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Conserved domains on  [gi|15217571|ref|NP_177320|]
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Hypoxanthine-guanine phosphoribosyltransferase [Arabidopsis thaliana]

Protein Classification

type I phosphoribosyltransferase; uracil phosphoribosyltransferase( domain architecture ID 10791302)

type I phosphoribosyltransferase similar to phosphoribosyltransferases with specificities for hypoxanthine, guanine, and/or xanthine; uracil phosphoribosyltransferase catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
1-188 3.42e-113

hypoxanthine phosphoribosyltransferase


:

Pssm-ID: 215132  Cd Length: 189  Bit Score: 320.06  E-value: 3.42e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    1 MALEKHIEKVLFSDEVIAHRVNQLGIDITSDFSGDSeetPIFVGVATGACLFLADLVRRIDL---PIAIDFIRAESYGSG 77
Cdd:PLN02238   1 PEYEVDIEKVLWTAEDISARVAELAAQIASDYAGKS---PVVLGVATGAFMFLADLVRAIQPlprGLTVDFIRASSYGGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   78 TVSSGVPRVSF-DLKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVGKGKFYSGFE 156
Cdd:PLN02238  78 TESSGVAKVSGaDLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYELVGDGKEYVGFE 157
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15217571  157 CPDEFVVGYGMDFAEQYRNLSYIGVLKPEYYM 188
Cdd:PLN02238 158 CPDEFVVGYGLDFAEKYRNLPYVGVLKPEVYQ 189
 
Name Accession Description Interval E-value
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
1-188 3.42e-113

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 320.06  E-value: 3.42e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    1 MALEKHIEKVLFSDEVIAHRVNQLGIDITSDFSGDSeetPIFVGVATGACLFLADLVRRIDL---PIAIDFIRAESYGSG 77
Cdd:PLN02238   1 PEYEVDIEKVLWTAEDISARVAELAAQIASDYAGKS---PVVLGVATGAFMFLADLVRAIQPlprGLTVDFIRASSYGGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   78 TVSSGVPRVSF-DLKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVGKGKFYSGFE 156
Cdd:PLN02238  78 TESSGVAKVSGaDLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYELVGDGKEYVGFE 157
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15217571  157 CPDEFVVGYGMDFAEQYRNLSYIGVLKPEYYM 188
Cdd:PLN02238 158 CPDEFVVGYGLDFAEKYRNLPYVGVLKPEVYQ 189
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
3-185 5.09e-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: 255.72  E-value: 5.09e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   3 LEKHIEKVLFSDEVIAHRVNQLGIDITSDFSGdseETPIFVGVATGACLFLADLVRRIDLPIAIDFIRAESYGSGTVSSG 82
Cdd:COG0634   1 MHDDIAEVLISEEEIQARVKELAAQITADYAG---KEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571  83 VPRVSFDLKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVgkgkfYSGFECPDEFV 162
Cdd:COG0634  78 EVRILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPAD-----YVGFEIPDEFV 152
                       170       180
                ....*....|....*....|...
gi 15217571 163 VGYGMDFAEQYRNLSYIGVLKPE 185
Cdd:COG0634 153 VGYGLDYAEYYRNLPYIYALKPE 175
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
10-183 1.83e-64

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: 195.92  E-value: 1.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    10 VLFSDEVIAHRVNQLGIDITSDFSGdseETPIFVGVATGACLFLADLVRRIDLPIAIDFIRAESYGSGTVSSGVPRVSFD 89
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAG---KPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    90 LKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVgkgkfYSGFECPDEFVVGYGMDF 169
Cdd:TIGR01203  78 LDLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVD-----FVGFEIPDKFVVGYGLDY 152
                         170
                  ....*....|....
gi 15217571   170 AEQYRNLSYIGVLK 183
Cdd:TIGR01203 153 AERYRNLPYIGVLE 166
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
32-156 5.07e-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: 5.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571  32 FSGDSEETPIFVGVATGACLFLADLVRRIDLPIaiDFIRAESYGSGTVSSGVPRVSFDLKLDITNKHVVLVEDIVDTGNT 111
Cdd:cd06223   9 IREDLLEPDVVVGILRGGLPLAAALARALGLPL--AFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLVDDVIATGGT 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15217571 112 LSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVGKgKFYSGFE 156
Cdd:cd06223  87 LLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD-PVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
40-169 8.91e-22

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: 86.26  E-value: 8.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    40 PIFVGVATGACLFLADLVRRIDLPIAidFIRAESYGSGTVSSGVPRvsfDLKLDITNKHVVLVEDIVDTGNTLSCLIEHM 119
Cdd:pfam00156  31 DVVVGILRGGLPFAGILARRLDVPLA--FVRKVSYNPDTSEVMKTS---SALPDLKGKTVLIVDDILDTGGTLLKVLELL 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 15217571   120 KAKKASSVSVCTLLDKPSRRKVHYKLVGKGKFysgfecPDEFVVGYGMDF 169
Cdd:pfam00156 106 KNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD------WIVFVVGFGLDE 149
 
Name Accession Description Interval E-value
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
1-188 3.42e-113

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 320.06  E-value: 3.42e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    1 MALEKHIEKVLFSDEVIAHRVNQLGIDITSDFSGDSeetPIFVGVATGACLFLADLVRRIDL---PIAIDFIRAESYGSG 77
Cdd:PLN02238   1 PEYEVDIEKVLWTAEDISARVAELAAQIASDYAGKS---PVVLGVATGAFMFLADLVRAIQPlprGLTVDFIRASSYGGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   78 TVSSGVPRVSF-DLKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVGKGKFYSGFE 156
Cdd:PLN02238  78 TESSGVAKVSGaDLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCALLDKRARRKVKYELVGDGKEYVGFE 157
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15217571  157 CPDEFVVGYGMDFAEQYRNLSYIGVLKPEYYM 188
Cdd:PLN02238 158 CPDEFVVGYGLDFAEKYRNLPYVGVLKPEVYQ 189
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
3-185 5.09e-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: 255.72  E-value: 5.09e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   3 LEKHIEKVLFSDEVIAHRVNQLGIDITSDFSGdseETPIFVGVATGACLFLADLVRRIDLPIAIDFIRAESYGSGTVSSG 82
Cdd:COG0634   1 MHDDIAEVLISEEEIQARVKELAAQITADYAG---KEPLVVGVLKGAFVFMADLLRALDFPLEIDFMHVSSYGGGTESSG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571  83 VPRVSFDLKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVgkgkfYSGFECPDEFV 162
Cdd:COG0634  78 EVRILKDLDEDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIATLLDKPERRKVDVPAD-----YVGFEIPDEFV 152
                       170       180
                ....*....|....*....|...
gi 15217571 163 VGYGMDFAEQYRNLSYIGVLKPE 185
Cdd:COG0634 153 VGYGLDYAEYYRNLPYIYALKPE 175
HGPRTase TIGR01203
hypoxanthine phosphoribosyltransferase; Alternate name: hypoxanthine-guanine ...
10-183 1.83e-64

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: 195.92  E-value: 1.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    10 VLFSDEVIAHRVNQLGIDITSDFSGdseETPIFVGVATGACLFLADLVRRIDLPIAIDFIRAESYGSGTVSSGVPRVSFD 89
Cdd:TIGR01203   1 VLIPEEQIKARIAELAKQITEDYAG---KPLVLLCVLKGSFPFFADLIRYIAVPVQVDFMAVSSYGNGMQSSGDVKILKD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    90 LKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVgkgkfYSGFECPDEFVVGYGMDF 169
Cdd:TIGR01203  78 LDLDIKGKDVLIVEDIVDTGLTLQYLLDLLKARKPKSLKIVTLLDKPSRRKVDVKVD-----FVGFEIPDKFVVGYGLDY 152
                         170
                  ....*....|....
gi 15217571   170 AEQYRNLSYIGVLK 183
Cdd:TIGR01203 153 AERYRNLPYIGVLE 166
PRK15423 PRK15423
hypoxanthine phosphoribosyltransferase; Provisional
5-180 1.47e-41

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 185321  Cd Length: 178  Bit Score: 137.84  E-value: 1.47e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    5 KHIEKVLFSDEVIAHRVNQLGIDITSDFSgDSEETPIFVGVATGACLFLADLVRRIDLPIAIDFIRAESYGSGTVSSGVP 84
Cdd:PRK15423   2 KHTVEVMIPEAEIKARIAELGRQITERYK-DSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   85 RVSFDLKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVgkgkfYSGFECPDEFVVG 164
Cdd:PRK15423  81 KILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVE-----FIGFSIPDEFVVG 155
                        170
                 ....*....|....*.
gi 15217571  165 YGMDFAEQYRNLSYIG 180
Cdd:PRK15423 156 YGIDYAQRYRHLPYIG 171
PTZ00271 PTZ00271
hypoxanthine-guanine phosphoribosyltransferase; Provisional
36-188 1.80e-37

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 140297  Cd Length: 211  Bit Score: 128.60  E-value: 1.80e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   36 SEETPIFV-GVATGACLFLADLVRRI---DLPIAIDFIRAESYGSGTVSSGVPRVSFDLKLDITNKHVVLVEDIVDTGNT 111
Cdd:PTZ00271  54 TTENPLYLlCVLKGSFIFTADLARFLadeGVPVKVEFICASSYGTGVETSGQVRMLLDVRDSVENRHILIVEDIVDSAIT 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15217571  112 LSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYkLVGkgkfYSGFECPDEFVVGYGMDFAEQYRNLSYIGVLKPEYYM 188
Cdd:PTZ00271 134 LQYLMRFMLAKKPASLKTVVLLDKPSGRKVEV-LVD----YPVITIPHAFVIGYGMDYAESYRELRDICVLKKEYYE 205
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
6-184 1.94e-26

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 99.17  E-value: 1.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    6 HIEKV------LFSDEVIAHRVNQLGIDITSDFSGDSeetPIFVGVATGACLFLADLVRRIDLPIAIDFIRAESYGSGTV 79
Cdd:PRK09162   5 EIRQVlaeadcLVSAAEVEAAIDRMADEITADLADEN---PLVLCVMGGGLVFTGQLLPRLDFPLEFDYLHATRYRNETT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   80 SSGV-----PRVSFdlkldiTNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVhyklvgKGKF--Y 152
Cdd:PRK09162  82 GGELvwkvkPRESL------KGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAVLVDKTHDRKA------KPLKadF 149
                        170       180       190
                 ....*....|....*....|....*....|..
gi 15217571  153 SGFECPDEFVVGYGMDFAEQYRNLSYIGVLKP 184
Cdd:PRK09162 150 VGLEVPDRYVFGYGMDYKGYWRNLPGIYAVKG 181
PTZ00149 PTZ00149
hypoxanthine phosphoribosyltransferase; Provisional
4-185 6.11e-25

hypoxanthine phosphoribosyltransferase; Provisional


Pssm-ID: 240293  Cd Length: 241  Bit Score: 96.76  E-value: 6.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    4 EKHIEKVLFSDEVIAHRVNQLGIDITSDFSGdsEETPIFVgVATGACLFLADLVRRI---------DLPIAI---DFIRA 71
Cdd:PTZ00149  50 KNYLTKILLPNGLIKDRVEKLAYDIKQVYGN--EELHILC-ILKGSRGFFSALVDYLnrihnysstESPKPPyqeHYVRV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   72 ESYGSGTVSSGVPRVSFDLKLdITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYklvgKGKF 151
Cdd:PTZ00149 127 KSYCNDESTGKLEIVSDDLSC-LKDKHVLIVEDIIDTGNTLVKFCEYLKKFEPKTIRIATLFEKRTPLSNGF----KGDF 201
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15217571  152 ySGFECPDEFVVGYGMDFAEQYRNLSYIGVLKPE 185
Cdd:PTZ00149 202 -VGFSIPDHFVVGYCLDYNEHFRDLDHVAVLNDE 234
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
32-156 5.07e-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: 5.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571  32 FSGDSEETPIFVGVATGACLFLADLVRRIDLPIaiDFIRAESYGSGTVSSGVPRVSFDLKLDITNKHVVLVEDIVDTGNT 111
Cdd:cd06223   9 IREDLLEPDVVVGILRGGLPLAAALARALGLPL--AFIRKERKGPGRTPSEPYGLELPLGGDVKGKRVLLVDDVIATGGT 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15217571 112 LSCLIEHMKAKKASSVSVCTLLDKPSRRKVHYKLVGKgKFYSGFE 156
Cdd:cd06223  87 LLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD-PVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
40-169 8.91e-22

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: 86.26  E-value: 8.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571    40 PIFVGVATGACLFLADLVRRIDLPIAidFIRAESYGSGTVSSGVPRvsfDLKLDITNKHVVLVEDIVDTGNTLSCLIEHM 119
Cdd:pfam00156  31 DVVVGILRGGLPFAGILARRLDVPLA--FVRKVSYNPDTSEVMKTS---SALPDLKGKTVLIVDDILDTGGTLLKVLELL 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 15217571   120 KAKKASSVSVCTLLDKPSRRKVHYKLVGKGKFysgfecPDEFVVGYGMDF 169
Cdd:pfam00156 106 KNVGPKEVKIAVLIDKPAGTEPKDKYDKRVDD------WIVFVVGFGLDE 149
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
5-143 2.65e-14

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: 66.79  E-value: 2.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217571   5 KHIEKVLFSDEVIAHRVNQLGIDITsdfsgDSEETPIF-VGVATGAcLFLADLV-RRIDLPiAIDFIRAESYGSGTVSSG 82
Cdd:COG2236   2 DKFKKEYLSWDEIHELSRRLAEQIL-----ESGFRPDViVAIARGG-LVPARILaDALGVP-DLASIRVSSYTGTAKRLE 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15217571  83 VPRVSFDLKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDKP-SRRKVHY 143
Cdd:COG2236  75 EPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRTAVLYYKPsSKFKPDY 136
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
93-130 2.36e-05

Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; Phosphoribosylpyrophosphate synthetase is part of the Pathway/BioSystem: Histidine biosynthesis, Purine biosynthesis


Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 43.51  E-value: 2.36e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15217571  93 DITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVC 130
Cdd:COG0462 208 DVEGKTCIIVDDMIDTGGTLVEAAEALKEAGAKSVYAA 245
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
93-130 9.76e-05

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 41.64  E-value: 9.76e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15217571   93 DITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVC 130
Cdd:PRK01259 205 DVEGRDCILVDDMIDTAGTLCKAAEALKERGAKSVYAY 242
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
93-132 3.73e-04

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 39.42  E-value: 3.73e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 15217571  93 DITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTL 132
Cdd:COG1040 152 RLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLVL 191
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
89-131 1.22e-03

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: 38.41  E-value: 1.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15217571    89 DLKLDITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCT 131
Cdd:TIGR01251 203 NLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAKRVIAAA 245
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
93-135 1.23e-03

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 37.93  E-value: 1.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15217571   93 DITNKHVVLVEDIVDTGNTLSCLIEHMKAKKASSVSVCTLLDK 135
Cdd:PRK02277 137 SVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDK 179
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
78-143 6.85e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 35.72  E-value: 6.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15217571   78 TVSSGVPRVsfdLKLD------ITNKHVVLVEDIVDTGNTL---SCLIEHMKAKKASSVSVCTLLDKPSRRKVHY 143
Cdd:PRK07322  99 SITTGKPQL---LVLDgadaekLKGKRVAIVDDVVSTGGTLtalERLVERAGGQVVAKAAIFAEGDASNRLDVIY 170
 
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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