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Conserved domains on  [gi|1266752492|gb|PHG27472|]
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hypoxanthine phosphoribosyltransferase [Bacillus toyonensis]

Protein Classification

phosphoribosyltransferase( domain architecture ID 10786076)

type I phosphoribosyltransferase similar to phosphoribosyltransferases with specificities for hypoxanthine, guanine, and/or xanthine

EC:  2.4.2.-
Gene Ontology:  GO:0016763|GO:0000166|GO:0046872|GO:0043174
PubMed:  11751055
SCOP:  4000253

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 2-177 5.22e-109

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: 308.49  E-value: 5.22e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   2 MNQDIEKVLISEEQIQEKVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDTYLEMDFMAVSSYGHSTVSTGEVK 81
Cdd:COG0634     1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  82 ILKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPHEFVVGYGLDYK 161
Cdd:COG0634    81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                         170
                  ....*....|....*.
gi 1266752492 162 EQYRNLPYVGVLKPSV 177
Cdd:COG0634   161 EYYRNLPYIYALKPEV 176
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 2-177 5.22e-109

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: 308.49  E-value: 5.22e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   2 MNQDIEKVLISEEQIQEKVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDTYLEMDFMAVSSYGHSTVSTGEVK 81
Cdd:COG0634     1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  82 ILKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPHEFVVGYGLDYK 161
Cdd:COG0634    81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                         170
                  ....*....|....*.
gi 1266752492 162 EQYRNLPYVGVLKPSV 177
Cdd:COG0634   161 EYYRNLPYIYALKPEV 176
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 9-174 2.62e-85

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: 248.31  E-value: 2.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   9 VLISEEQIQEKVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDTYLEMDFMAVSSYGHSTVSTGEVKILKDLDT 88
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  89 SVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPHEFVVGYGLDYKEQYRNLP 168
Cdd:TIGR01203  81 DIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLP 160


                  ....*.
gi 1266752492 169 YVGVLK 174
Cdd:TIGR01203 161 YIGVLE 166
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 2-179 7.59e-72

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 214.90  E-value: 7.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   2 MNQDIEKVLISEEQIQEKVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDTY---LEMDFMAVSSYGHSTVSTG 78
Cdd:PLN02238    3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQPLprgLTVDFIRASSYGGGTESSG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  79 EVKI-LKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLK-----ADYVGFTVPHEF 152
Cdd:PLN02238   83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGFECPDEF 162

                         170       180
                  ....*....|....*....|....*..
gi 1266752492 153 VVGYGLDYKEQYRNLPYVGVLKPSVYS 179
Cdd:PLN02238  163 VVGYGLDFAEKYRNLPYVGVLKPEVYQ 189
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 19-161 2.19e-24

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: 92.81  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  19 KVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDtyLEMDFMAVSSYGHSTvstGEVKILKDLDTSVEGRDILIV 98
Cdd:pfam00156  14 AVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLD--VPLAFVRKVSYNPDT---SEVMKTSSALPDLKGKTVLIV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1266752492  99 EDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPhEFVVGYGLDYK 161
Cdd:pfam00156  89 DDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDDWI-VFVVGFGLDER 150
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 20-147 2.43e-23

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


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 89.38  E-value: 2.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  20 VRELGAIIAEDYKNTVPLaIGVLKGAMPFMADLLKRTDtyLEMDFMAVSSYGHSTVSTGEVKILKDLDTSVEGRDILIVE 99
Cdd:cd06223     2 GRLLAEEIREDLLEPDVV-VGILRGGLPLAAALARALG--LPLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLVD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1266752492 100 DIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKA----DYVGFT 147
Cdd:cd06223    79 DVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASpgdpVYSLFT 130
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 2-177 5.22e-109

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: 308.49  E-value: 5.22e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   2 MNQDIEKVLISEEQIQEKVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDTYLEMDFMAVSSYGHSTVSTGEVK 81
Cdd:COG0634     1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  82 ILKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPHEFVVGYGLDYK 161
Cdd:COG0634    81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                         170
                  ....*....|....*.
gi 1266752492 162 EQYRNLPYVGVLKPSV 177
Cdd:COG0634   161 EYYRNLPYIYALKPEV 176
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 9-174 2.62e-85

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: 248.31  E-value: 2.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   9 VLISEEQIQEKVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDTYLEMDFMAVSSYGHSTVSTGEVKILKDLDT 88
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  89 SVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPHEFVVGYGLDYKEQYRNLP 168
Cdd:TIGR01203  81 DIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLP 160


                  ....*.
gi 1266752492 169 YVGVLK 174
Cdd:TIGR01203 161 YIGVLE 166
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 2-179 7.59e-72

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 214.90  E-value: 7.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   2 MNQDIEKVLISEEQIQEKVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDTY---LEMDFMAVSSYGHSTVSTG 78
Cdd:PLN02238    3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQPLprgLTVDFIRASSYGGGTESSG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  79 EVKI-LKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLK-----ADYVGFTVPHEF 152
Cdd:PLN02238   83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGFECPDEF 162

                         170       180
                  ....*....|....*....|....*..
gi 1266752492 153 VVGYGLDYKEQYRNLPYVGVLKPSVYS 179
Cdd:PLN02238  163 VVGYGLDFAEKYRNLPYVGVLKPEVYQ 189
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 8-171 5.69e-50

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 159.03  E-value: 5.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   8 KVLISEEQIQEKVRELGAIIAEDYKNTVP--LAIGVLKGAMPFMADLLKRTDTYLEMDFMAVSSYGHSTVSTGEVKILKD 85
Cdd:PRK15423    6 EVMIPEAEIKARIAELGRQITERYKDSGSdmVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  86 LDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPHEFVVGYGLDYKEQYR 165
Cdd:PRK15423   86 LDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYR 165


                  ....*.
gi 1266752492 166 NLPYVG 171
Cdd:PRK15423  166 HLPYIG 171
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 1-175 9.43e-43

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 140.77  E-value: 9.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   1 MMNQDIEKV------LISEEQIQEKVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDTYLEMDFMAVSSYGHST 74
Cdd:PRK09162    1 MSLEEIRQVlaeadcLVSAAEVEAAIDRMADEITADLADENPLVLCVMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  75 vSTGEVKILKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKV-DLKADYVGFTVPHEFV 153
Cdd:PRK09162   81 -TGGELVWKVKPRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAkPLKADFVGLEVPDRYV 159

                         170       180
                  ....*....|....*....|..
gi 1266752492 154 VGYGLDYKEQYRNLPYVGVLKP 175
Cdd:PRK09162  160 FGYGMDYKGYWRNLPGIYAVKG 181
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 8-178 5.04e-42

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 139.77  E-value: 5.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   8 KVLISEEQIQEKVRELGAIIAEDYKN-----TVPL-AIGVLKGAMPFMADL---LKRTDTYLEMDFMAVSSYGHSTVSTG 78
Cdd:PTZ00271   25 HTLVTQEQVWAATAKCAKKIAEDYRSfklttENPLyLLCVLKGSFIFTADLarfLADEGVPVKVEFICASSYGTGVETSG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  79 EVKILKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPHEFVVGYGL 158
Cdd:PTZ00271  105 QVRMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGM 184

                         170       180
                  ....*....|....*....|
gi 1266752492 159 DYKEQYRNLPYVGVLKPSVY 178
Cdd:PTZ00271  185 DYAESYRELRDICVLKKEYY 204
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 5-173 3.39e-34

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 120.64  E-value: 3.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   5 DIEKVLISEEQIQEKVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTD-----TYLEM-------DFMAVSSYgH 72
Cdd:PTZ00149   52 YLTKILLPNGLIKDRVEKLAYDIKQVYGNEELHILCILKGSRGFFSALVDYLNrihnySSTESpkppyqeHYVRVKSY-C 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  73 STVSTGEVKILKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPHEF 152
Cdd:PTZ00149  131 NDESTGKLEIVSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPDHF 210

                         170       180
                  ....*....|....*....|.
gi 1266752492 153 VVGYGLDYKEQYRNLPYVGVL 173
Cdd:PTZ00149  211 VVGYCLDYNEHFRDLDHVAVL 231
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 19-161 2.19e-24

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: 92.81  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  19 KVRELGAIIAEDYKNTVPLAIGVLKGAMPFMADLLKRTDtyLEMDFMAVSSYGHSTvstGEVKILKDLDTSVEGRDILIV 98
Cdd:pfam00156  14 AVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLD--VPLAFVRKVSYNPDT---SEVMKTSSALPDLKGKTVLIV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1266752492  99 EDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKADYVGFTVPhEFVVGYGLDYK 161
Cdd:pfam00156  89 DDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDDWI-VFVVGFGLDER 150
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 20-147 2.43e-23

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


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 89.38  E-value: 2.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  20 VRELGAIIAEDYKNTVPLaIGVLKGAMPFMADLLKRTDtyLEMDFMAVSSYGHSTVSTGEVKILKDLDTSVEGRDILIVE 99
Cdd:cd06223     2 GRLLAEEIREDLLEPDVV-VGILRGGLPLAAALARALG--LPLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLVD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1266752492 100 DIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRKVDLKA----DYVGFT 147
Cdd:cd06223    79 DVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASpgdpVYSLFT 130
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 4-153 3.70e-20

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: 81.82  E-value: 3.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492   4 QDIEKVLISEEQIQEKVRELGAIIAEDykNTVPLAI-GVLKGAMP---FMADLLKRTDtyleMDFMAVSSYGHSTVSTGE 79
Cdd:COG2236     2 DKFKKEYLSWDEIHELSRRLAEQILES--GFRPDVIvAIARGGLVparILADALGVPD----LASIRVSSYTGTAKRLEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  80 VKILKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDKPTGRkvdLKADYVGFTV------PHEFV 153
Cdd:COG2236    76 PVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSK---FKPDYYAEETdawivfPWELD 152
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 67-144 6.21e-07

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 46.78  E-value: 6.21e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1266752492  67 VSSYGHSTvsTGEVKILKDLDTSVEGrdILIVEDIIDSGLTLSYLVDLfkYRKAksvKIVTLLDKPTGRK-VDlkaDYV 144
Cdd:PRK09177   63 ISSYDHDN--QGELKVLKRAEGDGEG--FLVVDDLVDTGGTARAVREM--YPKA---HFATVYAKPAGRPlVD---TYV 129
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 76-123 8.30e-05

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


Pssm-ID: 273523 [Multi-domain]  Cd Length: 308  Bit Score: 41.88  E-value: 8.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1266752492  76 STGEVKIlKDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSV 123
Cdd:TIGR01251 195 ATNEVEV-MNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRV 241
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 72-127 9.27e-05

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 41.86  E-value: 9.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1266752492  72 HSTVSTGEVKIL--KDLDTSVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVT 127
Cdd:PRK06827  242 YSRVVNGRNPIVahEFLGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAA 299
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 89-131 2.03e-04

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 40.24  E-value: 2.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1266752492  89 SVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVTLLDK 131
Cdd:PRK02277  137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDK 179
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 11-123 7.40e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 39.13  E-value: 7.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266752492  11 ISEEQIQE----KVRELGAI--IAEDYKNTV--PLAIGVLKGAMPF---MADLLKRTDTYLEmdfmavssygHSTVSTGE 79
Cdd:PRK00934  123 IHEPSILEffpiPFINLDAAplIAEYIGDKLddPLVLAPDKGALELakeAAEILGCEYDYLE----------KTRISPTE 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1266752492  80 VKI-LKDLDtsVEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSV 123
Cdd:PRK00934  193 VEIaPKNLD--VKGKDVLIVDDIISTGGTMATAIKILKEQGAKKV 235
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
90-123 1.02e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 38.56  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1266752492  90 VEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSV 123
Cdd:PRK01259  206 VEGRDCILVDDMIDTAGTLCKAAEALKERGAKSV 239
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
85-149 1.83e-03

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 37.41  E-value: 1.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266752492  85 DLDTSVEGRDILIVEDIIDSGLTLSYLVD-LFKYRKAKSVKIVTLLDKpTGRKVDLKADYVGFTVP 149
Cdd:PRK05205   88 DIPFDIEGKRVILVDDVLYTGRTIRAALDaLFDYGRPARVQLAVLVDR-GHRELPIRADYVGKNIP 152
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 90-123 2.27e-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: 37.73  E-value: 2.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1266752492  90 VEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSV 123
Cdd:COG0462   209 VEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSV 242
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
90-127 2.46e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 37.62  E-value: 2.46e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1266752492  90 VEGRDILIVEDIIDSGLTLSYLVDLFKYRKAKSVKIVT 127
Cdd:PRK03092  199 VEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVIIAA 236
 
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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