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Conserved domains on  [gi|1169421559|gb|ARC54656|]
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hypoxanthine phosphoribosyltransferase [Candidatus Riesia pthiripubis]

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]; ...
 3-173 2.36e-88

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: 256.11  E-value: 2.36e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   3 KTIKILISKKDIQKRVKEMAKEIVKHYKNlsNELILVGILNGSFIFIADLCREINVPHSIDFMRVSSYGNKTIQNKKVKI 82
Cdd:COG0634     4 DIAEVLISEEEIQARVKELAAQITADYAG--KEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  83 IQDLNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSINDKFVVGYGIDYAQ 162
Cdd:COG0634    82 LKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYAE 161

                         170
                  ....*....|.
gi 1169421559 163 KYRHLPYIGYI 173
Cdd:COG0634   162 YYRNLPYIYAL 172
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 3-173 2.36e-88

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: 256.11  E-value: 2.36e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   3 KTIKILISKKDIQKRVKEMAKEIVKHYKNlsNELILVGILNGSFIFIADLCREINVPHSIDFMRVSSYGNKTIQNKKVKI 82
Cdd:COG0634     4 DIAEVLISEEEIQARVKELAAQITADYAG--KEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  83 IQDLNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSINDKFVVGYGIDYAQ 162
Cdd:COG0634    82 LKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYAE 161

                         170
                  ....*....|.
gi 1169421559 163 KYRHLPYIGYI 173
Cdd:COG0634   162 YYRNLPYIYAL 172
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 7-173 7.37e-75

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: 221.35  E-value: 7.37e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   7 ILISKKDIQKRVKEMAKEIVKHYKNlsNELILVGILNGSFIFIADLCREINVPHSIDFMRVSSYGNKTIQNKKVKIIQDL 86
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAG--KPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  87 NRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSINDKFVVGYGIDYAQKYRH 166
Cdd:TIGR01203  79 DLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRN 158


                  ....*..
gi 1169421559 167 LPYIGYI 173
Cdd:TIGR01203 159 LPYIGVL 165
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 1-173 3.68e-70

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 210.26  E-value: 3.68e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   1 MRKTIKILISKKDIQKRVKEMAKEIVKHYKNLSNELILVGILNGSFIFIADLCREINVPHSIDFMRVSSYGNKTIQNKKV 80
Cdd:PRK15423    1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  81 KIIQDLNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSINDKFVVGYGIDY 160
Cdd:PRK15423   81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160

                         170
                  ....*....|...
gi 1169421559 161 AQKYRHLPYIGYI 173
Cdd:PRK15423  161 AQRYRHLPYIGKV 173
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 14-160 1.49e-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: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  14 IQKRVKEMAKEIVKHYKNlsNELILVGILNGSFIFIADLCREINVPhsIDFMRVSSYGNKTIQNkkVKIIQDLNrNIYNK 93
Cdd:pfam00156  11 ILKAVARLAAQINEDYGG--KPDVVVGILRGGLPFAGILARRLDVP--LAFVRKVSYNPDTSEV--MKTSSALP-DLKGK 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169421559  94 HILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSiNDKFVVGYGIDY 160
Cdd:pfam00156  84 TVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-136 2.73e-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: 88.99  E-value: 2.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  18 VKEMAKEIVKHYKNlsnELILVGILNGSFIFIADLCREINVPhsIDFMRVSSYGNKTIQNKKVKIIQDLNRNIYNKHILI 97
Cdd:cd06223     2 GRLLAEEIREDLLE---PDVVVGILRGGLPLAAALARALGLP--LAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLL 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1169421559  98 VEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRK 136
Cdd:cd06223    77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA 115
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 3-173 2.36e-88

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: 256.11  E-value: 2.36e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   3 KTIKILISKKDIQKRVKEMAKEIVKHYKNlsNELILVGILNGSFIFIADLCREINVPHSIDFMRVSSYGNKTIQNKKVKI 82
Cdd:COG0634     4 DIAEVLISEEEIQARVKELAAQITADYAG--KEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  83 IQDLNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSINDKFVVGYGIDYAQ 162
Cdd:COG0634    82 LKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYAE 161

                         170
                  ....*....|.
gi 1169421559 163 KYRHLPYIGYI 173
Cdd:COG0634   162 YYRNLPYIYAL 172
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 7-173 7.37e-75

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: 221.35  E-value: 7.37e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   7 ILISKKDIQKRVKEMAKEIVKHYKNlsNELILVGILNGSFIFIADLCREINVPHSIDFMRVSSYGNKTIQNKKVKIIQDL 86
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAG--KPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  87 NRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSINDKFVVGYGIDYAQKYRH 166
Cdd:TIGR01203  79 DLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRN 158


                  ....*..
gi 1169421559 167 LPYIGYI 173
Cdd:TIGR01203 159 LPYIGVL 165
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 1-173 3.68e-70

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 210.26  E-value: 3.68e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   1 MRKTIKILISKKDIQKRVKEMAKEIVKHYKNLSNELILVGILNGSFIFIADLCREINVPHSIDFMRVSSYGNKTIQNKKV 80
Cdd:PRK15423    1 MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  81 KIIQDLNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSINDKFVVGYGIDY 160
Cdd:PRK15423   81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDY 160

                         170
                  ....*....|...
gi 1169421559 161 AQKYRHLPYIGYI 173
Cdd:PRK15423  161 AQRYRHLPYIGKV 173
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 6-171 1.74e-56

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 175.61  E-value: 1.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   6 KILISKKDIQKRVKEMAKEIVKHYKNLSneLILVGILNGSFIFIADLCREINV---PHSIDFMRVSSYGNKTIQNKKVKI 82
Cdd:PLN02238    9 KVLWTAEDISARVAELAAQIASDYAGKS--PVVLGVATGAFMFLADLVRAIQPlprGLTVDFIRASSYGGGTESSGVAKV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  83 -IQDLNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFV-----KWIGYSINDKFVVGY 156
Cdd:PLN02238   87 sGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYELvgdgkEYVGFECPDEFVVGY 166

                         170
                  ....*....|....*
gi 1169421559 157 GIDYAQKYRHLPYIG 171
Cdd:PLN02238  167 GLDFAEKYRNLPYVG 181
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 6-167 3.57e-38

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 129.76  E-value: 3.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   6 KILISKKDIQKRVKEMAKEIVKHYKNLS----NELILVGILNGSFIFIADLCREI---NVPHSIDFMRVSSYGNKTIQNK 78
Cdd:PTZ00271   25 HTLVTQEQVWAATAKCAKKIAEDYRSFKltteNPLYLLCVLKGSFIFTADLARFLadeGVPVKVEFICASSYGTGVETSG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  79 KVKIIQDLNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSINDKFVVGYGI 158
Cdd:PTZ00271  105 QVRMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGM 184


                  ....*....
gi 1169421559 159 DYAQKYRHL 167
Cdd:PTZ00271  185 DYAESYREL 193
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 6-170 2.66e-27

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 102.54  E-value: 2.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   6 KILISKKDIQKRVKEMAKEIVKHYKNlsNELILVGILNGSFIFIADLCREINV------------PHSIDFMRVSSYGNk 73
Cdd:PTZ00149   55 KILLPNGLIKDRVEKLAYDIKQVYGN--EELHILCILKGSRGFFSALVDYLNRihnysstespkpPYQEHYVRVKSYCN- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  74 TIQNKKVKIIQDLNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSINDKFV 153
Cdd:PTZ00149  132 DESTGKLEIVSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPDHFV 211

                         170
                  ....*....|....*..
gi 1169421559 154 VGYGIDYAQKYRHLPYI 170
Cdd:PTZ00149  212 VGYCLDYNEHFRDLDHV 228
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 14-160 1.49e-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: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  14 IQKRVKEMAKEIVKHYKNlsNELILVGILNGSFIFIADLCREINVPhsIDFMRVSSYGNKTIQNkkVKIIQDLNrNIYNK 93
Cdd:pfam00156  11 ILKAVARLAAQINEDYGG--KPDVVVGILRGGLPFAGILARRLDVP--LAFVRKVSYNPDTSEV--MKTSSALP-DLKGK 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1169421559  94 HILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVFVKWIGYSiNDKFVVGYGIDY 160
Cdd:pfam00156  84 TVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-136 2.73e-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: 88.99  E-value: 2.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  18 VKEMAKEIVKHYKNlsnELILVGILNGSFIFIADLCREINVPhsIDFMRVSSYGNKTIQNKKVKIIQDLNRNIYNKHILI 97
Cdd:cd06223     2 GRLLAEEIREDLLE---PDVVVGILRGGLPLAAALARALGLP--LAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLL 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1169421559  98 VEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRK 136
Cdd:cd06223    77 VDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA 115
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 8-170 1.88e-22

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 88.38  E-value: 1.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   8 LISKKDIQKRVKEMAKEIVKHYKNlSNELILVgILNGSFIFIADLCREINVPHSIDFMRVSSYGNKTIQNK---KVKIIQ 84
Cdd:PRK09162   16 LVSAAEVEAAIDRMADEITADLAD-ENPLVLC-VMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNETTGGElvwKVKPRE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  85 DLnrniYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRRKSKVF-VKWIGYSINDKFVVGYGIDYAQK 163
Cdd:PRK09162   94 SL----KGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAKPLkADFVGLEVPDRYVFGYGMDYKGY 169


                  ....*..
gi 1169421559 164 YRHLPYI 170
Cdd:PRK09162  170 WRNLPGI 176
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 1-135 2.12e-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: 79.89  E-value: 2.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   1 MRKTIKILISKKDIQKRVKEMAKEIVKhyknlSNEL--ILVGILNGSFIFIADLCREINVPHsIDFMRVSSYGNKTIQNK 78
Cdd:COG2236     1 MDKFKKEYLSWDEIHELSRRLAEQILE-----SGFRpdVIVAIARGGLVPARILADALGVPD-LASIRVSSYTGTAKRLE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1169421559  79 KVKIIQDLNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTFLDKPSRR 135
Cdd:COG2236    75 EPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSK 131
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 86-127 2.01e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 37.62  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1169421559  86 LNRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCT 127
Cdd:PRK06827  258 LGRDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAA 299
PRK09177 PRK09177
xanthine-guanine phosphoribosyltransferase; Validated
 50-135 4.96e-03

xanthine-guanine phosphoribosyltransferase; Validated


Pssm-ID: 236395  Cd Length: 156  Bit Score: 35.61  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559  50 ADLCREINVPHsIDFMRVSSYGNKTIQNKKV-KIIQDLNRNIynkhiLIVEDIIDSGNTLKRILQILksrnPKS--ITVC 126
Cdd:PRK09177   47 AILARELGIRL-VDTVCISSYDHDNQGELKVlKRAEGDGEGF-----LVVDDLVDTGGTARAVREMY----PKAhfATVY 116


                  ....*....
gi 1169421559 127 TfldKPSRR 135
Cdd:PRK09177  117 A---KPAGR 122
PRK05205 PRK05205
bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;
3-107 5.75e-03

bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR;


Pssm-ID: 235365  Cd Length: 176  Bit Score: 35.87  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169421559   3 KTIKILISKKDIQKRVKEMAKEIVKHYKNLSNeLILVGILNGSfIFIAD-LCREIN------VPH-SIDfmrVSSYGNKT 74
Cdd:PRK05205    1 MMKKEILDAEALRRALTRIAHEIIERNKGLDN-LVLVGIKTRG-VWLAErLAERLEqlegvdVPVgELD---ITLYRDDL 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1169421559  75 IQNKKVKIIQ--DLNRNIYNKHILIVEDIIDSGNT 107
Cdd:PRK05205   76 TKKGLHPQVKptDIPFDIEGKRVILVDDVLYTGRT 110
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 73-125 6.12e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 36.00  E-value: 6.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1169421559  73 KTIQNKKVKIIQDLNRN---IYNKHILIVEDIIDSGNTLKRILQILKSR--NPKSITV 125
Cdd:PRK02277  118 KWDHGEGEKKTGSFSRNfasVEGKRCVIVDDVITSGTTMKETIEYLKEHggKPVAVVV 175
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 87-128 6.45e-03

DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General function prediction only];


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 35.57  E-value: 6.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1169421559  87 NRNIYNKHILIVEDIIDSGNTLKRILQILKSRNPKSITVCTF 128
Cdd:COG1040   150 PARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVL 191
 
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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