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Conserved domains on  [gi|695712009|ref|WP_032644098|]
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MULTISPECIES: hypoxanthine phosphoribosyltransferase [Enterobacter]

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 1.08e-116

hypoxanthine phosphoribosyltransferase; Provisional


:

Pssm-ID: 185321  Cd Length: 178  Bit Score: 328.13  E-value: 1.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   1 MKHTVEVMIPEAEIKARIAELGRQITEHYKDSGSEMVLVGLLRGSFMFMADLCREVHVPHEVDFMTASSYGSGMSTTRDV 80
Cdd:PRK15423   1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSIPDEFVVGYGIDY 160
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160

                        170
                 ....*....|....*...
gi 695712009 161 AQRYRHLPYVGKVVLLDE 178
Cdd:PRK15423 161 AQRYRHLPYIGKVILLDE 178
 
Name Accession Description Interval E-value
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 1-178 1.08e-116

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 328.13  E-value: 1.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   1 MKHTVEVMIPEAEIKARIAELGRQITEHYKDSGSEMVLVGLLRGSFMFMADLCREVHVPHEVDFMTASSYGSGMSTTRDV 80
Cdd:PRK15423   1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSIPDEFVVGYGIDY 160
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160

                        170
                 ....*....|....*...
gi 695712009 161 AQRYRHLPYVGKVVLLDE 178
Cdd:PRK15423 161 AQRYRHLPYIGKVILLDE 178
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 1-174 2.10e-99

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: 284.23  E-value: 2.10e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   1 MKHTVEVMIPEAEIKARIAELGRQITEHYKdsGSEMVLVGLLRGSFMFMADLCREVHVPHEVDFMTASSYGSGMSTTRDV 80
Cdd:COG0634    2 HDDIAEVLISEEEIQARVKELAAQITADYA--GKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSIPDEFVVGYGIDY 160
Cdd:COG0634   80 RILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDY 159

                        170
                 ....*....|....
gi 695712009 161 AQRYRHLPYVGKVV 174
Cdd:COG0634  160 AEYYRNLPYIYALK 173
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 7-174 2.42e-94

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: 271.04  E-value: 2.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009    7 VMIPEAEIKARIAELGRQITEHYKdsGSEMVLVGLLRGSFMFMADLCREVHVPHEVDFMTASSYGSGMSTTRDVKILKDL 86
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYA--GKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   87 DEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSIPDEFVVGYGIDYAQRYRH 166
Cdd:TIGR01203  79 DLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRN 158


                  ....*...
gi 695712009  167 LPYVGKVV 174
Cdd:TIGR01203 159 LPYIGVLE 166
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 21-144 5.08e-22

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 85.91  E-value: 5.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  21 LGRQITEHYKDSGSE-MVLVGLLRGSFMFMADLCREVHVPheVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLIVE 99
Cdd:cd06223    1 AGRLLAEEIREDLLEpDVVVGILRGGLPLAAALARALGLP--LAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLVD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 695712009 100 DIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFV 144
Cdd:cd06223   79 DVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD 123
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 13-160 2.85e-21

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: 84.72  E-value: 2.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   13 EIKARIAELGRQITEHYKdsGSEMVLVGLLRGSFMFMADLCREVHVPheVDFMTASSYGSGMSTtrdVKILKDLDEDIRG 92
Cdd:pfam00156  10 AILKAVARLAAQINEDYG--GKPDVVVGILRGGLPFAGILARRLDVP--LAFVRKVSYNPDTSE---VMKTSSALPDLKG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695712009   93 KDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSiPDEFVVGYGIDY 160
Cdd:pfam00156  83 KTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
 
Name Accession Description Interval E-value
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 1-178 1.08e-116

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 328.13  E-value: 1.08e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   1 MKHTVEVMIPEAEIKARIAELGRQITEHYKDSGSEMVLVGLLRGSFMFMADLCREVHVPHEVDFMTASSYGSGMSTTRDV 80
Cdd:PRK15423   1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSIPDEFVVGYGIDY 160
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160

                        170
                 ....*....|....*...
gi 695712009 161 AQRYRHLPYVGKVVLLDE 178
Cdd:PRK15423 161 AQRYRHLPYIGKVILLDE 178
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 1-174 2.10e-99

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: 284.23  E-value: 2.10e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   1 MKHTVEVMIPEAEIKARIAELGRQITEHYKdsGSEMVLVGLLRGSFMFMADLCREVHVPHEVDFMTASSYGSGMSTTRDV 80
Cdd:COG0634    2 HDDIAEVLISEEEIQARVKELAAQITADYA--GKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSIPDEFVVGYGIDY 160
Cdd:COG0634   80 RILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDY 159

                        170
                 ....*....|....
gi 695712009 161 AQRYRHLPYVGKVV 174
Cdd:COG0634  160 AEYYRNLPYIYALK 173
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 7-174 2.42e-94

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: 271.04  E-value: 2.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009    7 VMIPEAEIKARIAELGRQITEHYKdsGSEMVLVGLLRGSFMFMADLCREVHVPHEVDFMTASSYGSGMSTTRDVKILKDL 86
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYA--GKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   87 DEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSIPDEFVVGYGIDYAQRYRH 166
Cdd:TIGR01203  79 DLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRN 158


                  ....*...
gi 695712009  167 LPYVGKVV 174
Cdd:TIGR01203 159 LPYIGVLE 166
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 2-178 7.20e-62

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 189.48  E-value: 7.20e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   2 KHTVEVMIPEAEIKARIAELGRQITEHYkdSGSEMVLVGLLRGSFMFMADLCREVHV---PHEVDFMTASSYGSGMSTTR 78
Cdd:PLN02238   5 VDIEKVLWTAEDISARVAELAAQIASDY--AGKSPVVLGVATGAFMFLADLVRAIQPlprGLTVDFIRASSYGGGTESSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  79 DVKI-LKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPV-----EFVGFSIPDEF 152
Cdd:PLN02238  83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYELvgdgkEYVGFECPDEF 162

                        170       180
                 ....*....|....*....|....*.
gi 695712009 153 VVGYGIDYAQRYRHLPYVGkvVLLDE 178
Cdd:PLN02238 163 VVGYGLDFAEKYRNLPYVG--VLKPE 186
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 4-167 1.15e-37

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 128.60  E-value: 1.15e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   4 TVEVMIPEAEIKARIAELGRQITEHYKD----SGSEMVLVGLLRGSFMFMADLCR---EVHVPHEVDFMTASSYGSGMST 76
Cdd:PTZ00271  23 SAHTLVTQEQVWAATAKCAKKIAEDYRSfkltTENPLYLLCVLKGSFIFTADLARflaDEGVPVKVEFICASSYGTGVET 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  77 TRDVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSIPDEFVVGY 156
Cdd:PTZ00271 103 SGQVRMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGY 182

                        170
                 ....*....|.
gi 695712009 157 GIDYAQRYRHL 167
Cdd:PTZ00271 183 GMDYAESYREL 193
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 7-178 9.84e-35

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 121.80  E-value: 9.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   7 VMIPEAEIKARIAELGRQITEHYKDSgsEMVLVGLLRGSFMFMADL-----------CREVHV-PHEVDFMTASSYGSGM 74
Cdd:PTZ00149  56 ILLPNGLIKDRVEKLAYDIKQVYGNE--ELHILCILKGSRGFFSALvdylnrihnysSTESPKpPYQEHYVRVKSYCNDE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  75 STTRdVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSIPDEFVV 154
Cdd:PTZ00149 134 STGK-LEIVSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPDHFVV 212

                        170       180
                 ....*....|....*....|....
gi 695712009 155 GYGIDYAQRYRHLPYVgkVVLLDE 178
Cdd:PTZ00149 213 GYCLDYNEHFRDLDHV--AVLNDE 234
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 6-168 6.72e-26

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 97.63  E-value: 6.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   6 EVMIPEAEIKARIAELGRQITEHYKDSGSemVLVGLLRGSFMFMADLCREVHVPHEVDFMTASSYGSGMSTTRDVKILKD 85
Cdd:PRK09162  14 DCLVSAAEVEAAIDRMADEITADLADENP--LVLCVMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNETTGGELVWKVKP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  86 lDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQ-VPVEFVGFSIPDEFVVGYGIDYAQRY 164
Cdd:PRK09162  92 -RESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAKpLKADFVGLEVPDRYVFGYGMDYKGYW 170


                 ....
gi 695712009 165 RHLP 168
Cdd:PRK09162 171 RNLP 174
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 21-144 5.08e-22

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 85.91  E-value: 5.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  21 LGRQITEHYKDSGSE-MVLVGLLRGSFMFMADLCREVHVPheVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLIVE 99
Cdd:cd06223    1 AGRLLAEEIREDLLEpDVVVGILRGGLPLAAALARALGLP--LAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLVD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 695712009 100 DIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFV 144
Cdd:cd06223   79 DVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD 123
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 13-160 2.85e-21

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: 84.72  E-value: 2.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   13 EIKARIAELGRQITEHYKdsGSEMVLVGLLRGSFMFMADLCREVHVPheVDFMTASSYGSGMSTtrdVKILKDLDEDIRG 92
Cdd:pfam00156  10 AILKAVARLAAQINEDYG--GKPDVVVGILRGGLPFAGILARRLDVP--LAFVRKVSYNPDTSE---VMKTSSALPDLKG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695712009   93 KDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQVPVEFVGFSiPDEFVVGYGIDY 160
Cdd:pfam00156  83 KTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 1-135 2.74e-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: 76.81  E-value: 2.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009   1 MKHTVEVMIPEAEIKARIAELGRQItehyKDSGSEM-VLVGLLRGSfMFMAD-LCREVHVPhEVDFMTASSYGSGMSTTR 78
Cdd:COG2236    1 MDKFKKEYLSWDEIHELSRRLAEQI----LESGFRPdVIVAIARGG-LVPARiLADALGVP-DLASIRVSSYTGTAKRLE 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 695712009  79 DVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERR 135
Cdd:COG2236   75 EPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSK 131
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 43-136 8.39e-08

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 49.09  E-value: 8.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  43 RGSFMFMADLCREVHVPHeVDFMTASSYGSgmSTTRDVKILKDLDEDirGKDVLIVEDIIDSGNTLSKVREILslrePKS 122
Cdd:PRK09177  40 RGGLVPAAILARELGIRL-VDTVCISSYDH--DNQGELKVLKRAEGD--GEGFLVVDDLVDTGGTARAVREMY----PKA 110

                         90
                 ....*....|....
gi 695712009 123 LaICTLLDKPERRE 136
Cdd:PRK09177 111 H-FATVYAKPAGRP 123
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
89-168 5.10e-05

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 42.41  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695712009  89 DIRGKDVLIVEDIIDSGNTLSKVREILSLREPKS-LAICT--LLDKPerrevqvPVEFVGFSIPDEFVVGYGIDYAQRYR 165
Cdd:PRK01259 205 DVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSvYAYAThpVLSGG-------AIERIENSVIDELVVTDSIPLSEEAK 277


                 ...
gi 695712009 166 HLP 168
Cdd:PRK01259 278 KCD 280
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 89-142 7.74e-05

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 41.39  E-value: 7.74e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 695712009  89 DIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPERREVQ-VPVE 142
Cdd:PRK02277 137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDKSGIDEIDgVPVY 191
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 84-115 2.35e-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: 2.35e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 695712009   84 KDLDEDIRGKDVLIVEDIIDSGNTLSKVREIL 115
Cdd:TIGR01251 202 MNLVGDVEGKDVVIVDDIIDTGGTIAKAAEIL 233
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 86-127 1.79e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 38.01  E-value: 1.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 695712009  86 LDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICT 127
Cdd:PRK06827 258 LGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAA 299
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 78-115 2.95e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 37.20  E-value: 2.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 695712009  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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