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Conserved domains on  [gi|518408537|ref|WP_019578744|]
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phosphoribosyltransferase [Pseudomonas mandelii]

Protein Classification

phosphoribosyltransferase( domain architecture ID 10004949)

phosphoribosyltransferase catalyzes the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
13-219 1.93e-102

Predicted phosphoribosyltransferase [General function prediction only];


:

Pssm-ID: 441529  Cd Length: 209  Bit Score: 295.06  E-value: 1.93e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  13 DRVDAGRSLVEPLLKYAKRaDVIVLALPRGGVPVAYEVATALEVRLDLMLVRKLGVPSHQEFAMGAIASGGIQIVNDDAL 92
Cdd:COG1926    4 DRTDAGRQLAERLAAYRGE-DPVVLALPRGGVPVAAEVARALGAPLDVLVVRKIGAPGNPELAIGAVAEDGVVVLNEDLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  93 RANGIDQRTLDAVVAKETQEMLRREQLFRASREPLVLKDQVVILIDDGLATGATMMAAIQAVRLQAPSRIVVAVPVAPME 172
Cdd:COG1926   83 RRLGISEEYIEAEKAREREELERRRRRYRGGRPPPDLKGRTVILVDDGIATGATMRAALRALRRQGPARIVVAVPVAPPD 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 518408537 173 TAEALRDEVDELICPLTPDWLVSIGYWYTDFTQTSDEEVIDLLHRAW 219
Cdd:COG1926  163 TLEELRREADEVVCLETPEPFRAVGQFYEDFPQVSDEEVIALLAQAR 209
 
Name Accession Description Interval E-value
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
13-219 1.93e-102

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 295.06  E-value: 1.93e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  13 DRVDAGRSLVEPLLKYAKRaDVIVLALPRGGVPVAYEVATALEVRLDLMLVRKLGVPSHQEFAMGAIASGGIQIVNDDAL 92
Cdd:COG1926    4 DRTDAGRQLAERLAAYRGE-DPVVLALPRGGVPVAAEVARALGAPLDVLVVRKIGAPGNPELAIGAVAEDGVVVLNEDLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  93 RANGIDQRTLDAVVAKETQEMLRREQLFRASREPLVLKDQVVILIDDGLATGATMMAAIQAVRLQAPSRIVVAVPVAPME 172
Cdd:COG1926   83 RRLGISEEYIEAEKAREREELERRRRRYRGGRPPPDLKGRTVILVDDGIATGATMRAALRALRRQGPARIVVAVPVAPPD 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 518408537 173 TAEALRDEVDELICPLTPDWLVSIGYWYTDFTQTSDEEVIDLLHRAW 219
Cdd:COG1926  163 TLEELRREADEVVCLETPEPFRAVGQFYEDFPQVSDEEVIALLAQAR 209
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 17-189 6.25e-13

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: 63.57  E-value: 6.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  17 AGRSLVEPLLKYAKRADVIVlALPRGGVPVAYEVATALEVRLDLMLVRKLGVPSHqefamgaiasggiqivnddalrang 96
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVVV-GILRGGLPLAAALARALGLPLAFIRKERKGPGRT------------------------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  97 idqrtldavvaketqemlRREQLFRASREPLVLKDQVVILIDDGLATGATMMAAIQAVRLQAPSRIVVAVPVAPMET-AE 175
Cdd:cd06223   55 ------------------PSEPYGLELPLGGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGgAR 116

                        170
                 ....*....|....
gi 518408537 176 ALRDEVDELICPLT 189
Cdd:cd06223  117 ELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 14-185 1.82e-06

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: 46.20  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537   14 RVDAGRSLVEPLLKYAKRADVIVLALPRGGVPVAYEVATALEVRLDLMLVRKlgvpshqefamgaiasggiqiVNDDAlr 93
Cdd:pfam00156  11 ILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVS---------------------YNPDT-- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537   94 angidqrtldavvaketqemlrREQLFRASREPLVlKDQVVILIDDGLATGATMMAAIQAVRLQAPSRIVVAVPVAPMET 173
Cdd:pfam00156  68 ----------------------SEVMKTSSALPDL-KGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAG 124

                         170
                  ....*....|..
gi 518408537  174 AEALRDEVDELI 185
Cdd:pfam00156 125 TEPKDKYDKRVD 136
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 126-180 1.64e-04

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 41.23  E-value: 1.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518408537 126 PLVLKDQVVILIDDGLATGATMMAAIQAVRLQAPSRIVVAVPVAPMETAEALRDE 180
Cdd:PRK00129 119 PEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCLVAAPEGIKALEEA 173
 
Name Accession Description Interval E-value
COG1926 COG1926
Predicted phosphoribosyltransferase [General function prediction only];
13-219 1.93e-102

Predicted phosphoribosyltransferase [General function prediction only];


Pssm-ID: 441529  Cd Length: 209  Bit Score: 295.06  E-value: 1.93e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  13 DRVDAGRSLVEPLLKYAKRaDVIVLALPRGGVPVAYEVATALEVRLDLMLVRKLGVPSHQEFAMGAIASGGIQIVNDDAL 92
Cdd:COG1926    4 DRTDAGRQLAERLAAYRGE-DPVVLALPRGGVPVAAEVARALGAPLDVLVVRKIGAPGNPELAIGAVAEDGVVVLNEDLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  93 RANGIDQRTLDAVVAKETQEMLRREQLFRASREPLVLKDQVVILIDDGLATGATMMAAIQAVRLQAPSRIVVAVPVAPME 172
Cdd:COG1926   83 RRLGISEEYIEAEKAREREELERRRRRYRGGRPPPDLKGRTVILVDDGIATGATMRAALRALRRQGPARIVVAVPVAPPD 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 518408537 173 TAEALRDEVDELICPLTPDWLVSIGYWYTDFTQTSDEEVIDLLHRAW 219
Cdd:COG1926  163 TLEELRREADEVVCLETPEPFRAVGQFYEDFPQVSDEEVIALLAQAR 209
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 17-189 6.25e-13

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: 63.57  E-value: 6.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  17 AGRSLVEPLLKYAKRADVIVlALPRGGVPVAYEVATALEVRLDLMLVRKLGVPSHqefamgaiasggiqivnddalrang 96
Cdd:cd06223    1 AGRLLAEEIREDLLEPDVVV-GILRGGLPLAAALARALGLPLAFIRKERKGPGRT------------------------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537  97 idqrtldavvaketqemlRREQLFRASREPLVLKDQVVILIDDGLATGATMMAAIQAVRLQAPSRIVVAVPVAPMET-AE 175
Cdd:cd06223   55 ------------------PSEPYGLELPLGGDVKGKRVLLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGgAR 116

                        170
                 ....*....|....
gi 518408537 176 ALRDEVDELICPLT 189
Cdd:cd06223  117 ELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 14-185 1.82e-06

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: 46.20  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537   14 RVDAGRSLVEPLLKYAKRADVIVLALPRGGVPVAYEVATALEVRLDLMLVRKlgvpshqefamgaiasggiqiVNDDAlr 93
Cdd:pfam00156  11 ILKAVARLAAQINEDYGGKPDVVVGILRGGLPFAGILARRLDVPLAFVRKVS---------------------YNPDT-- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518408537   94 angidqrtldavvaketqemlrREQLFRASREPLVlKDQVVILIDDGLATGATMMAAIQAVRLQAPSRIVVAVPVAPMET 173
Cdd:pfam00156  68 ----------------------SEVMKTSSALPDL-KGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPAG 124

                         170
                  ....*....|..
gi 518408537  174 AEALRDEVDELI 185
Cdd:pfam00156 125 TEPKDKYDKRVD 136
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 126-180 1.64e-04

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 41.23  E-value: 1.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518408537 126 PLVLKDQVVILIDDGLATGATMMAAIQAVRLQAPSRIVVAVPVAPMETAEALRDE 180
Cdd:PRK00129 119 PEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCLVAAPEGIKALEEA 173
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 128-155 1.06e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 38.52  E-value: 1.06e-03
                         10        20
                 ....*....|....*....|....*...
gi 518408537 128 VLKDQVVILIDDGLATGATMMAAIQAVR 155
Cdd:PRK02304 111 IKPGDRVLIVDDLLATGGTLEAAIKLLE 138
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 126-180 7.32e-03

Uracil phosphoribosyltransferase; This family includes the enzyme uracil phosphoribosyltransferase (EC:2.4.2.9). This enzyme catalyzes the first step of UMP biosynthesis.


Pssm-ID: 434124  Cd Length: 204  Bit Score: 36.32  E-value: 7.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 518408537  126 PLVLKDQVVILIDDGLATGATMMAAIQAVR-LQAP-SRIVVAVPVAPMETAEALRDE 180
Cdd:pfam14681 113 PKDISDRTVILLDPMLATGGSAIAAIQVLReHGVPeENIVVLSVIAAPEGLHRLAAA 169
 
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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