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Conserved domains on  [gi|488392074|ref|WP_002461459|]
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MULTISPECIES: hypoxanthine phosphoribosyltransferase [Staphylococcus]

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 3.27e-102

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: 291.16  E-value: 3.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   1 MHNDLKEIILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRIDTHLAIDFMDVSSYHGGTESTGEVQ 80
Cdd:COG0634    1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  81 IIKDLGTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYG 160
Cdd:COG0634   81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                        170
                 ....*....|....*.
gi 488392074 161 EHYRNLPYIGTLKPEV 176
Cdd:COG0634  161 EYYRNLPYIYALKPEV 176
 
Name Accession Description Interval E-value
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 1-176 3.27e-102

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: 291.16  E-value: 3.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   1 MHNDLKEIILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRIDTHLAIDFMDVSSYHGGTESTGEVQ 80
Cdd:COG0634    1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  81 IIKDLGTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYG 160
Cdd:COG0634   81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                        170
                 ....*....|....*.
gi 488392074 161 EHYRNLPYIGTLKPEV 176
Cdd:COG0634  161 EYYRNLPYIYALKPEV 176
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 8-173 9.31e-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: 226.36  E-value: 9.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074    8 IILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRIDTHLAIDFMDVSSYHGGTESTGEVQIIKDLGT 87
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   88 SIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYGEHYRNLP 167
Cdd:TIGR01203  81 DIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLP 160


                  ....*.
gi 488392074  168 YIGTLK 173
Cdd:TIGR01203 161 YIGVLE 166
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 1-177 1.27e-66

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 201.80  E-value: 1.27e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   1 MHNDLKEIILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRID---THLAIDFMDVSSYHGGTESTG 77
Cdd:PLN02238   3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQplpRGLTVDFIRASSYGGGTESSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  78 EVQI-IKDLGTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIE-----AKYVGKKIPDEF 151
Cdd:PLN02238  83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGFECPDEF 162

                        170       180
                 ....*....|....*....|....*.
gi 488392074 152 VVGYGLDYGEHYRNLPYIGTLKPEVY 177
Cdd:PLN02238 163 VVGYGLDFAEKYRNLPYVGVLKPEVY 188
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 7-159 2.63e-26

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: 97.82  E-value: 2.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074    7 EIILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRIDthLAIDFMDVSSYHGGTestGEVQIIKDLG 86
Cdd:pfam00156   3 DEILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLD--VPLAFVRKVSYNPDT---SEVMKTSSAL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488392074   87 TSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKiPDEFVVGYGLDY 159
Cdd:pfam00156  78 PDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-143 9.55e-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: 85.53  E-value: 9.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  18 LCKTLGEQITQDYQNKPLVcVGILKGSVMFMADLIKRIDthLAIDFMDVSSYHGGTESTGEVQIIKDLGTSIENKDVLII 97
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVV-VGILRGGLPLAAALARALG--LPLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488392074  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 3.27e-102

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: 291.16  E-value: 3.27e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   1 MHNDLKEIILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRIDTHLAIDFMDVSSYHGGTESTGEVQ 80
Cdd:COG0634    1 MHDDIAEVLISEEEIQARVKELAAQITADYAGKEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSGEVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  81 IIKDLGTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYG 160
Cdd:COG0634   81 ILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPADYVGFEIPDEFVVGYGLDYA 160

                        170
                 ....*....|....*.
gi 488392074 161 EHYRNLPYIGTLKPEV 176
Cdd:COG0634  161 EYYRNLPYIYALKPEV 176
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
 8-173 9.31e-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: 226.36  E-value: 9.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074    8 IILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRIDTHLAIDFMDVSSYHGGTESTGEVQIIKDLGT 87
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAGKPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKDLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   88 SIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYGEHYRNLP 167
Cdd:TIGR01203  81 DIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVDFVGFEIPDKFVVGYGLDYAERYRNLP 160


                  ....*.
gi 488392074  168 YIGTLK 173
Cdd:TIGR01203 161 YIGVLE 166
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 1-177 1.27e-66

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 201.80  E-value: 1.27e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   1 MHNDLKEIILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRID---THLAIDFMDVSSYHGGTESTG 77
Cdd:PLN02238   3 YEVDIEKVLWTAEDISARVAELAAQIASDYAGKSPVVLGVATGAFMFLADLVRAIQplpRGLTVDFIRASSYGGGTESSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  78 EVQI-IKDLGTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIE-----AKYVGKKIPDEF 151
Cdd:PLN02238  83 VAKVsGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYElvgdgKEYVGFECPDEF 162

                        170       180
                 ....*....|....*....|....*.
gi 488392074 152 VVGYGLDYGEHYRNLPYIGTLKPEVY 177
Cdd:PLN02238 163 VVGYGLDFAEKYRNLPYVGVLKPEVY 188
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
 7-172 4.99e-51

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 161.72  E-value: 4.99e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   7 EIILTEEEIQTLCKTLGEQITQDYQNK--PLVCVGILKGSVMFMADLIKRIDTHLAIDFMDVSSYHGGTESTGEVQIIKD 84
Cdd:PRK15423   6 EVMIPEAEIKARIAELGRQITERYKDSgsDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  85 LGTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDYGEHYR 164
Cdd:PRK15423  86 LDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYR 165


                 ....*...
gi 488392074 165 NLPYIGTL 172
Cdd:PRK15423 166 HLPYIGKV 173
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 9-179 3.19e-39

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 132.84  E-value: 3.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   9 ILTEEEIQTLCKTLGEQITQDYQ------NKPLVCVGILKGSVMFMADLIKRIDTH---LAIDFMDVSSYHGGTESTGEV 79
Cdd:PTZ00271  27 LVTQEQVWAATAKCAKKIAEDYRsfklttENPLYLLCVLKGSFIFTADLARFLADEgvpVKVEFICASSYGTGVETSGQV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  80 QIIKDLGTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDEFVVGYGLDY 159
Cdd:PTZ00271 107 RMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGMDY 186

                        170       180
                 ....*....|....*....|
gi 488392074 160 GEHYRNLPYIGTLKPEVYTK 179
Cdd:PTZ00271 187 AESYRELRDICVLKKEYYEK 206
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
 3-175 3.33e-35

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 123.34  E-value: 3.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   3 NDLKEIILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRI---------DTHLAI---DFMDVSSYH 70
Cdd:PTZ00149  51 NYLTKILLPNGLIKDRVEKLAYDIKQVYGNEELHILCILKGSRGFFSALVDYLnrihnysstESPKPPyqeHYVRVKSYC 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  71 GgTESTGEVQIIKDLGTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKIPDE 150
Cdd:PTZ00149 131 N-DESTGKLEIVSDDLSCLKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGFKGDFVGFSIPDH 209

                        170       180
                 ....*....|....*....|....*
gi 488392074 151 FVVGYGLDYGEHYRNLPYIGTLKPE 175
Cdd:PTZ00149 210 FVVGYCLDYNEHFRDLDHVAVLNDE 234
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 7-174 1.82e-27

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 101.48  E-value: 1.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   7 EIILTEEEIQTLCKTLGEQITQDYQNK-PLV-CVgiLKGSVMFMADLIKRIDTHLAIDFMDVSSYHGGTeSTGEVQIIKD 84
Cdd:PRK09162  14 DCLVSAAEVEAAIDRMADEITADLADEnPLVlCV--MGGGLVFTGQLLPRLDFPLEFDYLHATRYRNET-TGGELVWKVK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  85 LGTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKA-DIEAKYVGKKIPDEFVVGYGLDYGEHY 163
Cdd:PRK09162  91 PRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKAkPLKADFVGLEVPDRYVFGYGMDYKGYW 170

                        170
                 ....*....|.
gi 488392074 164 RNLPYIGTLKP 174
Cdd:PRK09162 171 RNLPGIYAVKG 181
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 7-159 2.63e-26

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: 97.82  E-value: 2.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074    7 EIILTEEEIQTLCKTLGEQITQDYQNKPLVCVGILKGSVMFMADLIKRIDthLAIDFMDVSSYHGGTestGEVQIIKDLG 86
Cdd:pfam00156   3 DEILDNPAILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLD--VPLAFVRKVSYNPDT---SEVMKTSSAL 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488392074   87 TSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYVGKKiPDEFVVGYGLDY 159
Cdd:pfam00156  78 PDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD-WIVFVVGFGLDE 149
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 18-143 9.55e-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: 85.53  E-value: 9.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  18 LCKTLGEQITQDYQNKPLVcVGILKGSVMFMADLIKRIDthLAIDFMDVSSYHGGTESTGEVQIIKDLGTSIENKDVLII 97
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVV-VGILRGGLPLAAALARALG--LPLAFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488392074  98 EDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRKADIEAKYV 143
Cdd:cd06223   78 DDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD 123
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 6-149 3.22e-16

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: 71.42  E-value: 3.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074   6 KEIILTEEEIQTLCKTLGEQITQDyQNKPLVCVGILKGSvMFMADLIKRIDTHLAIDFMDVSSYHGGTESTGEVQIIKDL 85
Cdd:COG2236    5 KKEYLSWDEIHELSRRLAEQILES-GFRPDVIVAIARGG-LVPARILADALGVPDLASIRVSSYTGTAKRLEEPVVKGPL 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488392074  86 GTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTLLDKPNRRkadIEAKYVGKKIPD 149
Cdd:COG2236   83 DEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPSSK---FKPDYYAEETDA 143
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 36-130 9.40e-04

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 38.31  E-value: 9.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392074  36 VCVGILKGSVMFmADLIKR-IDTHLAIdfmdvssYHGGTESTGEvqiIKDLG-------TSIENKDVLIIEDILETGTTL 107
Cdd:PRK02277  88 VVVGIAKSGVPL-ATLVADeLGKDLAI-------YHPKKWDHGE---GEKKTgsfsrnfASVEGKRCVIVDDVITSGTTM 156

                         90       100
                 ....*....|....*....|...
gi 488392074 108 KSITELLQSRKVNSLEIVTLLDK 130
Cdd:PRK02277 157 KETIEYLKEHGGKPVAVVVLIDK 179
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 86-127 3.07e-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: 3.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488392074  86 GTSIENKDVLIIEDILETGTTLKSITELLQSRKVNSLEIVTL 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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