMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGMDY 186

                 ....*..
gi 446603345 161 AQRYRHL 167
Cdd:PTZ00271 187 AESYREL 193
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
2-178 1.95e-33

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 118.72  E-value: 1.95e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   2 KHIVEVMIPEAEIKARIAELGRQITERYKDSgsDMVLVGLLRGSFMFMADLCREVQVSHEV------------DFMTASS 69
Cdd:PTZ00149  51 NYLTKILLPNGLIKDRVEKLAYDIKQVYGNE--ELHILCILKGSRGFFSALVDYLNRIHNYsstespkppyqeHYVRVKS 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  70 YGSGMSTTRdVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIP 149
Cdd:PTZ00149 129 YCNDESTGK-LEIVSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIP 207
                        170       180
                 ....*....|....*....|....*....
gi 446603345 150 DEFVVGYGIDYAQRYRHLPYIgkVILLDE 178
Cdd:PTZ00149 208 DHFVVGYCLDYNEHFRDLDHV--AVLNDE 234
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
6-170 2.07e-24

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 93.77  E-value: 2.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   6 EVMIPEAEIKARIAELGRQITERYKDSGSdmVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKD 85
Cdd:PRK09162  14 DCLVSAAEVEAAIDRMADEITADLADENP--LVLCVMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNETTGGELVWKVKP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  86 lDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREV-NVPVEFIGFSIPDEFVVGYGIDYAQRY 164
Cdd:PRK09162  92 -RESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAkPLKADFVGLEVPDRYVFGYGMDYKGYW 170

                 ....*.
gi 446603345 165 RHLPYI 170
Cdd:PRK09162 171 RNLPGI 176
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
18-136 1.98e-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: 82.06  E-value: 1.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  18 IAELGRQITERYKDsgsDMVLVGLLRGSFMFMADLCREVQVshEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLI 97
Cdd:cd06223    2 GRLLAEEIREDLLE---PDVVVGILRGGLPLAAALARALGL--PLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLL 76
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446603345  98 VEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRRE 136
Cdd:cd06223   77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA 115
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
13-160 3.68e-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: 79.33  E-value: 3.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   13 EIKARIAELGRQITEryKDSGSDMVLVGLLRGSFMFMADLCREVQVshEVDFMTASSYGSGMSTtrdVKILKDLDEDIRG 92
Cdd:pfam00156  10 AILKAVARLAAQINE--DYGGKPDVVVGILRGGLPFAGILARRLDV--PLAFVRKVSYNPDTSE---VMKTSSALPDLKG 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   93 KDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREvnvPVEFIGFSIPD--EFVVGYGIDY 160
Cdd:pfam00156  83 KTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTE---PKDKYDKRVDDwiVFVVGFGLDE 149
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
1-135 2.01e-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: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345   1 MKHIVEVMIPEAEIKARIAELGRQIteryKDSGS--DMVlVGLLRGSfMFMAD-LCREVQVsHEVDFMTASSYGSGMSTT 77
Cdd:COG2236    1 MDKFKKEYLSWDEIHELSRRLAEQI----LESGFrpDVI-VAIARGG-LVPARiLADALGV-PDLASIRVSSYTGTAKRL 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446603345  78 RDVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRR 135
Cdd:COG2236   74 EEPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSK 131
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
23-136 3.47e-08

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 50.25  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  23 RQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHeVDFMTASSYGSgmSTTRDVKILKDLDEDirGKDVLIVEDII 102
Cdd:PRK09177  20 RALAWRLLPAGQWKGIIAVTRGGLVPAAILARELGIRL-VDTVCISSYDH--DNQGELKVLKRAEGD--GEGFLVVDDLV 94
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446603345 103 DSGNTLSKVREILslrePKSLaICTLLDKPSRRE 136
Cdd:PRK09177  95 DTGGTARAVREMY----PKAH-FATVYAKPAGRP 123
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
89-142 1.04e-05

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 44.09  E-value: 1.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446603345  89 DIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREV-NVPVE 142
Cdd:PRK02277 137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDKSGIDEIdGVPVY 191
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
89-170 1.14e-05

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 44.34  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446603345  89 DIRGKDVLIVEDIIDSGNTLSKVREILSLREPKS-LAICT--LLDKPSrrevnvpVEFIGFSIPDEFVVGYGIDYAQRYR 165
Cdd:PRK01259 205 DVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSvYAYAThpVLSGGA-------IERIENSVIDELVVTDSIPLSEEAK 277

                 ....*
gi 446603345 166 HLPYI 170
Cdd:PRK01259 278 KCDKI 282
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
84-115 2.83e-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: 2.83e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446603345   84 KDLDEDIRGKDVLIVEDIIDSGNTLSKVREIL 115
Cdd:TIGR01251 202 MNLVGDVEGKDVVIVDDIIDTGGTIAKAAEIL 233
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
86-127 2.52e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 37.62  E-value: 2.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446603345  86 LDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICT 127
Cdd:PRK06827 258 LGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAA 299
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
78-115 4.13e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 36.81  E-value: 4.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446603345  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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