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Conserved domains on  [gi|857890032|emb|CDT05386|]
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adenine phosphoribosyltransferase [Vibrio coralliirubri]

Protein Classification

purine phosphoribosyltransferase family protein( domain architecture ID 10011795)

purine phosphoribosyltransferase family protein similar to adenine phosphoribosyltransferase and hypoxanthine/guanine phosphoribosyltransferase

EC:  2.4.2.-
Gene Ontology:  GO:0106130|GO:0016757
PubMed:  11751055|7030616

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 8-180 8.59e-99

adenine phosphoribosyltransferase; Provisional


:

Pssm-ID: 235028  Cd Length: 175  Bit Score: 282.74  E-value: 8.59e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   8 LIKASIKSIPDYPKAGILFRDVTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFLFGAPLALELGVGFIPVRKPG 87
Cdd:PRK02304   5 DLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  88 KLPRQTVAQSYELEYGTDTLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQg 167
Cdd:PRK02304  85 KLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE- 163

                        170
                 ....*....|...
gi 857890032 168 lGLEVFSICEFDG 180
Cdd:PRK02304 164 -GYPVKSLVKFDG 175
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 8-180 8.59e-99

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 282.74  E-value: 8.59e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   8 LIKASIKSIPDYPKAGILFRDVTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFLFGAPLALELGVGFIPVRKPG 87
Cdd:PRK02304   5 DLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  88 KLPRQTVAQSYELEYGTDTLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQg 167
Cdd:PRK02304  85 KLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE- 163

                        170
                 ....*....|...
gi 857890032 168 lGLEVFSICEFDG 180
Cdd:PRK02304 164 -GYPVKSLVKFDG 175
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 9-178 9.62e-93

adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273437  Cd Length: 169  Bit Score: 267.22  E-value: 9.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032    9 IKASIKSIPDYPKAGILFRDVTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFLFGAPLALELGVGFIPVRKPGK 88
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   89 LPRQTVAQSYELEYGTDTLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQGL 168
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPN 160

                         170
                  ....*....|
gi 857890032  169 gLEVFSICEF 178
Cdd:TIGR01090 161 -VPVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 8-178 1.13e-80

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 236.51  E-value: 1.13e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   8 LIKASIKSIPDYPKAGILFRDVTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFLFGAPLALELGVGFIPVRKPG 87
Cdd:COG0503    2 DLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  88 KLPRQTVAQSYELEYGT-DTLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQ 166
Cdd:COG0503   82 KLPGETVSEEYDLEYGTgDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKLR 161

                        170
                 ....*....|..
gi 857890032 167 glGLEVFSICEF 178
Cdd:COG0503  162 --DYPVESLLTL 171
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 43-177 1.61e-24

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: 92.46  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  43 IDLLAETYKDMG--FTKIVGTEARGFLFGAPLALELGVGFIPVRKPGKLPRQTVAQSYELEygtdtleIHTDAIVEGDKV 120
Cdd:cd06223    2 GRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLE-------LPLGGDVKGKRV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 857890032 121 LMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEiGGDKRLQGLGLEVFSICE 177
Cdd:cd06223   75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPE-GGARELASPGDPVYSLFT 130
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
52-155 7.39e-11

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 58.01  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  52 DMGFTKIVGTEARGFLFGAPLALELGVGFIPVRK-PGKLPRQtVAQSYELEYGTDTLEIhtDAIVEGDKVLMVDDLLATG 130
Cdd:NF040646  51 DLDVDKIVTVEAMGIPIATALSLKTDIPLVIIRKrKYGLPGE-VEVHQSTGYSKGELYI--NGINKGDRVLIVDDVISTG 127

                         90       100
                 ....*....|....*....|....*
gi 857890032 131 GTIEATTKLIRQLGGVVEHAAFVIN 155
Cdd:NF040646 128 GTLIAVIKALEKAGAEIKDVVVVIE 152
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 28-158 6.07e-10

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: 55.06  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   28 DVTSLMEDPAAYKATIDLLAETYKDMGFT--KIVGTEARGFLFGAPLALELGVGFIPVRKPGKLPRQtvaqsyeleyGTD 105
Cdd:pfam00156   1 SVDEILDNPAILKAVARLAAQINEDYGGKpdVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDT----------SEV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 857890032  106 TLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPE 158
Cdd:pfam00156  71 MKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPA 123
 
Name Accession Description Interval E-value
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 8-180 8.59e-99

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 282.74  E-value: 8.59e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   8 LIKASIKSIPDYPKAGILFRDVTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFLFGAPLALELGVGFIPVRKPG 87
Cdd:PRK02304   5 DLKSSIRTIPDFPKPGILFRDITPLLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVPVRKPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  88 KLPRQTVAQSYELEYGTDTLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQg 167
Cdd:PRK02304  85 KLPRETISESYELEYGTDTLEIHKDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGAEVVGAAFVIELPDLGGREKLE- 163

                        170
                 ....*....|...
gi 857890032 168 lGLEVFSICEFDG 180
Cdd:PRK02304 164 -GYPVKSLVKFDG 175
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 9-178 9.62e-93

adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the bi-directional best hit homologs from the spirochetes from the seed for this model and making only tentative predictions of adenine phosphoribosyltransferase function for this lineage. The trusted cutoff score is made high for this reason. Most proteins scoring between the trusted and noise cutoffs are likely to act as adenine phosphotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 273437  Cd Length: 169  Bit Score: 267.22  E-value: 9.62e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032    9 IKASIKSIPDYPKAGILFRDVTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFLFGAPLALELGVGFIPVRKPGK 88
Cdd:TIGR01090   1 LKQAIRSIPDFPKKGILFRDITPLLNNPELFRFLIDLLVERYKDANIDYIVGPEARGFIFGAALAYKLGVGFVPVRKPGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   89 LPRQTVAQSYELEYGTDTLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQGL 168
Cdd:TIGR01090  81 LPGETISASYDLEYGKDVLEIHKDAIKPGQRVLIVDDLLATGGTAAATDELIKKLGGEVVEAAFLIELKDLNGRAKLEPN 160

                         170
                  ....*....|
gi 857890032  169 gLEVFSICEF 178
Cdd:TIGR01090 161 -VPVFSLLEY 169
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 8-178 1.13e-80

Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage


Pssm-ID: 440269  Cd Length: 171  Bit Score: 236.51  E-value: 1.13e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   8 LIKASIKSIPDYPKAGILFRDVTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFLFGAPLALELGVGFIPVRKPG 87
Cdd:COG0503    2 DLKDLIRDIPDFPKPGILFRDITPLLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  88 KLPRQTVAQSYELEYGT-DTLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQ 166
Cdd:COG0503   82 KLPGETVSEEYDLEYGTgDTLELHKDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIELGFLGGREKLR 161

                        170
                 ....*....|..
gi 857890032 167 glGLEVFSICEF 178
Cdd:COG0503  162 --DYPVESLLTL 171
PLN02293 PLN02293
adenine phosphoribosyltransferase
 5-167 4.39e-70

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 210.30  E-value: 4.39e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   5 KISLIKASIKSIPDYPKAGILFRDVTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFLFGAPLALELGVGFIPVR 84
Cdd:PLN02293  13 RLQGISSAIRVVPDFPKPGIMFQDITTLLLDPKAFKDTIDLFVERYRDMGISVVAGIEARGFIFGPPIALAIGAKFVPLR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  85 KPGKLPRQTVAQSYELEYGTDTLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKR 164
Cdd:PLN02293  93 KPGKLPGEVISEEYVLEYGTDCLEMHVGAVEPGERALVIDDLIATGGTLCAAINLLERAGAEVVECACVIELPELKGREK 172


                 ...
gi 857890032 165 LQG 167
Cdd:PLN02293 173 LNG 175
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
 9-179 1.74e-36

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 124.90  E-value: 1.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   9 IKASIKSIPDYPKAGIL--FRDVTSLMEdPAAYKATIDLLAEtYKDMGFTKIVGTEARGFLFGAPLALelgVGFIPVRKP 86
Cdd:PRK12560   6 LYKNARVVNSGKALTTVneFTDQLPALR-PKVLKETAKEIIK-YIDKDIDKIVTEEDKGAPLATPVSL---LSGKPLAMA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  87 GKLPRQTVAQSY-ELEYGTDTLE--IHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDK 163
Cdd:PRK12560  81 RWYPYSLSELNYnVVEIGSEYFEgvVYLNGIEKGDRVAIIDDTLSTGGTVIALIKAIENSGGIVSDVICVIEKTQNNGRK 160

                        170
                 ....*....|....*..
gi 857890032 164 RLQGL-GLEVFSICEFD 179
Cdd:PRK12560 161 KLFTQtGINVKSLVKID 177
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 43-177 1.61e-24

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: 92.46  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  43 IDLLAETYKDMG--FTKIVGTEARGFLFGAPLALELGVGFIPVRKPGKLPRQTVAQSYELEygtdtleIHTDAIVEGDKV 120
Cdd:cd06223    2 GRLLAEEIREDLlePDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLE-------LPLGGDVKGKRV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 857890032 121 LMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEiGGDKRLQGLGLEVFSICE 177
Cdd:cd06223   75 LLVDDVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPE-GGARELASPGDPVYSLFT 130
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 32-179 1.98e-17

Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440229  Cd Length: 201  Bit Score: 75.96  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  32 LMEDPAAYKATIDLLAETYKDMG--FTKIVGTEARGFLFGAPLALELGVGFIPVRKPGKlprqtvaqsyelEYGTDT-LE 108
Cdd:COG0461   39 VLSYPEALELLGEALAELIKELGpeFDAVAGPATGGIPLAAAVARALGLPAIFVRKEAK------------DHGTGGqIE 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 857890032 109 ihtDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEiGGDKRLQGLGLEVFSICEFD 179
Cdd:COG0461  107 ---GGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREE-GAAENLEEAGVPLHSLLTLD 173
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 32-179 1.24e-14

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 68.64  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  32 LMEDPAAYKATIDLLAETYKDMG--FTKIVGTEARGFLFGAPLALELGVGFIPVRKPGKlprqtvaqsyelEYGTD-TLE 108
Cdd:PRK00455  40 LLSYPEALALLGRFLAEAIKDSGieFDVVAGPATGGIPLAAAVARALDLPAIFVRKEAK------------DHGEGgQIE 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 857890032 109 IhtdAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEiGGDKRLQGLGLEVFSICEFD 179
Cdd:PRK00455 108 G---RRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQS-AAQEVFADAGVPLISLITLD 174
HPT_Archaea NF040646
hypoxanthine/guanine phosphoribosyltransferase;
52-155 7.39e-11

hypoxanthine/guanine phosphoribosyltransferase;


Pssm-ID: 468613  Cd Length: 184  Bit Score: 58.01  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  52 DMGFTKIVGTEARGFLFGAPLALELGVGFIPVRK-PGKLPRQtVAQSYELEYGTDTLEIhtDAIVEGDKVLMVDDLLATG 130
Cdd:NF040646  51 DLDVDKIVTVEAMGIPIATALSLKTDIPLVIIRKrKYGLPGE-VEVHQSTGYSKGELYI--NGINKGDRVLIVDDVISTG 127

                         90       100
                 ....*....|....*....|....*
gi 857890032 131 GTIEATTKLIRQLGGVVEHAAFVIN 155
Cdd:NF040646 128 GTLIAVIKALEKAGAEIKDVVVVIE 152
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 28-158 6.07e-10

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: 55.06  E-value: 6.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   28 DVTSLMEDPAAYKATIDLLAETYKDMGFT--KIVGTEARGFLFGAPLALELGVGFIPVRKPGKLPRQtvaqsyeleyGTD 105
Cdd:pfam00156   1 SVDEILDNPAILKAVARLAAQINEDYGGKpdVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDT----------SEV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 857890032  106 TLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPE 158
Cdd:pfam00156  71 MKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLIDKPA 123
PRK08558 PRK08558
adenine phosphoribosyltransferase; Provisional
 26-179 2.37e-08

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 181466 [Multi-domain]  Cd Length: 238  Bit Score: 51.92  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  26 FRDVTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFLFGAPLALELGVGFIPVRK---PGklprqtVAQSYE--- 99
Cdd:PRK08558  83 YVDNSSVVFDPSFLRLIAPVVAERFMGLRVDVVLTAATDGIPLAVAIASYFGADLVYAKKskeTG------VEKFYEeyq 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032 100 -LEYGTD-TLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQGLGLEVFSICE 177
Cdd:PRK08558 157 rLASGIEvTLYLPASALKKGDRVLIVDDIIRSGETQRALLDLARQAGADVVGVFFLIAVGEVGIDRAREETDAPVDALYT 236


                 ..
gi 857890032 178 FD 179
Cdd:PRK08558 237 LE 238
PRK09219 PRK09219
xanthine phosphoribosyltransferase; Validated
 47-176 3.91e-08

xanthine phosphoribosyltransferase; Validated


Pssm-ID: 181705  Cd Length: 189  Bit Score: 50.55  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032  47 AETYKDMGFTKIVGTEARGFlfgAP---LALELGVGFIPVRKpgKLPR-----QTVAQSYELEYGTD-TLEIHTDAIVEG 117
Cdd:PRK09219  43 ARRFKDEGITKILTIEASGI---APavmAALALGVPVVFAKK--KKSLtltddVYTATVYSFTKQVTsTVSVSKKFLSEG 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 857890032 118 DKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQGLGLEVFSIC 176
Cdd:PRK09219 118 DRVLIIDDFLANGQAALGLIDIIEQAGAKVAGIGIVIEKSFQDGRKLLEEKGYRVESLA 176
purR_Bsub TIGR01743
pur operon repressor, Bacillus subtilis type; This model represents the puring operon ...
 29-142 5.75e-06

pur operon repressor, Bacillus subtilis type; This model represents the puring operon repressor PurR of low-GC Gram-positive bacteria. This homodimeric repressor contains a large region homologous to phosphoribosyltransferases and is inhibited by 5-phosphoribosyl 1-pyrophosphate. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis, Regulatory functions, DNA interactions]


Pssm-ID: 130804 [Multi-domain]  Cd Length: 268  Bit Score: 45.16  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857890032   29 VTSLMEDPAAYKATIDLLAETYKDMGFTKIVGTEARGFlfgaPLALE----LGVGFIPVRKPGKLPR-QTVAQSYEleYG 103
Cdd:TIGR01743 103 LTDILGKPSILSKIGKILASVFAEREIDAVMTVATKGI----PLAYAvasvLNVPLVIVRKDSKVTEgSTVSINYV--SG 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 857890032  104 T----DTLEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQ 142
Cdd:TIGR01743 177 SsnriQTMSLAKRSLKTGSKVLIIDDFMKAGGTINGMINLLDE 219
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 105-144 2.02e-04

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 40.67  E-value: 2.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 857890032 105 DTLEIHTDAI-VEGDKVLMVDDLLATGGTIEATTKLIRQLG 144
Cdd:PRK00934 191 TEVEIAPKNLdVKGKDVLIVDDIISTGGTMATAIKILKEQG 231
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 115-144 5.87e-04

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: 39.18  E-value: 5.87e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 857890032  115 VEGDKVLMVDDLLATGGTIEATTKLIRQLG 144
Cdd:TIGR01251 208 VEGKDVVIVDDIIDTGGTIAKAAEILKSAG 237
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 113-179 1.79e-03

orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 129436 [Multi-domain]  Cd Length: 173  Bit Score: 37.41  E-value: 1.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 857890032  113 AIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVEHAAFVINLPEIGGDKRLQGL-GLEVFSICEFD 179
Cdd:TIGR00336 104 ELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQERSAGQEFEKEyGLPVISLITLK 171
PLN02541 PLN02541
uracil phosphoribosyltransferase
 112-148 2.64e-03

uracil phosphoribosyltransferase


Pssm-ID: 215297  Cd Length: 244  Bit Score: 37.07  E-value: 2.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 857890032 112 DAIVEGDKVLMVDDLLATGGTIEATTKLIRQLGGVVE 148
Cdd:PLN02541 152 DKFPEGSRVLVVDPMLATGGTIVAAIDELVSRGASVE 188
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 107-144 3.20e-03

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: 36.36  E-value: 3.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 857890032 107 LEIHTDAIVEGDKVLMVDDLLATGGTIEATTKLIRQLG 144
Cdd:COG2236   78 VKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAG 115
PRK07322 PRK07322
adenine phosphoribosyltransferase; Provisional
 115-151 8.04e-03

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 180928  Cd Length: 178  Bit Score: 35.34  E-value: 8.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 857890032 115 VEGDKVLMVDDLLATGGTIEATTKLIRQLGG-VVEHAA 151
Cdd:PRK07322 118 LKGKRVAIVDDVVSTGGTLTALERLVERAGGqVVAKAA 155
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 115-144 8.12e-03

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 36.08  E-value: 8.12e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 857890032 115 VEGDKVLMVDDLLATGGTIEATTKLIRQLG 144
Cdd:PRK06827 262 VEGKDVLIVDDMIASGGSMIDAAKELKSRG 291
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 115-144 8.74e-03

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: 35.81  E-value: 8.74e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 857890032 115 VEGDKVLMVDDLLATGGTIEATTKLIRQLG 144
Cdd:COG0462  209 VEGKTCIIVDDMIDTGGTLVEAAEALKEAG 238
 
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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