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Conserved domains on  [gi|1936181336|gb|QPI14185|]
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ribose-phosphate pyrophosphokinase [Salmonella phage GEC_vB_B1]

Protein Classification

ribose-phosphate diphosphokinase( domain architecture ID 1000637)

ribose-phosphate diphosphokinase catalyzes the transfer of the pyrophosphoryl group from ATP to the 1-hydroxyl of ribose-5-phosphate to form the the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP)

CATH:  3.40.50.2020
EC:  2.7.6.1
Gene Ontology:  GO:0005524|GO:0002189|GO:0016301|GO:0016310|GO:0004749
PubMed:  11751055

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PrsA super family cl33889
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 87-292 1.45e-34

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


The actual alignment was detected with superfamily member COG0462:

Pssm-ID: 440230 [Multi-domain]  Cd Length: 311  Bit Score: 127.10  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYDRhMFK-GDAAALKVFAQQVNAMGFDAVCAVDPHSyvpDNLFNCFqSIPqkeiAVH-YANDPLIDYL- 163
Cdd:COG0462    86 TAVIPYYGYARQDR-KFRpREPITAKLVADLLEAAGADRVLTVDLHA---PQIQGFF-DIP----VDHlYAAPLLADYIk 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 164 ---------VAPDAGASKKIAETAKEVDKPYITMSKVRnLKTGEITGMRILDDVDltDKTVMILDDICDGGRTFVEAAKH 234
Cdd:COG0462   157 skdledlvvVSPDVGGVKRARAFAKRLGAPLAIIDKRR-PGANEVEVMNIIGDVE--GKTCIIVDDMIDTGGTLVEAAEA 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1936181336 235 LREAGAKRVELYVTHGIFSKD-VENLLDNGIDHIYTTNSLGEAKDRGLTHYSQVTVANL 292
Cdd:COG0462   234 LKEAGAKSVYAAATHGVLSGPaVERLENSPIDELVVTDTIPLPEEKRCDKIKVLSVAPL 292
 
Name Accession Description Interval E-value
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 87-292 1.45e-34

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: 127.10  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYDRhMFK-GDAAALKVFAQQVNAMGFDAVCAVDPHSyvpDNLFNCFqSIPqkeiAVH-YANDPLIDYL- 163
Cdd:COG0462    86 TAVIPYYGYARQDR-KFRpREPITAKLVADLLEAAGADRVLTVDLHA---PQIQGFF-DIP----VDHlYAAPLLADYIk 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 164 ---------VAPDAGASKKIAETAKEVDKPYITMSKVRnLKTGEITGMRILDDVDltDKTVMILDDICDGGRTFVEAAKH 234
Cdd:COG0462   157 skdledlvvVSPDVGGVKRARAFAKRLGAPLAIIDKRR-PGANEVEVMNIIGDVE--GKTCIIVDDMIDTGGTLVEAAEA 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1936181336 235 LREAGAKRVELYVTHGIFSKD-VENLLDNGIDHIYTTNSLGEAKDRGLTHYSQVTVANL 292
Cdd:COG0462   234 LKEAGAKSVYAAATHGVLSGPaVERLENSPIDELVVTDTIPLPEEKRCDKIKVLSVAPL 292
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 87-292 1.60e-30

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: 116.22  E-value: 1.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYDRHMFKGDAAALKVFAQQVNAMGFDAVCAVDPHSyvpDNLFNCFqSIP------QKEIAVHYANDPLI 160
Cdd:TIGR01251  84 TAVIPYYGYARQDKKFKSREPISAKLVANLLETAGADRVLTVDLHS---PQIQGFF-DVPvdnlyaSPVLAEYLKKKILD 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 161 D-YLVAPDAGASKKIAETAKEVDKPYITMSKVRNLKTGEITGMRILDDVDltDKTVMILDDICDGGRTFVEAAKHLREAG 239
Cdd:TIGR01251 160 NpVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATNEVEVMNLVGDVE--GKDVVIVDDIIDTGGTIAKAAEILKSAG 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1936181336 240 AKRVELYVTHGIFSKD-VENLLDNGIDHIYTTNSLgeAKDRGLTHYSQVTVANL 292
Cdd:TIGR01251 238 AKRVIAAATHGVFSGPaIERIANAGVEEVIVTNTI--PHEKHKPKVSVISVAPL 289
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 75-292 7.83e-24

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 98.06  E-value: 7.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  75 IDDLVPRKFAMKTAIFYYLPNARYDRHMFKGDAAALKVFAQQVNAMGfDAVCAVDPHSYVPDNLFNC-FQSI-PQKEIAV 152
Cdd:PRK00934   69 IDALRDEGAKSITLVIPYLGYARQDKRFKPGEPISARAIAKIISAYY-DRIITINIHEPSILEFFPIpFINLdAAPLIAE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 153 HYANDPLIDYLVAPDAGASKKIAETAKEVDKPYITMSKVRnLKTGEITgMRILDdVDLTDKTVMILDDICDGGRTFVEAA 232
Cdd:PRK00934  148 YIGDKLDDPLVLAPDKGALELAKEAAEILGCEYDYLEKTR-ISPTEVE-IAPKN-LDVKGKDVLIVDDIISTGGTMATAI 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1936181336 233 KHLREAGAKRVELYVTHGIFSKD-VENLLDNGIDHIYTTNSLgeakdrgLTHYSQVTVANL 292
Cdd:PRK00934  225 KILKEQGAKKVYVACVHPVLVGDaILKLYNAGVDEIIVTDTL-------ESEVSKISVAPL 278
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 148-272 1.34e-18

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: 79.75  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 148 KEIAVHYANDPL-IDYLVAPDAGASKKIAETAKEVDKPYITMSKVR---NLKTGEITGMRILDDVDLTDKTVMILDDICD 223
Cdd:cd06223     3 RLLAEEIREDLLePDVVVGILRGGLPLAAALARALGLPLAFIRKERkgpGRTPSEPYGLELPLGGDVKGKRVLLVDDVIA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1936181336 224 GGRTFVEAAKHLREAGAKRVELYVTHGIFSKDvENLLDNGIDHIYTTNS 272
Cdd:cd06223    83 TGGTLLAAIELLKEAGAKVVGVAVLLDKPEGG-ARELASPGDPVYSLFT 130
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 136-249 6.86e-09

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: 53.52  E-value: 6.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 136 DNLFNCFQSIPQKEIAVhyandplidylVAPDAGASKKIAETAKEVDKPYITMSKVRNLKTGEITGMRILDDVDLTDKTV 215
Cdd:pfam00156  17 RLAAQINEDYGGKPDVV-----------VGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALPDLKGKTV 85

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1936181336 216 MILDDICDGGRTFVEAAKHLREAGAKRVELYVTH 249
Cdd:pfam00156  86 LIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLI 119
 
Name Accession Description Interval E-value
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 87-292 1.45e-34

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: 127.10  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYDRhMFK-GDAAALKVFAQQVNAMGFDAVCAVDPHSyvpDNLFNCFqSIPqkeiAVH-YANDPLIDYL- 163
Cdd:COG0462    86 TAVIPYYGYARQDR-KFRpREPITAKLVADLLEAAGADRVLTVDLHA---PQIQGFF-DIP----VDHlYAAPLLADYIk 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 164 ---------VAPDAGASKKIAETAKEVDKPYITMSKVRnLKTGEITGMRILDDVDltDKTVMILDDICDGGRTFVEAAKH 234
Cdd:COG0462   157 skdledlvvVSPDVGGVKRARAFAKRLGAPLAIIDKRR-PGANEVEVMNIIGDVE--GKTCIIVDDMIDTGGTLVEAAEA 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1936181336 235 LREAGAKRVELYVTHGIFSKD-VENLLDNGIDHIYTTNSLGEAKDRGLTHYSQVTVANL 292
Cdd:COG0462   234 LKEAGAKSVYAAATHGVLSGPaVERLENSPIDELVVTDTIPLPEEKRCDKIKVLSVAPL 292
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 87-292 1.60e-30

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: 116.22  E-value: 1.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYDRHMFKGDAAALKVFAQQVNAMGFDAVCAVDPHSyvpDNLFNCFqSIP------QKEIAVHYANDPLI 160
Cdd:TIGR01251  84 TAVIPYYGYARQDKKFKSREPISAKLVANLLETAGADRVLTVDLHS---PQIQGFF-DVPvdnlyaSPVLAEYLKKKILD 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 161 D-YLVAPDAGASKKIAETAKEVDKPYITMSKVRNLKTGEITGMRILDDVDltDKTVMILDDICDGGRTFVEAAKHLREAG 239
Cdd:TIGR01251 160 NpVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATNEVEVMNLVGDVE--GKDVVIVDDIIDTGGTIAKAAEILKSAG 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1936181336 240 AKRVELYVTHGIFSKD-VENLLDNGIDHIYTTNSLgeAKDRGLTHYSQVTVANL 292
Cdd:TIGR01251 238 AKRVIAAATHGVFSGPaIERIANAGVEEVIVTNTI--PHEKHKPKVSVISVAPL 289
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 75-292 7.83e-24

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 98.06  E-value: 7.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  75 IDDLVPRKFAMKTAIFYYLPNARYDRHMFKGDAAALKVFAQQVNAMGfDAVCAVDPHSYVPDNLFNC-FQSI-PQKEIAV 152
Cdd:PRK00934   69 IDALRDEGAKSITLVIPYLGYARQDKRFKPGEPISARAIAKIISAYY-DRIITINIHEPSILEFFPIpFINLdAAPLIAE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 153 HYANDPLIDYLVAPDAGASKKIAETAKEVDKPYITMSKVRnLKTGEITgMRILDdVDLTDKTVMILDDICDGGRTFVEAA 232
Cdd:PRK00934  148 YIGDKLDDPLVLAPDKGALELAKEAAEILGCEYDYLEKTR-ISPTEVE-IAPKN-LDVKGKDVLIVDDIISTGGTMATAI 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1936181336 233 KHLREAGAKRVELYVTHGIFSKD-VENLLDNGIDHIYTTNSLgeakdrgLTHYSQVTVANL 292
Cdd:PRK00934  225 KILKEQGAKKVYVACVHPVLVGDaILKLYNAGVDEIIVTDTL-------ESEVSKISVAPL 278
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
92-272 9.99e-21

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 89.61  E-value: 9.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  92 YLPNARYDRHMFKGDAAALKVFAQQVNAmGFDAVCAVDPHSYVPDNLFNCFqSIPQkeIAVHYAndPLI----------D 161
Cdd:PRK07199   89 YLAYMRQDIAFHPGEAISQRHFARLLSG-SFDRLVTVDPHLHRYPSLSEVY-PIPA--VVLSAA--PAIaawirahvprP 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 162 YLVAPDAGASKKIAETAKEVDKPYITMSKVR-NLKTGEITgmrILDDVDLTDKTVMILDDICDGGRTFVEAAKHLREAGA 240
Cdd:PRK07199  163 LLIGPDEESEQWVAAVAERAGAPHAVLRKTRhGDRDVEIS---LPDAAPWAGRTPVLVDDIVSTGRTLIEAARQLRAAGA 239

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1936181336 241 KRVELYVTHGIFSKD-VENLLDNGIDHIYTTNS 272
Cdd:PRK07199  240 ASPDCVVVHALFAGDaYSALAAAGIARVVSTDT 272
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
87-292 1.12e-19

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 86.71  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYDRHMFKGDAAALKVFAQQVNAMGFDAVCAVDPHS-------YVP-DNLFncFQSIPQKEIAVHYANDP 158
Cdd:PRK01259   83 TAVIPYFGYARQDRKARSRVPITAKLVANLLETAGADRVLTMDLHAdqiqgffDIPvDNLY--GSPILLEDIKQKNLENL 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 159 LIdylVAPDAGASKKIAETAKEVDKPYITMSKvRNLKTGEITGMRILDDVDltDKTVMILDDICDGGRTFVEAAKHLREA 238
Cdd:PRK01259  161 VV---VSPDVGGVVRARALAKRLDADLAIIDK-RRPRANVSEVMNIIGDVE--GRDCILVDDMIDTAGTLCKAAEALKER 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1936181336 239 GAKRVELYVTHGIFSKD-VENLLDNGIDHIYTTNSLG-EAKDRGLTHYSQVTVANL 292
Cdd:PRK01259  235 GAKSVYAYATHPVLSGGaIERIENSVIDELVVTDSIPlSEEAKKCDKIRVLSVAPL 290
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 148-272 1.34e-18

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: 79.75  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 148 KEIAVHYANDPL-IDYLVAPDAGASKKIAETAKEVDKPYITMSKVR---NLKTGEITGMRILDDVDLTDKTVMILDDICD 223
Cdd:cd06223     3 RLLAEEIREDLLePDVVVGILRGGLPLAAALARALGLPLAFIRKERkgpGRTPSEPYGLELPLGGDVKGKRVLLVDDVIA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1936181336 224 GGRTFVEAAKHLREAGAKRVELYVTHGIFSKDvENLLDNGIDHIYTTNS 272
Cdd:cd06223    83 TGGTLLAAIELLKEAGAKVVGVAVLLDKPEGG-ARELASPGDPVYSLFT 130
PRK04923 PRK04923
ribose-phosphate diphosphokinase;
75-292 5.49e-16

ribose-phosphate diphosphokinase;


Pssm-ID: 179893 [Multi-domain]  Cd Length: 319  Bit Score: 76.89  E-value: 5.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  75 IDDLVPRKFAMKTAIFYYLPNARYDRHMFKGDAA-ALKVFAQQVNAMGFDAVCAVDPHSYVPDNLF-----NCFQS-IPQ 147
Cdd:PRK04923   77 IDALKRASAASVTAVIPYFGYSRQDRRMRSSRVPiTAKVAAKMISAMGADRVLTVDLHADQIQGFFdvpvdNVYASpLLL 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 148 KEIAVHYANDPLIdyLVAPDAGASKKIAETAKEVDKPYITMSKVRNLKTGEITGMRILDDVDltDKTVMILDDICDGGRT 227
Cdd:PRK04923  157 ADIWRAYGTDNLI--VVSPDVGGVVRARAVAKRLDDADLAIIDKRRPRANVATVMNIIGDVQ--GKTCVLVDDLVDTAGT 232

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1936181336 228 FVEAAKHLREAGAKRVELYVTHGIFS-KDVENLLDNGIDHIYTTNS--LGEAKdRGLTHYSQVTVANL 292
Cdd:PRK04923  233 LCAAAAALKQRGALKVVAYITHPVLSgPAVDNINNSQLDELVVTDTipLSEAA-RACAKIRQLSVAEL 299
PLN02369 PLN02369
ribose-phosphate pyrophosphokinase
 87-292 1.29e-15

ribose-phosphate pyrophosphokinase


Pssm-ID: 215209 [Multi-domain]  Cd Length: 302  Bit Score: 75.50  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYDRHMFKGDAAALKVFAQQVNAMGFDAVCAVDPHSYVPDNLFncfqSIPQKEIavhYANDPLIDYL--- 163
Cdd:PLN02369   74 TAVIPYFGYARADRKTQGRESIAAKLVANLITEAGADRVLACDLHSGQSMGYF----DIPVDHV---YGQPVILDYLask 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 164 ---------VAPDAGASKKIAETAKEV-DKPYITMSKVRNlKTGEITGMRILDDVDltDKTVMILDDICDGGRTFVEAAK 233
Cdd:PLN02369  147 tisspdlvvVSPDVGGVARARAFAKKLsDAPLAIVDKRRQ-GHNVAEVMNLIGDVK--GKVAIMVDDMIDTAGTITKGAA 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 234 HLREAGAKRVELYVTHGIFSKDVENLLDNGI-DHIYTTNSLGEAKDRGLTHYSQVTVANL 292
Cdd:PLN02369  224 LLHQEGAREVYACATHAVFSPPAIERLSSGLfQEVIVTNTIPVSEKNYFPQLTVLSVANL 283
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 87-292 7.20e-15

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 73.62  E-value: 7.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYDRHMFKGDAAALKVFAQQVNAMGFDAVCAVDPHSYVPDNLFNcfqsIPQKEIavhYANDPLIDYL--- 163
Cdd:PRK02812  104 TAVIPYYGYARADRKTAGRESITAKLVANLITKAGADRVLAMDLHSAQIQGYFD----IPCDHV---YGSPVLLDYLask 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 164 -------VAPDAGASKKIAETAKEV-DKPYITMSKVRNL-KTGEItgMRILDDVDltDKTVMILDDICDGGRTFVEAAKH 234
Cdd:PRK02812  177 nledivvVSPDVGGVARARAFAKKLnDAPLAIIDKRRQAhNVAEV--LNVIGDVK--GKTAILVDDMIDTGGTICEGARL 252

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1936181336 235 LREAGAKRVELYVTHGIFS-KDVENLLDNGIDHIYTTNSLGEAKDRGLTHYSQVTVANL 292
Cdd:PRK02812  253 LRKEGAKQVYACATHAVFSpPAIERLSSGLFEEVIVTNTIPVPEERRFPQLKVLSVANM 311
PTZ00145 PTZ00145
phosphoribosylpyrophosphate synthetase; Provisional
 87-253 4.49e-14

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 240290 [Multi-domain]  Cd Length: 439  Bit Score: 71.83  E-value: 4.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYDRHMFKGDAAALKVFAQQVNAMGFDAVCAVDPHS---------YVP-DNLfncfqsiPQKEIAVHY-- 154
Cdd:PTZ00145  202 TAVIPYYGYARQDRKLSSRVPISAADVARMIEAMGVDRVVAIDLHSgqiqgffgpRVPvDNL-------EAQLIGLDYft 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 155 ANDPLIDYLVAPDAGA---SKKIAE--TAKEVDKPYITMSKVRNLKTGEITGMRILDDVdlTDKTVMILDDICDGGRTFV 229
Cdd:PTZ00145  275 KKDLYKPVIVSPDAGGvyrARKFQDglNHRGISDCGIAMLIKQRTKPNEIEKMDLVGNV--YDSDVIIVDDMIDTSGTLC 352

                         170       180
                  ....*....|....*....|....
gi 1936181336 230 EAAKHLREAGAKRVELYVTHGIFS 253
Cdd:PTZ00145  353 EAAKQLKKHGARRVFAFATHGLFS 376
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
150-292 1.60e-13

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 69.59  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 150 IAVHYANDPLIdyLVAPDAGaSKKIAE--TAKEVDKPYITMSKVRN-LKTGEITGMRILDDVDltDKTVMILDDICDGGR 226
Cdd:PRK03092  141 VRDKYDLDNVT--VVSPDAG-RVRVAEqwADRLGGAPLAFIHKTRDpTVPNQVVANRVVGDVE--GRTCVLVDDMIDTGG 215

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1936181336 227 TFVEAAKHLREAGAKRVELYVTHGIFSK-DVENLLDNGIDHIYTTNSLGEAKDRGLTHYSQVTVANL 292
Cdd:PRK03092  216 TIAGAVRALKEAGAKDVIIAATHGVLSGpAAERLKNCGAREVVVTDTLPIPEEKRFDKLTVLSIAPL 282
PRK00553 PRK00553
ribose-phosphate pyrophosphokinase; Provisional
 74-292 4.91e-13

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 179062 [Multi-domain]  Cd Length: 332  Bit Score: 68.40  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  74 AIDDLVPRKFAMKTAIFYYLPNARYDRHMFKGDAAALKVFAQQVNAMGFDAVCAVDPHSYVPDNLFNcfqsIPQKEIAVH 153
Cdd:PRK00553   79 AIDALKRGSAKSITAILPYYGYARQDRKTAGREPITSKLVADLLTKAGVTRVTLTDIHSDQTQGFFD----IPVDILRTY 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 154 Y----------ANDPLIdyLVAPDAGASKKIAETAKEVDKPYITMSKvRNLKTGEITGMRILDDVdlTDKTVMILDDICD 223
Cdd:PRK00553  155 HvflsrvlellGKKDLV--VVSPDYGGVKRARLIAESLELPLAIIDK-RRPKHNVAESINVLGEV--KNKNCLIVDDMID 229

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1936181336 224 GGRTFVEAAKHLREAGAKRVELYVTHGIFSKDVENLLDNG-----IDHIYTTNSLGEAKDRGLTHYSQVTVANL 292
Cdd:PRK00553  230 TGGTVIAAAKLLKKQKAKKVCVMATHGLFNKNAIQLFDEAfkkklIDKLFVSNSIPQTKFEKKPQFKVVDLAHL 303
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 133-272 1.04e-11

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 64.33  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 133 YVPDNLFNCFQS-IP---QKEIAVHYANDPLIDYlvaPDAGASKKIAETAKEVdkPYITMSKVRN-------LKTGEITG 201
Cdd:PLN02297  156 YFGDNVLPCFESgIPllkKRLQQLPDSDNIVIAF---PDDGAWKRFHKQFEHF--PMVVCTKVREgdkrivrIKEGNPAG 230

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1936181336 202 mrilddvdltdKTVMILDDICDGGRTFVEAAKHLREAGAKRVELYVTHGIFSKDV-------ENLLDNGIDHIYTTNS 272
Cdd:PLN02297  231 -----------RHVVIVDDLVQSGGTLIECQKVLAAHGAAKVSAYVTHGVFPNESwerfthdNGGPEAGFAYFWITDS 297
PRK02269 PRK02269
ribose-phosphate diphosphokinase;
92-292 5.76e-09

ribose-phosphate diphosphokinase;


Pssm-ID: 167353 [Multi-domain]  Cd Length: 320  Bit Score: 55.95  E-value: 5.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  92 YLPNARYDRHMFKGDAAALKVFAQQVNAMGFDAVCAVDPHSYVPDNLFNcfqsIPQKeiavHYANDPLI-DY-------- 162
Cdd:PRK02269   93 YYGYARQDRKARSREPITSKLVANMLEVAGVDRLLTVDLHAAQIQGFFD----IPVD----HLMGAPLIaDYfdrrglvg 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 163 ----LVAPDAGASKKIAETAKEVDKPYITMSKVRN---LKTGEItgMRILDDVDltDKTVMILDDICDGGRTFVEAAKHL 235
Cdd:PRK02269  165 ddvvVVSPDHGGVTRARKLAQFLKTPIAIIDKRRSvdkMNTSEV--MNIIGNVK--GKKCILIDDMIDTAGTICHAADAL 240

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1936181336 236 REAGAKRVELYVTHGIFSKD-VENLLDNGIDHIYTTNSLGEAKDRGLTHYSQVTVANL 292
Cdd:PRK02269  241 AEAGATEVYASCTHPVLSGPaLDNIQKSAIEKLVVLDTIYLPEERLIDKIEQISIADL 298
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 136-249 6.86e-09

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: 53.52  E-value: 6.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 136 DNLFNCFQSIPQKEIAVhyandplidylVAPDAGASKKIAETAKEVDKPYITMSKVRNLKTGEITGMRILDDVDLTDKTV 215
Cdd:pfam00156  17 RLAAQINEDYGGKPDVV-----------VGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKTSSALPDLKGKTV 85

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1936181336 216 MILDDICDGGRTFVEAAKHLREAGAKRVELYVTH 249
Cdd:pfam00156  86 LIVDDILDTGGTLLKVLELLKNVGPKEVKIAVLI 119
Pribosyl_synth pfam14572
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ...
 209-273 1.09e-08

Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes from class EC:2.7.6.1, phosphoribosyl-pyrophosphate transferase.


Pssm-ID: 434046  Cd Length: 184  Bit Score: 53.67  E-value: 1.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1936181336 209 DLTDKTVMILDDICDGGRTFVEAAKHLREAGAKRVELYVTHGIFSKDVENLLDNG-IDHIYTTNSL 273
Cdd:pfam14572  80 DVGGRIAIIVDDMIDDVDSFVAAAELLKERGAYKIYVMATHGLLSSDAPRLLEASpIDEVVVTNTI 145
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 92-273 2.86e-08

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 53.97  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  92 YLPNARYDRHMFKGDAAALKVFAQQVNAMGFDAVCAVDPHSY-------VP-DNLFncfqSIPQkeIAVHYANDPLID-- 161
Cdd:PRK02458   97 YFGYARQDRIAKPREPITAKLVANMLVKAGVDRVLTLDLHAVqvqgffdIPvDNLF----TVPL--FAKHYCKKGLSGsd 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 162 -YLVAPDAGASKKIAETAKEVDKP-----YITMSKVRNlkTGEITGmrilddvDLTDKTVMILDDICDGGRTFVEAAKHL 235
Cdd:PRK02458  171 vVVVSPKNSGIKRARSLAEYLDAPiaiidYAQDDSERE--EGYIIG-------DVAGKKAILIDDILNTGKTFAEAAKIV 241

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1936181336 236 REAGAKRVELYVTHGIFSKDVENLLDNG-IDHIYTTNSL 273
Cdd:PRK02458  242 EREGATEIYAVASHGLFAGGAAEVLENApIKEILVTDSV 280
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 87-271 2.40e-07

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 51.49  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336  87 TAIFYYLPNARYD-RHMFKGDAAALkvFAQQVNAMGFDAVCAVDPHSYVPDNLFNC------------FQSIPQKEIAVH 153
Cdd:PRK06827  126 TVIMPFLYESRQHkRKGRESLDCAL--ALQELEELGVDNIITFDAHDPRIENAIPLmgfenlypsyqiIKALLKNEKDLE 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1936181336 154 YANDPLIdyLVAPDAGA-----------SKKIAETAKEVDkpYITMSKVRNlktgEITGMRILDDvDLTDKTVMILDDIC 222
Cdd:PRK06827  204 IDKDHLM--VISPDTGAmdrakyyasvlGVDLGLFYKRRD--YSRVVNGRN----PIVAHEFLGR-DVEGKDVLIVDDMI 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1936181336 223 DGGRTFVEAAKHLREAGAKRVELYVTHGIFSKDVENL---LDNG-IDHIYTTN 271
Cdd:PRK06827  275 ASGGSMIDAAKELKSRGAKKIIVAATFGFFTNGLEKFdkaYEEGyFDRIIGTN 327
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 196-244 3.70e-06

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: 46.17  E-value: 3.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1936181336 196 TGEItgmRILDDV--DLTDKTVMILDDICDGGRTFVEAAKHLREAGAKRVE 244
Cdd:COG0634    76 SGEV---RILKDLdeDIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVK 123
PRK09162 PRK09162
hypoxanthine-guanine phosphoribosyltransferase; Provisional
 180-247 3.21e-05

hypoxanthine-guanine phosphoribosyltransferase; Provisional


Pssm-ID: 181675  Cd Length: 181  Bit Score: 43.70  E-value: 3.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1936181336 180 EVDkpYITMSKVRNLKTGEITGMRILDDVDLTDKTVMILDDICDGGRTFVEAAKHLREAGAKRVELYV 247
Cdd:PRK09162   67 EFD--YLHATRYRNETTGGELVWKVKPRESLKGRTVLVVDDILDEGHTLAAIRDRCLEMGAAEVYSAV 132
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 202-247 1.40e-04

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 42.12  E-value: 1.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1936181336 202 MRILDDVDLTDKTVMILDDICDGGRTFVEAAKHLREAGAKRVELYV 247
Cdd:COG1040   145 FAVRPPARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLV 190
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 207-243 2.22e-04

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: 40.60  E-value: 2.22e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1936181336 207 DVDLTDKTVMILDDICDGGRTFVEAAKHLREAGAKRV 243
Cdd:COG2236    83 DEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEV 119
 
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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