NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|518446252|ref|WP_019616459|]
View 

hypoxanthine phosphoribosyltransferase [Psychromonas ossibalaenae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 4-172 5.44e-93

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: 267.66  E-value: 5.44e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   4 NHTITTMISEEEIKKRIQEMAVEINERYKDSEsVVLIGLLRGSAIFLADLARLLTVPVVLDFMATSSYGSGTDSSGDVKI 83
Cdd:COG0634    3 DDIAEVLISEEEIQARVKELAAQITADYAGKE-PLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  84 LKELDEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSIEDKFVVGYGIDYAQ 163
Cdd:COG0634   82 LKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYAE 161


                 ....*....
gi 518446252 164 RYRNLPYIG 172
Cdd:COG0634  162 YYRNLPYIY 170
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 4-172 5.44e-93

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: 267.66  E-value: 5.44e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   4 NHTITTMISEEEIKKRIQEMAVEINERYKDSEsVVLIGLLRGSAIFLADLARLLTVPVVLDFMATSSYGSGTDSSGDVKI 83
Cdd:COG0634    3 DDIAEVLISEEEIQARVKELAAQITADYAGKE-PLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  84 LKELDEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSIEDKFVVGYGIDYAQ 163
Cdd:COG0634   82 LKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYAE 161


                 ....*....
gi 518446252 164 RYRNLPYIG 172
Cdd:COG0634  162 YYRNLPYIY 170
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 9-175 8.17e-82

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: 239.07  E-value: 8.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252    9 TMISEEEIKKRIQEMAVEINERYKDSEsVVLIGLLRGSAIFLADLARLLTVPVVLDFMATSSYGSGTDSSGDVKILKELD 88
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKP-LVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   89 EEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSIEDKFVVGYGIDYAQRYRNL 168
Cdd:TIGR01203  80 LDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNL 159


                  ....*..
gi 518446252  169 PYIGFVS 175
Cdd:TIGR01203 160 PYIGVLE 166
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 5-176 1.37e-73

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 219.12  E-value: 1.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   5 HTITTMISEEEIKKRIQEMAVEINERYKDSES-VVLIGLLRGSAIFLADLARLLTVPVVLDFMATSSYGSGTDSSGDVKI 83
Cdd:PRK15423   3 HTVEVMIPEAEIKARIAELGRQITERYKDSGSdMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  84 LKELDEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSIEDKFVVGYGIDYAQ 163
Cdd:PRK15423  83 LKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQ 162

                        170
                 ....*....|...
gi 518446252 164 RYRNLPYIGFVSF 176
Cdd:PRK15423 163 RYRHLPYIGKVIL 175
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 15-161 3.86e-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: 92.04  E-value: 3.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   15 EIKKRIQEMAVEINERYKDSEsVVLIGLLRGSAIFLADLARLLTVPvvLDFMATSSYGsgTDSSGDVKILkELDEEIHGR 94
Cdd:pfam00156  10 AILKAVARLAAQINEDYGGKP-DVVVGILRGGLPFAGILARRLDVP--LAFVRKVSYN--PDTSEVMKTS-SALPDLKGK 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518446252   95 DVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSiEDKFVVGYGIDY 161
Cdd:pfam00156  84 TVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 20-139 1.05e-21

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: 85.14  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  20 IQEMAVEINERYKdsESVVLIGLLRGSAIFLADLARLLTVPVVldFMATSSYGSGTDSSGDVKILKELDEEIHGRDVLIV 99
Cdd:cd06223    2 GRLLAEEIREDLL--EPDVVVGILRGGLPLAAALARALGLPLA--FIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 518446252 100 EDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVE 139
Cdd:cd06223   78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARE 117
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 4-172 5.44e-93

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: 267.66  E-value: 5.44e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   4 NHTITTMISEEEIKKRIQEMAVEINERYKDSEsVVLIGLLRGSAIFLADLARLLTVPVVLDFMATSSYGSGTDSSGDVKI 83
Cdd:COG0634    3 DDIAEVLISEEEIQARVKELAAQITADYAGKE-PLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  84 LKELDEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSIEDKFVVGYGIDYAQ 163
Cdd:COG0634   82 LKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYAE 161


                 ....*....
gi 518446252 164 RYRNLPYIG 172
Cdd:COG0634  162 YYRNLPYIY 170
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 9-175 8.17e-82

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: 239.07  E-value: 8.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252    9 TMISEEEIKKRIQEMAVEINERYKDSEsVVLIGLLRGSAIFLADLARLLTVPVVLDFMATSSYGSGTDSSGDVKILKELD 88
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKP-LVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   89 EEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSIEDKFVVGYGIDYAQRYRNL 168
Cdd:TIGR01203  80 LDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNL 159


                  ....*..
gi 518446252  169 PYIGFVS 175
Cdd:TIGR01203 160 PYIGVLE 166
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 5-176 1.37e-73

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 219.12  E-value: 1.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   5 HTITTMISEEEIKKRIQEMAVEINERYKDSES-VVLIGLLRGSAIFLADLARLLTVPVVLDFMATSSYGSGTDSSGDVKI 83
Cdd:PRK15423   3 HTVEVMIPEAEIKARIAELGRQITERYKDSGSdMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  84 LKELDEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSIEDKFVVGYGIDYAQ 163
Cdd:PRK15423  83 LKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQ 162

                        170
                 ....*....|...
gi 518446252 164 RYRNLPYIGFVSF 176
Cdd:PRK15423 163 RYRHLPYIGKVIL 175
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 12-175 1.15e-56

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 176.38  E-value: 1.15e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  12 SEEEIKKRIQEMAVEINERYKDSESVVLiGLLRGSAIFLADLAR---LLTVPVVLDFMATSSYGSGTDSSGDVKI-LKEL 87
Cdd:PLN02238  13 TAEDISARVAELAAQIASDYAGKSPVVL-GVATGAFMFLADLVRaiqPLPRGLTVDFIRASSYGGGTESSGVAKVsGADL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  88 DEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQV-----EWEGFSIEDKFVVGYGIDYA 162
Cdd:PLN02238  92 KIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYELvgdgkEYVGFECPDEFVVGYGLDFA 171

                        170
                 ....*....|...
gi 518446252 163 QRYRNLPYIGFVS 175
Cdd:PLN02238 172 EKYRNLPYVGVLK 184
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 9-168 6.15e-39

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 132.07  E-value: 6.15e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   9 TMISEEEIKKRIQEMAVEINERYKD-----SESVVLIGLLRGSAIFLADLARLLT---VPVVLDFMATSSYGSGTDSSGD 80
Cdd:PTZ00271  26 TLVTQEQVWAATAKCAKKIAEDYRSfklttENPLYLLCVLKGSFIFTADLARFLAdegVPVKVEFICASSYGTGVETSGQ 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  81 VKILKELDEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSIEDKFVVGYGID 160
Cdd:PTZ00271 106 VRMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGMD 185


                 ....*...
gi 518446252 161 YAQRYRNL 168
Cdd:PTZ00271 186 YAESYREL 193
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 16-175 6.23e-30

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 109.47  E-value: 6.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  16 IKKRIQEMAVEINERYKDSEsVVLIGLLRGSAIFLADLARLLTV------------PVVLDFMATSSYgSGTDSSGDVKI 83
Cdd:PTZ00149  63 IKDRVEKLAYDIKQVYGNEE-LHILCILKGSRGFFSALVDYLNRihnysstespkpPYQEHYVRVKSY-CNDESTGKLEI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  84 LKELDEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSIEDKFVVGYGIDYAQ 163
Cdd:PTZ00149 141 VSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPDHFVVGYCLDYNE 220

                        170
                 ....*....|..
gi 518446252 164 RYRNLPYIGFVS 175
Cdd:PTZ00149 221 HFRDLDHVAVLN 232
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 11-171 7.10e-26

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 97.24  E-value: 7.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  11 ISEEEIKKRIQEMAVEINERYKDSESVVLIgLLRGSAIFLADLARLLTVPVVLDFMATSSYGSGTdSSGDVKILKELDEE 90
Cdd:PRK09162  17 VSAAEVEAAIDRMADEITADLADENPLVLC-VMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNET-TGGELVWKVKPRES 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  91 IHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVE-VQVEWEGFSIEDKFVVGYGIDYAQRYRNLP 169
Cdd:PRK09162  95 LKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAKpLKADFVGLEVPDRYVFGYGMDYKGYWRNLP 174


                 ..
gi 518446252 170 YI 171
Cdd:PRK09162 175 GI 176
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 15-161 3.86e-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: 92.04  E-value: 3.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252   15 EIKKRIQEMAVEINERYKDSEsVVLIGLLRGSAIFLADLARLLTVPvvLDFMATSSYGsgTDSSGDVKILkELDEEIHGR 94
Cdd:pfam00156  10 AILKAVARLAAQINEDYGGKP-DVVVGILRGGLPFAGILARRLDVP--LAFVRKVSYN--PDTSEVMKTS-SALPDLKGK 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518446252   95 DVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVEVQVEWEGFSiEDKFVVGYGIDY 161
Cdd:pfam00156  84 TVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 20-139 1.05e-21

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: 85.14  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  20 IQEMAVEINERYKdsESVVLIGLLRGSAIFLADLARLLTVPVVldFMATSSYGSGTDSSGDVKILKELDEEIHGRDVLIV 99
Cdd:cd06223    2 GRLLAEEIREDLL--EPDVVVGILRGGLPLAAALARALGLPLA--FIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 518446252 100 EDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRREVE 139
Cdd:cd06223   78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARE 117
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 11-136 3.80e-19

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: 79.12  E-value: 3.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  11 ISEEEIKKRIQEMAVEIneryKDSESV--VLIGLLRGSAIfLAD-LARLLTVPVvLDFMATSSYGSGTDSSGDVKILKEL 87
Cdd:COG2236    9 LSWDEIHELSRRLAEQI----LESGFRpdVIVAIARGGLV-PARiLADALGVPD-LASIRVSSYTGTAKRLEEPVVKGPL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 518446252  88 DEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICTLLTKPSRR 136
Cdd:COG2236   83 DEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSK 131
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 40-137 2.44e-08

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 50.63  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518446252  40 IGLLRGSAIFLADLARLLTVPVVlDFMATSSYGSgtDSSGDVKILKELDEEihGRDVLIVEDIIDTGNTLTKIKKMLllr 119
Cdd:PRK09177  36 IAVTRGGLVPAAILARELGIRLV-DTVCISSYDH--DNQGELKVLKRAEGD--GEGFLVVDDLVDTGGTARAVREMY--- 107

                         90
                 ....*....|....*....
gi 518446252 120 dPKS-FAicTLLTKPSRRE 137
Cdd:PRK09177 108 -PKAhFA--TVYAKPAGRP 123
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
90-128 2.56e-06

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 46.26  E-value: 2.56e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 518446252  90 EIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKS-FAICT 128
Cdd:PRK01259 205 DVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSvYAYAT 244
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 76-128 2.72e-06

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: 46.21  E-value: 2.72e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 518446252  76 DSSGDVKILkELDEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKS-FAICT 128
Cdd:COG0462  195 PGANEVEVM-NIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSvYAAAT 247
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 76-129 1.79e-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: 40.73  E-value: 1.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 518446252   76 DSSGDVKILKeLDEEIHGRDVLIVEDIIDTGNTLtkIKKMLLLRDP---KSFAICTL 129
Cdd:TIGR01251 194 SATNEVEVMN-LVGDVEGKDVVIVDDIIDTGGTI--AKAAEILKSAgakRVIAAATH 247
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 85-116 1.74e-03

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 37.97  E-value: 1.74e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 518446252  85 KELDeeIHGRDVLIVEDIIDTGNTLTKIKKML 116
Cdd:PRK00934 198 KNLD--VKGKDVLIVDDIISTGGTMATAIKIL 227
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 87-128 7.81e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 36.08  E-value: 7.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 518446252  87 LDEEIHGRDVLIVEDIIDTGNTLTKIKKMLLLRDPKSFAICT 128
Cdd:PRK06827 258 LGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAA 299
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH