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Conserved domains on  [gi|1705233321|ref|WP_142589632|]
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MULTISPECIES: ribose-phosphate pyrophosphokinase [Hyphomicrobiales]

Protein Classification

ribose-phosphate pyrophosphokinase( domain architecture ID 11482623)

ribose-phosphate pyrophosphokinase 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)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
13-302 1.13e-160

ribose-phosphate diphosphokinase;


:

Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 451.31  E-value: 1.13e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  13 RRLILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARPDDGFLRLIFAADAARELGAC 92
Cdd:PRK07199    2 QPLLLALPGNEAAAGRLAAALGVEVGRIELHRFPDGESYVRLDSPVAGRTVVLVCSLDRPDEKLLPLLFAAEAARELGAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  93 QVNLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSSSFDRLLTVDPHLHRYPALSPLYTVPTDTLHAAPLLADWIAAEVDK 172
Cdd:PRK07199   82 RVGLVAPYLAYMRQDIAFHPGEAISQRHFARLLSGSFDRLVTVDPHLHRYPSLSEVYPIPAVVLSAAPAIAAWIRAHVPR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 173 PLIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSKWRGRQPVLADDIASSGNTLIEAARQLPLQGFVR 252
Cdd:PRK07199  162 PLLIGPDEESEQWVAAVAERAGAPHAVLRKTRHGDRDVEISLPDAAPWAGRTPVLVDDIVSTGRTLIEAARQLRAAGAAS 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1705233321 253 PVVAVVHAIFADDSFQRLV-PLCNRIVSTDSVPHESNAVALAPLIGNVIAS 302
Cdd:PRK07199  242 PDCVVVHALFAGDAYSALAaAGIARVVSTDTVPHPSNAISLAPLLAEALRR 292
 
Name Accession Description Interval E-value
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
13-302 1.13e-160

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 451.31  E-value: 1.13e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  13 RRLILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARPDDGFLRLIFAADAARELGAC 92
Cdd:PRK07199    2 QPLLLALPGNEAAAGRLAAALGVEVGRIELHRFPDGESYVRLDSPVAGRTVVLVCSLDRPDEKLLPLLFAAEAARELGAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  93 QVNLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSSSFDRLLTVDPHLHRYPALSPLYTVPTDTLHAAPLLADWIAAEVDK 172
Cdd:PRK07199   82 RVGLVAPYLAYMRQDIAFHPGEAISQRHFARLLSGSFDRLVTVDPHLHRYPSLSEVYPIPAVVLSAAPAIAAWIRAHVPR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 173 PLIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSKWRGRQPVLADDIASSGNTLIEAARQLPLQGFVR 252
Cdd:PRK07199  162 PLLIGPDEESEQWVAAVAERAGAPHAVLRKTRHGDRDVEISLPDAAPWAGRTPVLVDDIVSTGRTLIEAARQLRAAGAAS 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1705233321 253 PVVAVVHAIFADDSFQRLV-PLCNRIVSTDSVPHESNAVALAPLIGNVIAS 302
Cdd:PRK07199  242 PDCVVVHALFAGDAYSALAaAGIARVVSTDTVPHPSNAISLAPLLAEALRR 292
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 13-300 1.28e-100

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: 298.90  E-value: 1.28e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  13 RRLILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGA 91
Cdd:COG0462     3 DLKIFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPvNDNLMELLIMIDALKRASA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  92 CQVNLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSSS-FDRLLTVDPHLHRYPAlspLYTVPTDTLHAAPLLADWIAA-E 169
Cdd:COG0462    83 RRITAVIPYYGYARQDRKFRPREPITAKLVADLLEAAgADRVLTVDLHAPQIQG---FFDIPVDHLYAAPLLADYIKSkD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 170 VDKPLIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSkWRGRQPVLADDIASSGNTLIEAARQLPLQG 249
Cdd:COG0462   160 LEDLVVVSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGD-VEGKTCIIVDDMIDTGGTLVEAAEALKEAG 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1705233321 250 FVRPVVAVVHAIFADDSFQRLV-PLCNRIVSTDSVPHE-------SNAVALAPLIGNVI 300
Cdd:COG0462   239 AKSVYAAATHGVLSGPAVERLEnSPIDELVVTDTIPLPeekrcdkIKVLSVAPLLAEAI 297
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 16-301 4.19e-68

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: 215.99  E-value: 4.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  16 ILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVC--TLARPDDGFLRLIFAADAARELGACQ 93
Cdd:TIGR01251   3 IFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIQqsTSAPVNDNLMELLIMIDALKRASAKS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  94 VNLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSS-SFDRLLTVDPHLhryPALSPLYTVPTDTLHAAPLLADWIAAEVDK 172
Cdd:TIGR01251  83 ITAVIPYYGYARQDKKFKSREPISAKLVANLLETaGADRVLTVDLHS---PQIQGFFDVPVDNLYASPVLAEYLKKKILD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 173 -PLIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSKWRGRQPVLADDIASSGNTLIEAARQLPLQGFV 251
Cdd:TIGR01251 160 nPVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAK 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1705233321 252 RPVVAVVHAIFADDSFQRLVPLC-NRIVSTDSVPHESNA-----VALAPLIGNVIA 301
Cdd:TIGR01251 240 RVIAAATHGVFSGPAIERIANAGvEEVIVTNTIPHEKHKpkvsvISVAPLIAEAIR 295
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 16-128 7.77e-21

N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.


Pssm-ID: 433483 [Multi-domain]  Cd Length: 117  Bit Score: 86.32  E-value: 7.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  16 ILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQV 94
Cdd:pfam13793   3 IFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPvNDNLMELLIMIDALKRASAKRI 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1705233321  95 NLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSSS 128
Cdd:pfam13793  83 TAVIPYFGYARQDRKDKPREPITAKLVADLLEAA 116
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 158-282 1.07e-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: 67.04  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 158 AAPLLADWIAAEVDKP-LIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSKW-----RGRQPVLADDI 231
Cdd:cd06223     1 AGRLLAEEIREDLLEPdVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPlggdvKGKRVLLVDDV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1705233321 232 ASSGNTLIEAARQLPLQGFVRPVVAVVHAIFADDSFQRLVPLCnRIVSTDS 282
Cdd:cd06223    81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD-PVYSLFT 130
 
Name Accession Description Interval E-value
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
13-302 1.13e-160

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 451.31  E-value: 1.13e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  13 RRLILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARPDDGFLRLIFAADAARELGAC 92
Cdd:PRK07199    2 QPLLLALPGNEAAAGRLAAALGVEVGRIELHRFPDGESYVRLDSPVAGRTVVLVCSLDRPDEKLLPLLFAAEAARELGAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  93 QVNLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSSSFDRLLTVDPHLHRYPALSPLYTVPTDTLHAAPLLADWIAAEVDK 172
Cdd:PRK07199   82 RVGLVAPYLAYMRQDIAFHPGEAISQRHFARLLSGSFDRLVTVDPHLHRYPSLSEVYPIPAVVLSAAPAIAAWIRAHVPR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 173 PLIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSKWRGRQPVLADDIASSGNTLIEAARQLPLQGFVR 252
Cdd:PRK07199  162 PLLIGPDEESEQWVAAVAERAGAPHAVLRKTRHGDRDVEISLPDAAPWAGRTPVLVDDIVSTGRTLIEAARQLRAAGAAS 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1705233321 253 PVVAVVHAIFADDSFQRLV-PLCNRIVSTDSVPHESNAVALAPLIGNVIAS 302
Cdd:PRK07199  242 PDCVVVHALFAGDAYSALAaAGIARVVSTDTVPHPSNAISLAPLLAEALRR 292
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 13-300 1.28e-100

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: 298.90  E-value: 1.28e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  13 RRLILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGA 91
Cdd:COG0462     3 DLKIFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPvNDNLMELLIMIDALKRASA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  92 CQVNLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSSS-FDRLLTVDPHLHRYPAlspLYTVPTDTLHAAPLLADWIAA-E 169
Cdd:COG0462    83 RRITAVIPYYGYARQDRKFRPREPITAKLVADLLEAAgADRVLTVDLHAPQIQG---FFDIPVDHLYAAPLLADYIKSkD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 170 VDKPLIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSkWRGRQPVLADDIASSGNTLIEAARQLPLQG 249
Cdd:COG0462   160 LEDLVVVSPDVGGVKRARAFAKRLGAPLAIIDKRRPGANEVEVMNIIGD-VEGKTCIIVDDMIDTGGTLVEAAEALKEAG 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1705233321 250 FVRPVVAVVHAIFADDSFQRLV-PLCNRIVSTDSVPHE-------SNAVALAPLIGNVI 300
Cdd:COG0462   239 AKSVYAAATHGVLSGPAVERLEnSPIDELVVTDTIPLPeekrcdkIKVLSVAPLLAEAI 297
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 16-300 9.60e-75

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 232.11  E-value: 9.60e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  16 ILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARPDDGFLRLIFAADAARELGACQVN 95
Cdd:PRK00934    2 IIGGSASQLLASEVARLLNTELALVETKRFPDGELYVRILGEIDGEDVVIISTTYPQDENLVELLLLIDALRDEGAKSIT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  96 LIAPYLSYMRQDRRFQPGEAVTSRSFARLVSSSFDRLLTVDPHlhrYPALSPLYTVPTDTLHAAPLLADWIAAEVDKPLI 175
Cdd:PRK00934   82 LVIPYLGYARQDKRFKPGEPISARAIAKIISAYYDRIITINIH---EPSILEFFPIPFINLDAAPLIAEYIGDKLDDPLV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 176 IGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSKwRGRQPVLADDIASSGNTLIEAARQLPLQGFVRPVV 255
Cdd:PRK00934  159 LAPDKGALELAKEAAEILGCEYDYLEKTRISPTEVEIAPKNLDV-KGKDVLIVDDIISTGGTMATAIKILKEQGAKKVYV 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1705233321 256 AVVHAIFADDSFQRL-VPLCNRIVSTDSVPHESNAVALAPLIGNVI 300
Cdd:PRK00934  238 ACVHPVLVGDAILKLyNAGVDEIIVTDTLESEVSKISVAPLIADLL 283
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 16-301 4.19e-68

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: 215.99  E-value: 4.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  16 ILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVC--TLARPDDGFLRLIFAADAARELGACQ 93
Cdd:TIGR01251   3 IFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIQqsTSAPVNDNLMELLIMIDALKRASAKS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  94 VNLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSS-SFDRLLTVDPHLhryPALSPLYTVPTDTLHAAPLLADWIAAEVDK 172
Cdd:TIGR01251  83 ITAVIPYYGYARQDKKFKSREPISAKLVANLLETaGADRVLTVDLHS---PQIQGFFDVPVDNLYASPVLAEYLKKKILD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 173 -PLIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSKWRGRQPVLADDIASSGNTLIEAARQLPLQGFV 251
Cdd:TIGR01251 160 nPVVVSPDAGGVERAKKVADALGCPLAIIDKRRISATNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAGAK 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1705233321 252 RPVVAVVHAIFADDSFQRLVPLC-NRIVSTDSVPHESNA-----VALAPLIGNVIA 301
Cdd:TIGR01251 240 RVIAAATHGVFSGPAIERIANAGvEEVIVTNTIPHEKHKpkvsvISVAPLIAEAIR 295
PRK02269 PRK02269
ribose-phosphate diphosphokinase;
16-300 7.94e-30

ribose-phosphate diphosphokinase;


Pssm-ID: 167353 [Multi-domain]  Cd Length: 320  Bit Score: 116.05  E-value: 7.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  16 ILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQV 94
Cdd:PRK02269    8 LFALSSNKELAEKVAQEIGIELGKSSVRQFSDGEIQVNIEESIRGHHVFILQSTSSPvNDNLMEILIMVDALKRASAESI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  95 NLIAPYLSYMRQDRRFQPGEAVTSRSFARLVS-SSFDRLLTVDPHLhryPALSPLYTVPTDTLHAAPLLADWI---AAEV 170
Cdd:PRK02269   88 NVVMPYYGYARQDRKARSREPITSKLVANMLEvAGVDRLLTVDLHA---AQIQGFFDIPVDHLMGAPLIADYFdrrGLVG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 171 DKPLIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDR-NVEVKLPDLSKWRGRQPVLADDIASSGNTLIEAARQLPLQG 249
Cdd:PRK02269  165 DDVVVVSPDHGGVTRARKLAQFLKTPIAIIDKRRSVDKmNTSEVMNIIGNVKGKKCILIDDMIDTAGTICHAADALAEAG 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1705233321 250 FVRPVVAVVHAIFADDSFQRL-VPLCNRIVSTDSV--PHES-----NAVALAPLIGNVI 300
Cdd:PRK02269  245 ATEVYASCTHPVLSGPALDNIqKSAIEKLVVLDTIylPEERlidkiEQISIADLLGEAI 303
PLN02369 PLN02369
ribose-phosphate pyrophosphokinase
 34-303 5.69e-28

ribose-phosphate pyrophosphokinase


Pssm-ID: 215209 [Multi-domain]  Cd Length: 302  Bit Score: 110.55  E-value: 5.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  34 GWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQVNLIAPYLSYMRQDRRFQP 112
Cdd:PLN02369   12 GLELGKITIKRFADGEIYVQLQESVRGCDVFLVQPTCPPaNENLMELLIMIDACRRASAKRITAVIPYFGYARADRKTQG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 113 GEAVTSRSFARLVSSS-FDRLLTVDPHlhrYPALSPLYTVPTDTLHAAPLLADWIAAE---VDKPLIIGPDEESDQWVSA 188
Cdd:PLN02369   92 RESIAAKLVANLITEAgADRVLACDLH---SGQSMGYFDIPVDHVYGQPVILDYLASKtisSPDLVVVSPDVGGVARARA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 189 IAARIG-APHAVLRKVRHGDRNVEV-KLpdLSKWRGRQPVLADDIASSGNTLIEAARQLPLQGfVRPVVA-VVHAIFADD 265
Cdd:PLN02369  169 FAKKLSdAPLAIVDKRRQGHNVAEVmNL--IGDVKGKVAIMVDDMIDTAGTITKGAALLHQEG-AREVYAcATHAVFSPP 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1705233321 266 SFQRLV-PLCNRIVSTDSVPH-ESNA------VALAPLIGNVIASA 303
Cdd:PLN02369  246 AIERLSsGLFQEVIVTNTIPVsEKNYfpqltvLSVANLLGETIWRV 291
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
22-300 1.28e-27

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 109.82  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  22 NEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQVNLIAPY 100
Cdd:PRK01259    9 NPELAEKIAKYLGIPLGKASVGRFSDGEISVEINENVRGKDVFIIQSTCAPtNDNLMELLIMIDALKRASAGRITAVIPY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 101 LSYMRQDRRFQPGEAVTSRSFARLVSSS-FDRLLTVDphLHRyPALSPLYTVPTDTLHAAPLLADWIAA-EVDKPLIIGP 178
Cdd:PRK01259   89 FGYARQDRKARSRVPITAKLVANLLETAgADRVLTMD--LHA-DQIQGFFDIPVDNLYGSPILLEDIKQkNLENLVVVSP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 179 DEESDQWVSAIAARIGAPHAVLRKVRHGDrNV--------EVKlpdlskwrGRQPVLADDIASSGNTLIEAARQLPLQGF 250
Cdd:PRK01259  166 DVGGVVRARALAKRLDADLAIIDKRRPRA-NVsevmniigDVE--------GRDCILVDDMIDTAGTLCKAAEALKERGA 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 251 VRPVVAVVHAIFADDSFQRLV--PLcNRIVSTDSVPHESNA--------VALAPLIGNVI 300
Cdd:PRK01259  237 KSVYAYATHPVLSGGAIERIEnsVI-DELVVTDSIPLSEEAkkcdkirvLSVAPLLAEAI 295
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 22-300 1.63e-24

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 101.74  E-value: 1.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  22 NEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQVNLIAPY 100
Cdd:PRK02812   30 NPALAQEVARYLGMDLGPMIRKRFADGELYVQIQESIRGCDVYLIQPTCAPvNDHLMELLIMVDACRRASARQITAVIPY 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 101 LSYMRQDRRFQPGEAVTSRSFARL-VSSSFDRLLTVDPHLHRypaLSPLYTVPTDTLHAAPLLADWIAA-EVDKPLIIGP 178
Cdd:PRK02812  110 YGYARADRKTAGRESITAKLVANLiTKAGADRVLAMDLHSAQ---IQGYFDIPCDHVYGSPVLLDYLASkNLEDIVVVSP 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 179 DEESDQWVSAIAARI-GAPHAVLRKVRHGDRNVEVkLPDLSKWRGRQPVLADDIASSGNTLIEAARQLPLQGFVRPVVAV 257
Cdd:PRK02812  187 DVGGVARARAFAKKLnDAPLAIIDKRRQAHNVAEV-LNVIGDVKGKTAILVDDMIDTGGTICEGARLLRKEGAKQVYACA 265

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1705233321 258 VHAIFADDSFQRLVP-LCNRIVSTDSVPHESN-------AVALAPLIGNVI 300
Cdd:PRK02812  266 THAVFSPPAIERLSSgLFEEVIVTNTIPVPEErrfpqlkVLSVANMLGEAI 316
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
26-300 1.30e-23

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 98.87  E-value: 1.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  26 ARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQVNLIAPYLSYM 104
Cdd:PRK03092    2 AEEVAKELGVEVTPTTAYDFANGEIYVRFEESVRGCDAFVLQSHTAPiNKWLMEQLIMIDALKRASAKRITVVLPFYPYA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 105 RQDRRFQPGEAVTsrsfARLVSSSF-----DRLLTVDPHLhryPALSPLYTVPTDTLHAAPLLADWIAAEVDKP--LIIG 177
Cdd:PRK03092   82 RQDKKHRGREPIS----ARLVADLFktagaDRIMTVDLHT---AQIQGFFDGPVDHLFAMPLLADYVRDKYDLDnvTVVS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 178 PD----EESDQWvsaiAARIG-APHAVLRKVRHGDRNVEVKLPDL-SKWRGRQPVLADDIASSGNTLIEAARQLPLQGFV 251
Cdd:PRK03092  155 PDagrvRVAEQW----ADRLGgAPLAFIHKTRDPTVPNQVVANRVvGDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAK 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1705233321 252 RPVVAVVHAIFADDSFQRLVPLCNR-IVSTDSVPHESNA-------VALAPLIGNVI 300
Cdd:PRK03092  231 DVIIAATHGVLSGPAAERLKNCGAReVVVTDTLPIPEEKrfdkltvLSIAPLLARAI 287
PRK04923 PRK04923
ribose-phosphate diphosphokinase;
22-291 3.24e-22

ribose-phosphate diphosphokinase;


Pssm-ID: 179893 [Multi-domain]  Cd Length: 319  Bit Score: 95.38  E-value: 3.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  22 NEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLV-CTLARPDDGFLRLIFAADAARELGACQVNLIAPY 100
Cdd:PRK04923   15 NKPLAQSICKELGVRMGKALVTRFSDGEVQVEIEESVRRQEVFVIqPTCAPSAENLMELLVLIDALKRASAASVTAVIPY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 101 LSYMRQDRRFQPGEA-VTSRSFARLVSSS-FDRLLTVDPHLHRypaLSPLYTVPTDTLHAAP-LLAD-WIAAEVDKPLII 176
Cdd:PRK04923   95 FGYSRQDRRMRSSRVpITAKVAAKMISAMgADRVLTVDLHADQ---IQGFFDVPVDNVYASPlLLADiWRAYGTDNLIVV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 177 GPDEESDQWVSAIAARIG-APHAVLRKvRHGDRNVEVKLPDLSKWRGRQPVLADDIASSGNTLIEAARQLPLQGFVRPVV 255
Cdd:PRK04923  172 SPDVGGVVRARAVAKRLDdADLAIIDK-RRPRANVATVMNIIGDVQGKTCVLVDDLVDTAGTLCAAAAALKQRGALKVVA 250

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1705233321 256 AVVHAIFADDSFQRLV-PLCNRIVSTDSVPHESNAVA 291
Cdd:PRK04923  251 YITHPVLSGPAVDNINnSQLDELVVTDTIPLSEAARA 287
PRK00553 PRK00553
ribose-phosphate pyrophosphokinase; Provisional
 38-313 5.39e-21

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 179062 [Multi-domain]  Cd Length: 332  Bit Score: 91.90  E-value: 5.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  38 GAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQVNLIAPYLSYMRQDRRFQPGEAV 116
Cdd:PRK00553   34 GEIVIQKFADGETYIRFDESVRNKDVVIFQSTCSPvNDSLMELLIAIDALKRGSAKSITAILPYYGYARQDRKTAGREPI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 117 TSRSFARLVSSS-FDRLLTVDPHLHRYPAlspLYTVPTDTLHAAPLLADWIAAEVDKP--LIIGPDEESDQWVSAIAARI 193
Cdd:PRK00553  114 TSKLVADLLTKAgVTRVTLTDIHSDQTQG---FFDIPVDILRTYHVFLSRVLELLGKKdlVVVSPDYGGVKRARLIAESL 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 194 GAPHAVLRKvRHGDRNVEVKLPDLSKWRGRQPVLADDIASSGNTLIEAARQLPLQGFVRPVVAVVHAIFADDSFQRLVP- 272
Cdd:PRK00553  191 ELPLAIIDK-RRPKHNVAESINVLGEVKNKNCLIVDDMIDTGGTVIAAAKLLKKQKAKKVCVMATHGLFNKNAIQLFDEa 269

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1705233321 273 ----LCNRIVSTDSVPH-------ESNAVALAPLIGNVI---ASAASVDGDLVRH 313
Cdd:PRK00553  270 fkkkLIDKLFVSNSIPQtkfekkpQFKVVDLAHLYEEVLlcyANGGSISAIYTRH 324
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 16-128 7.77e-21

N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found N-terminal to the Pribosyltran, pfam00156.


Pssm-ID: 433483 [Multi-domain]  Cd Length: 117  Bit Score: 86.32  E-value: 7.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  16 ILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQV 94
Cdd:pfam13793   3 IFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPvNDNLMELLIMIDALKRASAKRI 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1705233321  95 NLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSSS 128
Cdd:pfam13793  83 TAVIPYFGYARQDRKDKPREPITAKLVADLLEAA 116
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 16-300 2.39e-20

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 90.18  E-value: 2.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  16 ILPLPGNEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQV 94
Cdd:PRK02458   12 LFSLNSNLEIAEKIAQAAGVPLGKLSSRQFSDGEIMINIEESVRGDDIYIIQSTSFPvNDHLWELLIMIDACKRASANTV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  95 NLIAPYLSYMRQDRRFQPGEAVTSRSFAR-LVSSSFDRLLTVDPHLHRypaLSPLYTVPTDTLHAAPLLADW---IAAEV 170
Cdd:PRK02458   92 NVVLPYFGYARQDRIAKPREPITAKLVANmLVKAGVDRVLTLDLHAVQ---VQGFFDIPVDNLFTVPLFAKHyckKGLSG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 171 DKPLIIGPDEESDQWVSAIAARIGAPHAVLRKVR-HGDRNVEVKLPDLSkwrGRQPVLADDIASSGNTLIEAARQLPLQG 249
Cdd:PRK02458  169 SDVVVVSPKNSGIKRARSLAEYLDAPIAIIDYAQdDSEREEGYIIGDVA---GKKAILIDDILNTGKTFAEAAKIVEREG 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1705233321 250 FVRPVVAVVHAIFADDSFQRL--VPLcNRIVSTDSV------PHESNAVALAPLIGNVI 300
Cdd:PRK02458  246 ATEIYAVASHGLFAGGAAEVLenAPI-KEILVTDSVatkervPKNVTYLSASELIADAI 303
PTZ00145 PTZ00145
phosphoribosylpyrophosphate synthetase; Provisional
 22-288 3.63e-18

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 240290 [Multi-domain]  Cd Length: 439  Bit Score: 84.92  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  22 NEIFARRLADEGGWELGAMETRRFPDGETYVRLLSEVKDKSVDLVCTLARP-DDGFLRLIFAADAARELGACQVNLIAPY 100
Cdd:PTZ00145  128 NPLLSKNIADHLGTILGRVHLKRFADGEVSMQFLESIRGKDVYIIQPTCPPvNENLIELLLMISTCRRASAKKITAVIPY 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 101 LSYMRQDRRFQPGEAVTSRSFARLVSS-SFDRLLTVDPHLHRYPA-LSPlyTVPTDTLHAAPLLADWIA-AEVDKPLIIG 177
Cdd:PTZ00145  208 YGYARQDRKLSSRVPISAADVARMIEAmGVDRVVAIDLHSGQIQGfFGP--RVPVDNLEAQLIGLDYFTkKDLYKPVIVS 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 178 PDE----ESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDL-SKWRGRQPVLADDIASSGNTLIEAARQLPLQGFVR 252
Cdd:PTZ00145  286 PDAggvyRARKFQDGLNHRGISDCGIAMLIKQRTKPNEIEKMDLvGNVYDSDVIIVDDMIDTSGTLCEAAKQLKKHGARR 365

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1705233321 253 PVVAVVHAIFADDSFQRL--VPLcNRIVSTDSVPHESN 288
Cdd:PTZ00145  366 VFAFATHGLFSGPAIERIeaSPL-EEVVVTDTVKSNKN 402
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 16-285 1.06e-13

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 71.14  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  16 ILPLPGNEIFA---------RRLADEGGWELGAMETR-------------RFPDGETYVRLLSEVKDKSVDLVCTLAR-- 71
Cdd:PRK06827   11 IIALPSCRELAdkvdehlvrIRERKENENIESLAFKGysresylipakfiRFSNGEAKGEILESVRGKDIYILQDVGNys 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  72 -------------PDDGFLRLIFAADAARElGACQVNLIAPYLSYMRQDRRfQPGEAVTSRSFAR-LVSSSFDRLLTVDP 137
Cdd:PRK06827   91 vtynmfgeknhmsPDDHFQDLKRTIDAIRG-KARRITVIMPFLYESRQHKR-KGRESLDCALALQeLEELGVDNIITFDA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 138 HLHRYPALSPLYTVptDTLHAA-----PLLADWIAAEVDKP--LIIGPDEESDQWVSAIAARIGAPHAVLRKVR------ 204
Cdd:PRK06827  169 HDPRIENAIPLMGF--ENLYPSyqiikALLKNEKDLEIDKDhlMVISPDTGAMDRAKYYASVLGVDLGLFYKRRdysrvv 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 205 HGD----------RNVEvklpdlskwrGRQPVLADDIASSGNTLIEAARQLPLQGFVRPVVAVVHAIFAD--DSFQRLVP 272
Cdd:PRK06827  247 NGRnpivaheflgRDVE----------GKDVLIVDDMIASGGSMIDAAKELKSRGAKKIIVAATFGFFTNglEKFDKAYE 316

                         330
                  ....*....|....*
gi 1705233321 273 --LCNRIVSTDSVPH 285
Cdd:PRK06827  317 egYFDRIIGTNLVYH 331
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 158-282 1.07e-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: 67.04  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 158 AAPLLADWIAAEVDKP-LIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKLPDLSKW-----RGRQPVLADDI 231
Cdd:cd06223     1 AGRLLAEEIREDLLEPdVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLELPlggdvKGKRVLLVDDV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1705233321 232 ASSGNTLIEAARQLPLQGFVRPVVAVVHAIFADDSFQRLVPLCnRIVSTDS 282
Cdd:cd06223    81 IATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGARELASPGD-PVYSLFT 130
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 6-294 1.30e-08

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 55.47  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321   6 KQPGTPARRLILPLPGNEIFARRLADEGG-WELGAMETRRFPDG--ETYVRLLSEVKDKSVDLVCTLARPDDGF--LRLI 80
Cdd:PLN02297    9 SSKKNKKQVHLFYCEETEELARKIAAESDaIELGSINWRKFPDGfpNLFINNAHGIRGQHVAFLASFSSPAVIFeqLSVI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321  81 FAADaarELGACQVNLIAPYLSYMRQDRRFQPGEAVTSRSFARLVSS------SFDRLLTVDPHlhrypALSPLYTVPTD 154
Cdd:PLN02297   89 YALP---KLFVASFTLVLPFFPTGTSERVEREGDVATAFTLARILSNipisrgGPTSLVIFDIH-----ALQERFYFGDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 155 TL----HAAPLLADWIAA--EVDKPLIIGPDEESdqWVSAIAARIGAPHAVLRKVRHGDRNVeVKLPDlSKWRGRQPVLA 228
Cdd:PLN02297  161 VLpcfeSGIPLLKKRLQQlpDSDNIVIAFPDDGA--WKRFHKQFEHFPMVVCTKVREGDKRI-VRIKE-GNPAGRHVVIV 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705233321 229 DDIASSGNTLIEAARQLPLQGFVRPVVAVVHAIFADDSFQRLVPLCNRIVS-------TDSVPHESNAVALAP 294
Cdd:PLN02297  237 DDLVQSGGTLIECQKVLAAHGAAKVSAYVTHGVFPNESWERFTHDNGGPEAgfayfwiTDSCPQTVKAVRGKA 309
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 152-245 2.04e-07

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: 49.67  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233321 152 PTDTLHAAPLLADWI---AAEVDK------PLIIGPDEESDQWVSAIAARIGAPHAVLRKVRHGDRNVEVKL--PDLSKW 220
Cdd:pfam00156   1 SVDEILDNPAILKAVarlAAQINEdyggkpDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDTSEVMKtsSALPDL 80

                          90       100
                  ....*....|....*....|....*
gi 1705233321 221 RGRQPVLADDIASSGNTLIEAARQL 245
Cdd:pfam00156  81 KGKTVLIVDDILDTGGTLLKVLELL 105
 
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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