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Conserved domains on  [gi|489737991|ref|WP_003642086|]
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MULTISPECIES: hypoxanthine phosphoribosyltransferase [Lactiplantibacillus]

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]; ...
 1-176 6.87e-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: 282.68  E-value: 6.87e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   1 MNNDIERVLYSREDIHQVAQKLGKELTTAYAGKNPLIICVLKGAVLFTTDIIREMDIYADLDFINLSSYGNETISSGEVQ 80
Cdd:COG0634    1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  81 LTKDLDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEVPNEFVVGYGLDYA 160
Cdd:COG0634   81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                        170
                 ....*....|....*.
gi 489737991 161 ERYRNLPYVGILKPAI 176
Cdd:COG0634  161 EYYRNLPYIYALKPEV 176
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 1-176 6.87e-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: 282.68  E-value: 6.87e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   1 MNNDIERVLYSREDIHQVAQKLGKELTTAYAGKNPLIICVLKGAVLFTTDIIREMDIYADLDFINLSSYGNETISSGEVQ 80
Cdd:COG0634    1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  81 LTKDLDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEVPNEFVVGYGLDYA 160
Cdd:COG0634   81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                        170
                 ....*....|....*.
gi 489737991 161 ERYRNLPYVGILKPAI 176
Cdd:COG0634  161 EYYRNLPYIYALKPEV 176
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 8-173 1.65e-72

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: 215.95  E-value: 1.65e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991    8 VLYSREDIHQVAQKLGKELTTAYAGKNPLIICVLKGAVLFTTDIIREMDIYADLDFINLSSYGNETISSGEVQLTKDLDA 87
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   88 DVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEVPNEFVVGYGLDYAERYRNLP 167
Cdd:TIGR01203  81 DIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLP 160


                  ....*.
gi 489737991  168 YVGILK 173
Cdd:TIGR01203 161 YIGVLE 166
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 1-177 2.49e-69

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 208.74  E-value: 2.49e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   1 MNNDIERVLYSREDIHQVAQKLGKELTTAYAGKNPLIICVLKGAVLFTTDIIREMDIY---ADLDFINLSSYGNETISSG 77
Cdd:PLN02238   3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQPLprgLTVDFIRASSYGGGTESSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  78 EVQL-TKDLDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGR-----LVDIKADYIGFEVPNEF 151
Cdd:PLN02238  83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRkvkyeLVGDGKEYVGFECPDEF 162

                        170       180
                 ....*....|....*....|....*.
gi 489737991 152 VVGYGLDYAERYRNLPYVGILKPAIY 177
Cdd:PLN02238 163 VVGYGLDFAEKYRNLPYVGVLKPEVY 188
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 30-159 4.60e-25

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: 94.35  E-value: 4.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   30 YAGKNPLIICVLKGAVLFTTDIIREMDIyaDLDFINLSSYGNETissGEVQLTKDLDADVTGRDVLVIEDIIDTGRTLKF 109
Cdd:pfam00156  26 YGGKPDVVVGILRGGLPFAGILARRLDV--PLAFVRKVSYNPDT---SEVMKTSSALPDLKGKTVLIVDDILDTGGTLLK 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489737991  110 LIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEvPNEFVVGYGLDY 159
Cdd:pfam00156 101 VLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-146 1.67e-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: 87.45  E-value: 1.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  18 VAQKLGKELTTAYaGKNPLIICVLKGAVLFTTDIIREMDIyaDLDFINLSSYGNETISSGEVQLTKDLDADVTGRDVLVI 97
Cdd:cd06223    1 AGRLLAEEIREDL-LEPDVVVGILRGGLPLAAALARALGL--PLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489737991  98 EDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGR----LVDIKADYIGFE 146
Cdd:cd06223   78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGarelASPGDPVYSLFT 130
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 1-176 6.87e-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: 282.68  E-value: 6.87e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   1 MNNDIERVLYSREDIHQVAQKLGKELTTAYAGKNPLIICVLKGAVLFTTDIIREMDIYADLDFINLSSYGNETISSGEVQ 80
Cdd:COG0634    1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  81 LTKDLDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEVPNEFVVGYGLDYA 160
Cdd:COG0634   81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                        170
                 ....*....|....*.
gi 489737991 161 ERYRNLPYVGILKPAI 176
Cdd:COG0634  161 EYYRNLPYIYALKPEV 176
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 8-173 1.65e-72

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: 215.95  E-value: 1.65e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991    8 VLYSREDIHQVAQKLGKELTTAYAGKNPLIICVLKGAVLFTTDIIREMDIYADLDFINLSSYGNETISSGEVQLTKDLDA 87
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   88 DVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEVPNEFVVGYGLDYAERYRNLP 167
Cdd:TIGR01203  81 DIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLP 160


                  ....*.
gi 489737991  168 YVGILK 173
Cdd:TIGR01203 161 YIGVLE 166
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 1-177 2.49e-69

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 208.74  E-value: 2.49e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   1 MNNDIERVLYSREDIHQVAQKLGKELTTAYAGKNPLIICVLKGAVLFTTDIIREMDIY---ADLDFINLSSYGNETISSG 77
Cdd:PLN02238   3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQPLprgLTVDFIRASSYGGGTESSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  78 EVQL-TKDLDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGR-----LVDIKADYIGFEVPNEF 151
Cdd:PLN02238  83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRkvkyeLVGDGKEYVGFECPDEF 162

                        170       180
                 ....*....|....*....|....*.
gi 489737991 152 VVGYGLDYAERYRNLPYVGILKPAIY 177
Cdd:PLN02238 163 VVGYGLDFAEKYRNLPYVGVLKPEVY 188
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 1-170 1.17e-45

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 148.24  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   1 MNNDIErVLYSREDIHQVAQKLGKELTTAY--AGKNPLIICVLKGAVLFTTDIIREMDIYADLDFINLSSYGNETISSGE 78
Cdd:PRK15423   1 MKHTVE-VMIPEAEIKARIAELGRQITERYkdSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  79 VQLTKDLDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEVPNEFVVGYGLD 158
Cdd:PRK15423  80 VKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGID 159

                        170
                 ....*....|..
gi 489737991 159 YAERYRNLPYVG 170
Cdd:PRK15423 160 YAQRYRHLPYIG 171
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 9-177 1.37e-38

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 129.98  E-value: 1.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   9 LYSREDIHQVAQKLGKELTTAYAGKNPLIICVLKGAVLFTTDIIREMDIYADLDFINLSSYGNETiSSGEVQLTKDLDAD 88
Cdd:PRK09162  16 LVSAAEVEAAIDRMADEITADLADENPLVLCVMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNET-TGGELVWKVKPRES 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  89 VTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRLV-DIKADYIGFEVPNEFVVGYGLDYAERYRNLp 167
Cdd:PRK09162  95 LKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAkPLKADFVGLEVPDRYVFGYGMDYKGYWRNL- 173

                        170
                 ....*....|
gi 489737991 168 yvgilkPAIY 177
Cdd:PRK09162 174 ------PGIY 177
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 7-178 2.01e-36

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 125.52  E-value: 2.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   7 RVLYSREDIHQVAQKLGKELTTAY-----AGKNPL-IICVLKGAVLFTTDIIR---EMDIYADLDFINLSSYGNETISSG 77
Cdd:PTZ00271  25 HTLVTQEQVWAATAKCAKKIAEDYrsfklTTENPLyLLCVLKGSFIFTADLARflaDEGVPVKVEFICASSYGTGVETSG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  78 EVQLTKDLDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEVPNEFVVGYGL 157
Cdd:PTZ00271 105 QVRMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGM 184

                        170       180
                 ....*....|....*....|.
gi 489737991 158 DYAERYRNLPYVGILKPAIYE 178
Cdd:PTZ00271 185 DYAESYRELRDICVLKKEYYE 205
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 3-172 1.68e-29

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 108.70  E-value: 1.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   3 NDIERVLYSREDIHQVAQKLGKELTTAYAGKNPLIICVLKGAVLFTTDII-----------REMD--IYADlDFINLSSY 69
Cdd:PTZ00149  51 NYLTKILLPNGLIKDRVEKLAYDIKQVYGNEELHILCILKGSRGFFSALVdylnrihnyssTESPkpPYQE-HYVRVKSY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  70 GNeTISSGEVQLTKDLDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEVPN 149
Cdd:PTZ00149 130 CN-DESTGKLEIVSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPD 208

                        170       180
                 ....*....|....*....|...
gi 489737991 150 EFVVGYGLDYAERYRNLPYVGIL 172
Cdd:PTZ00149 209 HFVVGYCLDYNEHFRDLDHVAVL 231
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 30-159 4.60e-25

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: 94.35  E-value: 4.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   30 YAGKNPLIICVLKGAVLFTTDIIREMDIyaDLDFINLSSYGNETissGEVQLTKDLDADVTGRDVLVIEDIIDTGRTLKF 109
Cdd:pfam00156  26 YGGKPDVVVGILRGGLPFAGILARRLDV--PLAFVRKVSYNPDT---SEVMKTSSALPDLKGKTVLIVDDILDTGGTLLK 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489737991  110 LIDLLKRRDVNSVKVCTLLDKPAGRLVDIKADYIGFEvPNEFVVGYGLDY 159
Cdd:pfam00156 101 VLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-146 1.67e-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: 87.45  E-value: 1.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  18 VAQKLGKELTTAYaGKNPLIICVLKGAVLFTTDIIREMDIyaDLDFINLSSYGNETISSGEVQLTKDLDADVTGRDVLVI 97
Cdd:cd06223    1 AGRLLAEEIREDL-LEPDVVVGILRGGLPLAAALARALGL--PLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489737991  98 EDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGR----LVDIKADYIGFE 146
Cdd:cd06223   78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGarelASPGDPVYSLFT 130
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 4-148 7.54e-21

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: 83.74  E-value: 7.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   4 DIERVLYSREDIHQVAQKLGKELTTAyaGKNP-LIICVLKGAvLFTTDII-REMDIyADLDFINLSSYGNETISSGEVQL 81
Cdd:COG2236    3 KFKKEYLSWDEIHELSRRLAEQILES--GFRPdVIVAIARGG-LVPARILaDALGV-PDLASIRVSSYTGTAKRLEEPVV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489737991  82 TKDLDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDKPAGRlvdIKADYIGFEVP 148
Cdd:COG2236   79 KGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSK---FKPDYYAEETD 142
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 11-165 4.39e-10

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 55.25  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  11 SREDIHQVAQKLGKELttayAGKNPL--IICVLKGAvLFTTDII-REMDIYAdLDFINLSSYGNETisSGEVQLTKDLDA 87
Cdd:PRK09177  11 SWDQLHRDARALAWRL----LPAGQWkgIIAVTRGG-LVPAAILaRELGIRL-VDTVCISSYDHDN--QGELKVLKRAEG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991  88 DvtGRDVLVIEDIIDTGRTLKFLIDLLKRrdvnsVKVCTLLDKPAGR-LVDikaDYIgFEVPN----EFVVGYGLDYAER 162
Cdd:PRK09177  83 D--GEGFLVVDDLVDTGGTARAVREMYPK-----AHFATVYAKPAGRpLVD---TYV-TDVPQdtwiEFPWDMGLTFVPP 151


                 ...
gi 489737991 163 YRN 165
Cdd:PRK09177 152 LAD 154
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 87-130 4.15e-06

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 45.25  E-value: 4.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 489737991  87 ADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCTLLDK 130
Cdd:PRK02277 136 ASVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDK 179
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 88-125 1.13e-05

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: 44.28  E-value: 1.13e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 489737991  88 DVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVC 125
Cdd:COG0462  208 DVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAA 245
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 74-125 1.25e-05

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 44.13  E-value: 1.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489737991  74 ISSGEVQL-TKDLDadVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVC 125
Cdd:PRK00934 188 ISPTEVEIaPKNLD--VKGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYVA 238
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 33-126 6.03e-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: 42.27  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489737991   33 KNPLIICVLKGAVLFTTDIIREMDiyADLDFINlssygNETISSGEVQLTKDLDADVTGRDVLVIEDIIDTGRTLKFLID 112
Cdd:TIGR01251 159 DNPVVVSPDAGGVERAKKVADALG--CPLAIID-----KRRISATNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAE 231

                          90
                  ....*....|....
gi 489737991  113 LLKRRDVNSVKVCT 126
Cdd:TIGR01251 232 ILKSAGAKRVIAAA 245
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
88-125 4.28e-04

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 39.72  E-value: 4.28e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 489737991  88 DVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVC 125
Cdd:PRK01259 205 DVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSVYAY 242
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 85-126 2.12e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 37.62  E-value: 2.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 489737991  85 LDADVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCT 126
Cdd:PRK06827 258 LGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAA 299
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
88-141 2.42e-03

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 37.62  E-value: 2.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489737991  88 DVTGRDVLVIEDIIDTGRTLKFLIDLLKRRDVNSVKVCT---LLDKPAG-RLVDIKAD 141
Cdd:PRK03092 198 DVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVIIAAthgVLSGPAAeRLKNCGAR 255
 
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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