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Conserved domains on  [gi|578681358|gb|EUP15351|]
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hypoxanthine-guanine phosphoribosyltransferase [Staphylococcus aureus M1527]

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 4.50e-103

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: 293.47  E-value: 4.50e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   1 MHNDLKEVLLTEEDIQNICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRIDTHLSIDFMDVSSYHGGTESTGEVQ 80
Cdd:COG0634    1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  81 IIKDLGSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYR 160
Cdd:COG0634   81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                        170
                 ....*....|....*.
gi 578681358 161 ELYRNLPYIGTLKPEV 176
Cdd:COG0634  161 EYYRNLPYIYALKPEV 176
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 1-176 4.50e-103

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: 293.47  E-value: 4.50e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   1 MHNDLKEVLLTEEDIQNICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRIDTHLSIDFMDVSSYHGGTESTGEVQ 80
Cdd:COG0634    1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  81 IIKDLGSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYR 160
Cdd:COG0634   81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                        170
                 ....*....|....*.
gi 578681358 161 ELYRNLPYIGTLKPEV 176
Cdd:COG0634  161 EYYRNLPYIYALKPEV 176
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 8-173 4.88e-77

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: 227.13  E-value: 4.88e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358    8 VLLTEEDIQNICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRIDTHLSIDFMDVSSYHGGTESTGEVQIIKDLGS 87
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   88 SIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYRELYRNLP 167
Cdd:TIGR01203  81 DIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLP 160


                  ....*.
gi 578681358  168 YIGTLK 173
Cdd:TIGR01203 161 YIGVLE 166
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 1-178 6.32e-70

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 209.89  E-value: 6.32e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   1 MHNDLKEVLLTEEDIQNICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRID---THLSIDFMDVSSYHGGTESTG 77
Cdd:PLN02238   3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQplpRGLTVDFIRASSYGGGTESSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  78 EVQI-IKDLGSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIE-----AKYVGKKIPDEF 151
Cdd:PLN02238  83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGFECPDEF 162

                        170       180
                 ....*....|....*....|....*..
gi 578681358 152 VVGYGLDYRELYRNLPYIGTLKPEVYS 178
Cdd:PLN02238 163 VVGYGLDFAEKYRNLPYVGVLKPEVYQ 189
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 18-160 1.43e-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: 95.89  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   18 ICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRIDthLSIDFMDVSSYHGGTestGEVQIIKDLGSSIENKDVLII 97
Cdd:pfam00156  14 AVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLD--VPLAFVRKVSYNPDT---SEVMKTSSALPDLKGKTVLIV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578681358   98 EDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKiPDEFVVGYGLDYR 160
Cdd:pfam00156  89 DDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDER 150
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-143 2.95e-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: 83.98  E-value: 2.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  18 ICKELGAQLTKDYqGKPLVCVGILKGSAMFMSDLIKRIDthLSIDFMDVSSYHGGTESTGEVQIIKDLGSSIENKDVLII 97
Cdd:cd06223    1 AGRLLAEEIREDL-LEPDVVVGILRGGLPLAAALARALG--LPLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 578681358  98 EDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYV 143
Cdd:cd06223   78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD 123
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 1-176 4.50e-103

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: 293.47  E-value: 4.50e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   1 MHNDLKEVLLTEEDIQNICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRIDTHLSIDFMDVSSYHGGTESTGEVQ 80
Cdd:COG0634    1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  81 IIKDLGSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYR 160
Cdd:COG0634   81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                        170
                 ....*....|....*.
gi 578681358 161 ELYRNLPYIGTLKPEV 176
Cdd:COG0634  161 EYYRNLPYIYALKPEV 176
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 8-173 4.88e-77

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: 227.13  E-value: 4.88e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358    8 VLLTEEDIQNICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRIDTHLSIDFMDVSSYHGGTESTGEVQIIKDLGS 87
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   88 SIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYRELYRNLP 167
Cdd:TIGR01203  81 DIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLP 160


                  ....*.
gi 578681358  168 YIGTLK 173
Cdd:TIGR01203 161 YIGVLE 166
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 1-178 6.32e-70

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 209.89  E-value: 6.32e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   1 MHNDLKEVLLTEEDIQNICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRID---THLSIDFMDVSSYHGGTESTG 77
Cdd:PLN02238   3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQplpRGLTVDFIRASSYGGGTESSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  78 EVQI-IKDLGSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIE-----AKYVGKKIPDEF 151
Cdd:PLN02238  83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGFECPDEF 162

                        170       180
                 ....*....|....*....|....*..
gi 578681358 152 VVGYGLDYRELYRNLPYIGTLKPEVYS 178
Cdd:PLN02238 163 VVGYGLDFAEKYRNLPYVGVLKPEVYQ 189
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 7-172 3.21e-50

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 159.80  E-value: 3.21e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   7 EVLLTEEDIQNICKELGAQLTKDYQ--GKPLVCVGILKGSAMFMSDLIKRIDTHLSIDFMDVSSYHGGTESTGEVQIIKD 84
Cdd:PRK15423   6 EVMIPEAEIKARIAELGRQITERYKdsGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  85 LGSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYRELYR 164
Cdd:PRK15423  86 LDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYR 165


                 ....*...
gi 578681358 165 NLPYIGTL 172
Cdd:PRK15423 166 HLPYIGKV 173
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 9-177 8.79e-36

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 123.98  E-value: 8.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   9 LLTEEDIQNICKELGAQLTKDYQG------KPLVCVGILKGSAMFMSDLIKRIDTH---LSIDFMDVSSYHGGTESTGEV 79
Cdd:PTZ00271  27 LVTQEQVWAATAKCAKKIAEDYRSfkltteNPLYLLCVLKGSFIFTADLARFLADEgvpVKVEFICASSYGTGVETSGQV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  80 QIIKDLGSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDY 159
Cdd:PTZ00271 107 RMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGMDY 186

                        170
                 ....*....|....*...
gi 578681358 160 RELYRNLPYIGTLKPEVY 177
Cdd:PTZ00271 187 AESYRELRDICVLKKEYY 204
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 3-175 1.96e-34

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 121.41  E-value: 1.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   3 NDLKEVLLTEEDIQNICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRI---------DTHLSI---DFMDVSSYH 70
Cdd:PTZ00149  51 NYLTKILLPNGLIKDRVEKLAYDIKQVYGNEELHILCILKGSRGFFSALVDYLnrihnysstESPKPPyqeHYVRVKSYC 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  71 GgTESTGEVQIIKDLGSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDE 150
Cdd:PTZ00149 131 N-DESTGKLEIVSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPDH 209

                        170       180
                 ....*....|....*....|....*
gi 578681358 151 FVVGYGLDYRELYRNLPYIGTLKPE 175
Cdd:PTZ00149 210 FVVGYCLDYNEHFRDLDHVAVLNDE 234
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 7-174 2.23e-27

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 101.48  E-value: 2.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   7 EVLLTEEDIQNICKELGAQLTKDYQGK-PLV-CVgiLKGSAMFMSDLIKRIDTHLSIDFMDVSSYHGGTeSTGEVQIIKD 84
Cdd:PRK09162  14 DCLVSAAEVEAAIDRMADEITADLADEnPLVlCV--MGGGLVFTGQLLPRLDFPLEFDYLHATRYRNET-TGGELVWKVK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  85 LGSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKA-DIEAKYVGKKIPDEFVVGYGLDYRELY 163
Cdd:PRK09162  91 PRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAkPLKADFVGLEVPDRYVFGYGMDYKGYW 170

                        170
                 ....*....|.
gi 578681358 164 RNLPYIGTLKP 174
Cdd:PRK09162 171 RNLPGIYAVKG 181
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 18-160 1.43e-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: 95.89  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   18 ICKELGAQLTKDYQGKPLVCVGILKGSAMFMSDLIKRIDthLSIDFMDVSSYHGGTestGEVQIIKDLGSSIENKDVLII 97
Cdd:pfam00156  14 AVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLD--VPLAFVRKVSYNPDT---SEVMKTSSALPDLKGKTVLIV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578681358   98 EDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKiPDEFVVGYGLDYR 160
Cdd:pfam00156  89 DDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDER 150
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-143 2.95e-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: 83.98  E-value: 2.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  18 ICKELGAQLTKDYqGKPLVCVGILKGSAMFMSDLIKRIDthLSIDFMDVSSYHGGTESTGEVQIIKDLGSSIENKDVLII 97
Cdd:cd06223    1 AGRLLAEEIREDL-LEPDVVVGILRGGLPLAAALARALG--LPLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 578681358  98 EDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYV 143
Cdd:cd06223   78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD 123
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 6-149 2.09e-13

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: 64.10  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358   6 KEVLLTEEDIQNICKELGAQLTKDyQGKPLVCVGILKGSaMFMSDLIKRIDTHLSIDFMDVSSYHGGTESTGEVQIIKDL 85
Cdd:COG2236    5 KKEYLSWDEIHELSRRLAEQILES-GFRPDVIVAIARGG-LVPARILADALGVPDLASIRVSSYTGTAKRLEEPVVKGPL 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578681358  86 GSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRkadIEAKYVGKKIPD 149
Cdd:COG2236   83 DEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSK---FKPDYYAEETDA 143
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 41-130 4.64e-04

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 39.08  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578681358  41 LKGSAMFMSDLIKR----IDTHLSI------------DFMDV--SSYHGGTESTGEvqiIKDLG-------SSIENKDVL 95
Cdd:PRK02277  68 LRYIASAMADMLEKedeeVDVVVGIaksgvplatlvaDELGKdlAIYHPKKWDHGE---GEKKTgsfsrnfASVEGKRCV 144

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 578681358  96 IIEDILETGTTLKSITELLQSRKVNSLEIVTLLDK 130
Cdd:PRK02277 145 IVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDK 179
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 86-127 2.90e-03

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 36.72  E-value: 2.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 578681358  86 GSSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTL 127
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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