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Conserved domains on  [gi|2541200110|ref|WP_297316176|]
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ribose-phosphate diphosphokinase [Bifidobacterium indicum]

Protein Classification

ribose-phosphate pyrophosphokinase( domain architecture ID 11479877)

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
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
24-327 0e+00

ribose-phosphate diphosphokinase;


:

Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 608.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  24 LAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASAGSITAVCPLLGY 103
Cdd:PRK03092    1 LAEEVAKELGVEVTPTTAYDFANGEIYVRFEESVRGCDAFVLQSHTAPINKWLMEQLIMIDALKRASAKRITVVLPFYPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 104 SRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRMDLSKVAVVSPDAGRI 183
Cdd:PRK03092   81 ARQDKKHRGREPISARLVADLFKTAGADRIMTVDLHTAQIQGFFDGPVDHLFAMPLLADYVRDKYDLDNVTVVSPDAGRV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 184 RVAEQWAQRLGGVPLAFIHKTRDVTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIVATHGV 263
Cdd:PRK03092  161 RVAEQWADRLGGAPLAFIHKTRDPTVPNQVVANRVVGDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVIIAATHGV 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 264 MSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLFDTYP 327
Cdd:PRK03092  241 LSGPAAERLKNCGAREVVVTDTLPIPEEKRFDKLTVLSIAPLLARAIREVFEDGSVTSLFDGLA 304
 
Name Accession Description Interval E-value
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
24-327 0e+00

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 608.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  24 LAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASAGSITAVCPLLGY 103
Cdd:PRK03092    1 LAEEVAKELGVEVTPTTAYDFANGEIYVRFEESVRGCDAFVLQSHTAPINKWLMEQLIMIDALKRASAKRITVVLPFYPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 104 SRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRMDLSKVAVVSPDAGRI 183
Cdd:PRK03092   81 ARQDKKHRGREPISARLVADLFKTAGADRIMTVDLHTAQIQGFFDGPVDHLFAMPLLADYVRDKYDLDNVTVVSPDAGRV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 184 RVAEQWAQRLGGVPLAFIHKTRDVTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIVATHGV 263
Cdd:PRK03092  161 RVAEQWADRLGGAPLAFIHKTRDPTVPNQVVANRVVGDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVIIAATHGV 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 264 MSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLFDTYP 327
Cdd:PRK03092  241 LSGPAAERLKNCGAREVVVTDTLPIPEEKRFDKLTVLSIAPLLARAIREVFEDGSVTSLFDGLA 304
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 11-324 2.66e-167

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: 468.00  E-value: 2.66e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  11 KNLILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRAS 90
Cdd:COG0462     2 KDLKIFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPVNDNLMELLIMIDALKRAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  91 AGSITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRmDL 170
Cdd:COG0462    82 ARRITAVIPYYGYARQDRKFRPREPITAKLVADLLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSK-DL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 171 SKVAVVSPDAGRIRVAEQWAQRLgGVPLAFIHKTRDvtQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKA 250
Cdd:COG0462   161 EDLVVVSPDVGGVKRARAFAKRL-GAPLAIIDKRRP--GANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 251 GASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLFD 324
Cdd:COG0462   238 GAKSVYAAATHGVLSGPAVERLENSPIDELVVTDTIPLPEEKRCDKIKVLSVAPLLAEAIRRIHEGESVSSLFD 311
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 13-324 2.17e-121

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: 351.58  E-value: 2.17e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  13 LILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVL-QSHADPINKSIMEQLIMIDALKRASA 91
Cdd:TIGR01251   1 MKIFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIqQSTSAPVNDNLMELLIMIDALKRASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  92 GSITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRMDLS 171
Cdd:TIGR01251  81 KSITAVIPYYGYARQDKKFKSREPISAKLVANLLETAGADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKKILDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 172 KVaVVSPDAGRIRVAEQWAQRLgGVPLAFIHKTRDvTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAG 251
Cdd:TIGR01251 161 PV-VVSPDAGGVERAKKVADAL-GCPLAIIDKRRI-SATNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAG 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541200110 252 ASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWdgLTVLSIAPLLASAIRAVFEDGSVAKLFD 324
Cdd:TIGR01251 238 AKRVIAAATHGVFSGPAIERIANAGVEEVIVTNTIPHEKHKPK--VSVISVAPLIAEAIRRIHNNESVSSLFD 308
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 13-129 2.56e-60

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: 188.78  E-value: 2.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  13 LILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASAG 92
Cdd:pfam13793   1 LKIFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPVNDNLMELLIMIDALKRASAK 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2541200110  93 SITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAG 129
Cdd:pfam13793  81 RITAVIPYFGYARQDRKDKPREPITAKLVADLLEAAG 117
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 156-285 1.18e-21

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 88.99  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 156 AMPVLVDYVRDRMdLSKVAVVSPDAGRIRVAEQWAQRLGgVPLAFIHKTRD----VTQPNKAVAHRVVGDVKGLDCVLVD 231
Cdd:cd06223     1 AGRLLAEEIREDL-LEPDVVVGILRGGLPLAAALARALG-LPLAFIRKERKgpgrTPSEPYGLELPLGGDVKGKRVLLVD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 232 DLIDTGGTIAEACNVLRKAGASSITIVATHGVMSGPAvqRLQDCEAKEVVVTDT 285
Cdd:cd06223    79 DVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA--RELASPGDPVYSLFT 130
 
Name Accession Description Interval E-value
PRK03092 PRK03092
ribose-phosphate diphosphokinase;
24-327 0e+00

ribose-phosphate diphosphokinase;


Pssm-ID: 179535 [Multi-domain]  Cd Length: 304  Bit Score: 608.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  24 LAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASAGSITAVCPLLGY 103
Cdd:PRK03092    1 LAEEVAKELGVEVTPTTAYDFANGEIYVRFEESVRGCDAFVLQSHTAPINKWLMEQLIMIDALKRASAKRITVVLPFYPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 104 SRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRMDLSKVAVVSPDAGRI 183
Cdd:PRK03092   81 ARQDKKHRGREPISARLVADLFKTAGADRIMTVDLHTAQIQGFFDGPVDHLFAMPLLADYVRDKYDLDNVTVVSPDAGRV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 184 RVAEQWAQRLGGVPLAFIHKTRDVTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIVATHGV 263
Cdd:PRK03092  161 RVAEQWADRLGGAPLAFIHKTRDPTVPNQVVANRVVGDVEGRTCVLVDDMIDTGGTIAGAVRALKEAGAKDVIIAATHGV 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 264 MSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLFDTYP 327
Cdd:PRK03092  241 LSGPAAERLKNCGAREVVVTDTLPIPEEKRFDKLTVLSIAPLLARAIREVFEDGSVTSLFDGLA 304
PrsA COG0462
Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism]; ...
 11-324 2.66e-167

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: 468.00  E-value: 2.66e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  11 KNLILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRAS 90
Cdd:COG0462     2 KDLKIFSGNANPELAEEIAEYLGVPLGKAEVRRFSDGEIYVRIEESVRGRDVFVIQSTSPPVNDNLMELLIMIDALKRAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  91 AGSITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRmDL 170
Cdd:COG0462    82 ARRITAVIPYYGYARQDRKFRPREPITAKLVADLLEAAGADRVLTVDLHAPQIQGFFDIPVDHLYAAPLLADYIKSK-DL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 171 SKVAVVSPDAGRIRVAEQWAQRLgGVPLAFIHKTRDvtQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKA 250
Cdd:COG0462   161 EDLVVVSPDVGGVKRARAFAKRL-GAPLAIIDKRRP--GANEVEVMNIIGDVEGKTCIIVDDMIDTGGTLVEAAEALKEA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 251 GASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLFD 324
Cdd:COG0462   238 GAKSVYAAATHGVLSGPAVERLENSPIDELVVTDTIPLPEEKRCDKIKVLSVAPLLAEAIRRIHEGESVSSLFD 311
PRK01259 PRK01259
ribose-phosphate diphosphokinase;
13-324 1.73e-129

ribose-phosphate diphosphokinase;


Pssm-ID: 234929 [Multi-domain]  Cd Length: 309  Bit Score: 372.14  E-value: 1.73e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  13 LILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASAG 92
Cdd:PRK01259    1 MKLFAGNANPELAEKIAKYLGIPLGKASVGRFSDGEISVEINENVRGKDVFIIQSTCAPTNDNLMELLIMIDALKRASAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  93 SITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRmDLSK 172
Cdd:PRK01259   81 RITAVIPYFGYARQDRKARSRVPITAKLVANLLETAGADRVLTMDLHADQIQGFFDIPVDNLYGSPILLEDIKQK-NLEN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 173 VAVVSPDAGRIRVAEQWAQRLgGVPLAFIHKTRdvTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGA 252
Cdd:PRK01259  160 LVVVSPDVGGVVRARALAKRL-DADLAIIDKRR--PRANVSEVMNIIGDVEGRDCILVDDMIDTAGTLCKAAEALKERGA 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541200110 253 SSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKRW-DGLTVLSIAPLLASAIRAVFEDGSVAKLFD 324
Cdd:PRK01259  237 KSVYAYATHPVLSGGAIERIENSVIDELVVTDSIPLSEEAKKcDKIRVLSVAPLLAEAIRRISNEESVSSLFD 309
ribP_PPkin TIGR01251
ribose-phosphate pyrophosphokinase; Alternate name: phosphoribosylpyrophosphate synthetase In ...
 13-324 2.17e-121

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: 351.58  E-value: 2.17e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  13 LILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVL-QSHADPINKSIMEQLIMIDALKRASA 91
Cdd:TIGR01251   1 MKIFSGSSNQELAQKVAKNLGLPLGDVEVKRFPDGELYVRINESVRGKDVFIIqQSTSAPVNDNLMELLIMIDALKRASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  92 GSITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRMDLS 171
Cdd:TIGR01251  81 KSITAVIPYYGYARQDKKFKSREPISAKLVANLLETAGADRVLTVDLHSPQIQGFFDVPVDNLYASPVLAEYLKKKILDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 172 KVaVVSPDAGRIRVAEQWAQRLgGVPLAFIHKTRDvTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAG 251
Cdd:TIGR01251 161 PV-VVSPDAGGVERAKKVADAL-GCPLAIIDKRRI-SATNEVEVMNLVGDVEGKDVVIVDDIIDTGGTIAKAAEILKSAG 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541200110 252 ASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWdgLTVLSIAPLLASAIRAVFEDGSVAKLFD 324
Cdd:TIGR01251 238 AKRVIAAATHGVFSGPAIERIANAGVEEVIVTNTIPHEKHKPK--VSVISVAPLIAEAIRRIHNNESVSSLFD 308
PRK02812 PRK02812
ribose-phosphate pyrophosphokinase; Provisional
 13-323 4.29e-106

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235072 [Multi-domain]  Cd Length: 330  Bit Score: 313.60  E-value: 4.29e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  13 LILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASAG 92
Cdd:PRK02812   22 LRLFSGSSNPALAQEVARYLGMDLGPMIRKRFADGELYVQIQESIRGCDVYLIQPTCAPVNDHLMELLIMVDACRRASAR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  93 SITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRmDLSK 172
Cdd:PRK02812  102 QITAVIPYYGYARADRKTAGRESITAKLVANLITKAGADRVLAMDLHSAQIQGYFDIPCDHVYGSPVLLDYLASK-NLED 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 173 VAVVSPDAGRIRVAEQWAQRLGGVPLAFIHKTRdvTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGA 252
Cdd:PRK02812  181 IVVVSPDVGGVARARAFAKKLNDAPLAIIDKRR--QAHNVAEVLNVIGDVKGKTAILVDDMIDTGGTICEGARLLRKEGA 258

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541200110 253 SSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLF 323
Cdd:PRK02812  259 KQVYACATHAVFSPPAIERLSSGLFEEVIVTNTIPVPEERRFPQLKVLSVANMLGEAIWRIHEESSVSSMF 329
PRK02269 PRK02269
ribose-phosphate diphosphokinase;
12-324 4.46e-104

ribose-phosphate diphosphokinase;


Pssm-ID: 167353 [Multi-domain]  Cd Length: 320  Bit Score: 307.87  E-value: 4.46e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  12 NLILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASA 91
Cdd:PRK02269    5 DLKLFALSSNKELAEKVAQEIGIELGKSSVRQFSDGEIQVNIEESIRGHHVFILQSTSSPVNDNLMEILIMVDALKRASA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  92 GSITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDR-MDL 170
Cdd:PRK02269   85 ESINVVMPYYGYARQDRKARSREPITSKLVANMLEVAGVDRLLTVDLHAAQIQGFFDIPVDHLMGAPLIADYFDRRgLVG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 171 SKVAVVSPDAGRIRVAEQWAQRLgGVPLAFIHKTRDVTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKA 250
Cdd:PRK02269  165 DDVVVVSPDHGGVTRARKLAQFL-KTPIAIIDKRRSVDKMNTSEVMNIIGNVKGKKCILIDDMIDTAGTICHAADALAEA 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 251 GASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLFD 324
Cdd:PRK02269  244 GATEVYASCTHPVLSGPALDNIQKSAIEKLVVLDTIYLPEERLIDKIEQISIADLLGEAIIRIHEKRPLSPLFE 317
PLN02369 PLN02369
ribose-phosphate pyrophosphokinase
 22-324 4.60e-102

ribose-phosphate pyrophosphokinase


Pssm-ID: 215209 [Multi-domain]  Cd Length: 302  Bit Score: 302.38  E-value: 4.60e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  22 PRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASAGSITAVCPLL 101
Cdd:PLN02369    1 PALSQEIACYLGLELGKITIKRFADGEIYVQLQESVRGCDVFLVQPTCPPANENLMELLIMIDACRRASAKRITAVIPYF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 102 GYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRMDLSK-VAVVSPDA 180
Cdd:PLN02369   81 GYARADRKTQGRESIAAKLVANLITEAGADRVLACDLHSGQSMGYFDIPVDHVYGQPVILDYLASKTISSPdLVVVSPDV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 181 GRIRVAEQWAQRLGGVPLAFIHKTRdvTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIVAT 260
Cdd:PLN02369  161 GGVARARAFAKKLSDAPLAIVDKRR--QGHNVAEVMNLIGDVKGKVAIMVDDMIDTAGTITKGAALLHQEGAREVYACAT 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 261 HGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLFD 324
Cdd:PLN02369  239 HAVFSPPAIERLSSGLFQEVIVTNTIPVSEKNYFPQLTVLSVANLLGETIWRVHDDCSVSSIFD 302
PRK04923 PRK04923
ribose-phosphate diphosphokinase;
8-323 3.77e-82

ribose-phosphate diphosphokinase;


Pssm-ID: 179893 [Multi-domain]  Cd Length: 319  Bit Score: 252.16  E-value: 3.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110   8 RPGKNLILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALK 87
Cdd:PRK04923    2 QDQRNLLVFSGNANKPLAQSICKELGVRMGKALVTRFSDGEVQVEIEESVRRQEVFVIQPTCAPSAENLMELLVLIDALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  88 RASAGSITAVCPLLGYSRQDKK-HLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRD 166
Cdd:PRK04923   82 RASAASVTAVIPYFGYSRQDRRmRSSRVPITAKVAAKMISAMGADRVLTVDLHADQIQGFFDVPVDNVYASPLLLADIWR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 167 RMDLSKVAVVSPDAGRIRVAEQWAQRLGGVPLAFIHKTRdvTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNV 246
Cdd:PRK04923  162 AYGTDNLIVVSPDVGGVVRARAVAKRLDDADLAIIDKRR--PRANVATVMNIIGDVQGKTCVLVDDLVDTAGTLCAAAAA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541200110 247 LRKAGASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKRWDG-LTVLSIAPLLASAIRAVFEDGSVAKLF 323
Cdd:PRK04923  240 LKQRGALKVVAYITHPVLSGPAVDNINNSQLDELVVTDTIPLSEAARACAkIRQLSVAELLAETIRRIAFGESVSSLY 317
PRK00553 PRK00553
ribose-phosphate pyrophosphokinase; Provisional
 11-326 1.37e-80

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 179062 [Multi-domain]  Cd Length: 332  Bit Score: 248.68  E-value: 1.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  11 KNLILVTGRTHpRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRAS 90
Cdd:PRK00553    9 NHVIFSLSKAK-KLVDSICRKLSMKPGEIVIQKFADGETYIRFDESVRNKDVVIFQSTCSPVNDSLMELLIAIDALKRGS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  91 AGSITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDRMDL 170
Cdd:PRK00553   88 AKSITAILPYYGYARQDRKTAGREPITSKLVADLLTKAGVTRVTLTDIHSDQTQGFFDIPVDILRTYHVFLSRVLELLGK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 171 SKVAVVSPDAGRIRVAEQWAQRLgGVPLAFIHKTRdvTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKA 250
Cdd:PRK00553  168 KDLVVVSPDYGGVKRARLIAESL-ELPLAIIDKRR--PKHNVAESINVLGEVKNKNCLIVDDMIDTGGTVIAAAKLLKKQ 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 251 GASSITIVATHGVMSGPAVQRLQDCEAKEVV----VTDTVPIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLFDTY 326
Cdd:PRK00553  245 KAKKVCVMATHGLFNKNAIQLFDEAFKKKLIdklfVSNSIPQTKFEKKPQFKVVDLAHLYEEVLLCYANGGSISAIYTRH 324
PTZ00145 PTZ00145
phosphoribosylpyrophosphate synthetase; Provisional
 12-327 2.84e-78

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 240290 [Multi-domain]  Cd Length: 439  Bit Score: 245.94  E-value: 2.84e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  12 NLILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASA 91
Cdd:PTZ00145  119 NAILFSGSSNPLLSKNIADHLGTILGRVHLKRFADGEVSMQFLESIRGKDVYIIQPTCPPVNENLIELLLMISTCRRASA 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  92 GSITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDG--PVDHLIAMPVLVDYVRDRmD 169
Cdd:PTZ00145  199 KKITAVIPYYGYARQDRKLSSRVPISAADVARMIEAMGVDRVVAIDLHSGQIQGFFGPrvPVDNLEAQLIGLDYFTKK-D 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 170 LSKVAVVSPDAGRIRVAEQWAQRL-----GGVPLAFIHKTRdvTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEAC 244
Cdd:PTZ00145  278 LYKPVIVSPDAGGVYRARKFQDGLnhrgiSDCGIAMLIKQR--TKPNEIEKMDLVGNVYDSDVIIVDDMIDTSGTLCEAA 355

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 245 NVLRKAGASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPI-PSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLF 323
Cdd:PTZ00145  356 KQLKKHGARRVFAFATHGLFSGPAIERIEASPLEEVVVTDTVKSnKNIDSCKKITKLSVSVLVADAIRRIHQKESLNDLF 435


                  ....
gi 2541200110 324 DTYP 327
Cdd:PTZ00145  436 NVKG 439
PRK02458 PRK02458
ribose-phosphate pyrophosphokinase; Provisional
 11-323 3.25e-76

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 235039 [Multi-domain]  Cd Length: 323  Bit Score: 236.94  E-value: 3.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  11 KNLILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRAS 90
Cdd:PRK02458    8 KQIKLFSLNSNLEIAEKIAQAAGVPLGKLSSRQFSDGEIMINIEESVRGDDIYIIQSTSFPVNDHLWELLIMIDACKRAS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  91 AGSITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGAERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDR-MD 169
Cdd:PRK02458   88 ANTVNVVLPYFGYARQDRIAKPREPITAKLVANMLVKAGVDRVLTLDLHAVQVQGFFDIPVDNLFTVPLFAKHYCKKgLS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 170 LSKVAVVSPDAGRIRVAEQWAQRLGGvPLAFIHKTRDVTQPNKAVahrVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRK 249
Cdd:PRK02458  168 GSDVVVVSPKNSGIKRARSLAEYLDA-PIAIIDYAQDDSEREEGY---IIGDVAGKKAILIDDILNTGKTFAEAAKIVER 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 250 AGASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVpIPSEKRWDGLTVLSIAPLLASAIRAVFEDGSVAKLF 323
Cdd:PRK02458  244 EGATEIYAVASHGLFAGGAAEVLENAPIKEILVTDSV-ATKERVPKNVTYLSASELIADAIIRIHERKPLSPLF 316
PRK00934 PRK00934
ribose-phosphate pyrophosphokinase; Provisional
 14-311 1.03e-67

ribose-phosphate pyrophosphokinase; Provisional


Pssm-ID: 234868 [Multi-domain]  Cd Length: 285  Bit Score: 214.01  E-value: 1.03e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  14 ILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHAdPINKSIMEQLIMIDALKRASAGS 93
Cdd:PRK00934    1 MIIGGSASQLLASEVARLLNTELALVETKRFPDGELYVRILGEIDGEDVVIISTTY-PQDENLVELLLLIDALRDEGAKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  94 ITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAGaERIMSVDLHAAQSQGFFDGPVDHLIAMPVLVDYVRDrmDLSKV 173
Cdd:PRK00934   80 ITLVIPYLGYARQDKRFKPGEPISARAIAKIISAYY-DRIITINIHEPSILEFFPIPFINLDAAPLIAEYIGD--KLDDP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 174 AVVSPDAGRIRVAEQWAQRLGgVPLAFIHKTRdvTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGAS 253
Cdd:PRK00934  157 LVLAPDKGALELAKEAAEILG-CEYDYLEKTR--ISPTEVEIAPKNLDVKGKDVLIVDDIISTGGTMATAIKILKEQGAK 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2541200110 254 SITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKrwdgltvLSIAPLLASAIR 311
Cdd:PRK00934  234 KVYVACVHPVLVGDAILKLYNAGVDEIIVTDTLESEVSK-------ISVAPLIADLLK 284
Pribosyltran_N pfam13793
N-terminal domain of ribose phosphate pyrophosphokinase; This family is frequently found ...
 13-129 2.56e-60

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: 188.78  E-value: 2.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  13 LILVTGRTHPRLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPINKSIMEQLIMIDALKRASAG 92
Cdd:pfam13793   1 LKIFSGNSNPELAEKIAKRLGIPLGKATVSRFSDGEIYVRIEESVRGKDVFIIQSTCPPVNDNLMELLIMIDALKRASAK 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2541200110  93 SITAVCPLLGYSRQDKKHLGREPISCRLMFDLLKTAG 129
Cdd:pfam13793  81 RITAVIPYFGYARQDRKDKPREPITAKLVADLLEAAG 117
PRK07199 PRK07199
ribose-phosphate diphosphokinase;
23-316 6.45e-42

ribose-phosphate diphosphokinase;


Pssm-ID: 235960 [Multi-domain]  Cd Length: 301  Bit Score: 147.39  E-value: 6.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  23 RLAADVANQLGIEVLETTAYDFANGEMYVRYTESVRGADVFVLQSHADPiNKSIMEQLIMIDALKRASAGSITAVCPLLG 102
Cdd:PRK07199   13 AAAGRLAAALGVEVGRIELHRFPDGESYVRLDSPVAGRTVVLVCSLDRP-DEKLLPLLFAAEAARELGARRVGLVAPYLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 103 YSRQDKK-HLGrEPISCRLMFDLLkTAGAERIMSVDLH---AAQSQGFFDGPVDHLIAMPVLVDYVRDRMDlsKVAVVSP 178
Cdd:PRK07199   92 YMRQDIAfHPG-EAISQRHFARLL-SGSFDRLVTVDPHlhrYPSLSEVYPIPAVVLSAAPAIAAWIRAHVP--RPLLIGP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 179 DAGrirvAEQWAQ---RLGGVPLAFIHKTR------DVTQPNKAV-AHRVVgdvkgldcVLVDDLIDTGGTIAEACNVLR 248
Cdd:PRK07199  168 DEE----SEQWVAavaERAGAPHAVLRKTRhgdrdvEISLPDAAPwAGRTP--------VLVDDIVSTGRTLIEAARQLR 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541200110 249 KAGASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEKrwdgltvLSIAPLLASAIRAVFED 316
Cdd:PRK07199  236 AAGAASPDCVVVHALFAGDAYSALAAAGIARVVSTDTVPHPSNA-------ISLAPLLAEALRREFDD 296
PRK06827 PRK06827
phosphoribosylpyrophosphate synthetase; Provisional
 44-324 8.61e-35

phosphoribosylpyrophosphate synthetase; Provisional


Pssm-ID: 180714 [Multi-domain]  Cd Length: 382  Bit Score: 130.46  E-value: 8.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  44 FANGEMYVRYTESVRGADVFVLQshaDPINKSIM-----EQLIM------------IDALkRASAGSITAVCPLLGYSRQ 106
Cdd:PRK06827   62 FSNGEAKGEILESVRGKDIYILQ---DVGNYSVTynmfgEKNHMspddhfqdlkrtIDAI-RGKARRITVIMPFLYESRQ 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 107 DKKHlGREPISCRLMFDLLKTAGAERIMSVDLH------AAQSQGFFDGPVDHLIAMPVLVDYVRDRMDLSKVAVVSPDA 180
Cdd:PRK06827  138 HKRK-GRESLDCALALQELEELGVDNIITFDAHdprienAIPLMGFENLYPSYQIIKALLKNEKDLEIDKDHLMVISPDT 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 181 GRIRVAEQWAQRLGgVPLAFIHKTRDVTQ----PNKAVAHRVVG-DVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSI 255
Cdd:PRK06827  217 GAMDRAKYYASVLG-VDLGLFYKRRDYSRvvngRNPIVAHEFLGrDVEGKDVLIVDDMIASGGSMIDAAKELKSRGAKKI 295

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541200110 256 TIVATHGVMSGpAVQRLQdcEAKE------VVVTDTVPIPSE---KRWdgLTVLSIAPLLASAIRAVFEDGSVAKLFD 324
Cdd:PRK06827  296 IVAATFGFFTN-GLEKFD--KAYEegyfdrIIGTNLVYHPEEllsKPW--YIEVDMSKLIARIIDALNHDVSLSKLLD 368
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
 156-285 1.18e-21

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 88.99  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 156 AMPVLVDYVRDRMdLSKVAVVSPDAGRIRVAEQWAQRLGgVPLAFIHKTRD----VTQPNKAVAHRVVGDVKGLDCVLVD 231
Cdd:cd06223     1 AGRLLAEEIREDL-LEPDVVVGILRGGLPLAAALARALG-LPLAFIRKERKgpgrTPSEPYGLELPLGGDVKGKRVLLVD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2541200110 232 DLIDTGGTIAEACNVLRKAGASSITIVATHGVMSGPAvqRLQDCEAKEVVVTDT 285
Cdd:cd06223    79 DVIATGGTLLAAIELLKEAGAKVVGVAVLLDKPEGGA--RELASPGDPVYSLFT 130
Pribosyl_synth pfam14572
Phosphoribosyl synthetase-associated domain; This family includes several examples of enzymes ...
 218-323 3.67e-18

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: 81.02  E-value: 3.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 218 VVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIVATHGVMSGPAVQRLQDCEAKEVVVTDTVPIPSEK-RWDG 296
Cdd:pfam14572  77 VVGDVGGRIAIIVDDMIDDVDSFVAAAELLKERGAYKIYVMATHGLLSSDAPRLLEASPIDEVVVTNTIPHEIQKmQCHK 156

                          90       100
                  ....*....|....*....|....*..
gi 2541200110 297 LTVLSIAPLLASAIRAVFEDGSVAKLF 323
Cdd:pfam14572 157 IKTIDISQLIAEAIRRIHNGESMSYLF 183
PLN02297 PLN02297
ribose-phosphate pyrophosphokinase
 24-263 3.02e-14

ribose-phosphate pyrophosphokinase


Pssm-ID: 177934 [Multi-domain]  Cd Length: 326  Bit Score: 72.41  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110  24 LAADVANQLG-IEVLETTAYDFANG--EMYVRYTESVRGADVFVLQSHADPinKSIMEQLIMIDALKRASAGSITAVCPL 100
Cdd:PLN02297   28 LARKIAAESDaIELGSINWRKFPDGfpNLFINNAHGIRGQHVAFLASFSSP--AVIFEQLSVIYALPKLFVASFTLVLPF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 101 L--GYS-RQDK-----------KHLGREPIScrlmfdllkTAGAERIMSVDLHAAQSQGFFDGPVDHLI--AMPVLVDYV 164
Cdd:PLN02297  106 FptGTSeRVERegdvataftlaRILSNIPIS---------RGGPTSLVIFDIHALQERFYFGDNVLPCFesGIPLLKKRL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 165 RDRMDLSKVAVVSPDAGrirVAEQWAQRLGGVPLAFIHKTRDVTQpnkavahRVV----GDVKGLDCVLVDDLIDTGGTI 240
Cdd:PLN02297  177 QQLPDSDNIVIAFPDDG---AWKRFHKQFEHFPMVVCTKVREGDK-------RIVrikeGNPAGRHVVIVDDLVQSGGTL 246

                         250       260
                  ....*....|....*....|...
gi 2541200110 241 AEACNVLRKAGASSITIVATHGV 263
Cdd:PLN02297  247 IECQKVLAAHGAAKVSAYVTHGV 269
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
 173-266 9.72e-11

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: 59.30  E-value: 9.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 173 VAVVSPDAGRIRVAEQWAQRLGgVPLAFI-HKTRDVTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAG 251
Cdd:pfam00156  31 DVVVGILRGGLPFAGILARRLD-VPLAFVrKVSYNPDTSEVMKTSSALPDLKGKTVLIVDDILDTGGTLLKVLELLKNVG 109

                          90
                  ....*....|....*
gi 2541200110 252 ASSITIVATHGVMSG 266
Cdd:pfam00156 110 PKEVKIAVLIDKPAG 124
HptA COG0634
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ...
 221-259 9.71e-07

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: 48.10  E-value: 9.71e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2541200110 221 DVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIVA 259
Cdd:COG0634    88 DIEGRDVLIVEDIIDTGLTLSYLLELLKSRGPASVKIAT 126
ComFC COG1040
DNA utilization protein ComFC/GntX, contains phosphoribosyltransferase domain [General ...
 220-259 4.25e-06

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


Pssm-ID: 440662 [Multi-domain]  Cd Length: 196  Bit Score: 46.74  E-value: 4.25e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2541200110 220 GDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIVA 259
Cdd:COG1040   151 ARLAGKHVLLVDDVLTTGATLAEAARALKAAGAARVDVLV 190
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
 220-258 3.00e-05

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 44.09  E-value: 3.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2541200110 220 GDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIV 258
Cdd:PRK02277  136 ASVEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVV 174
PRK11595 PRK11595
DNA utilization protein GntX; Provisional
 215-257 7.14e-05

DNA utilization protein GntX; Provisional


Pssm-ID: 183221 [Multi-domain]  Cd Length: 227  Bit Score: 43.49  E-value: 7.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2541200110 215 AHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITI 257
Cdd:PRK11595  178 AFRLELPVQGQHMAIVDDVVTTGSTVAEIAQLLLRNGAASVQV 220
PLN02238 PLN02238
hypoxanthine phosphoribosyltransferase
 221-259 8.27e-05

hypoxanthine phosphoribosyltransferase


Pssm-ID: 215132  Cd Length: 189  Bit Score: 42.72  E-value: 8.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2541200110 221 DVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIVA 259
Cdd:PLN02238   94 DVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAASVSVCA 132
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
 190-252 1.57e-04

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 42.06  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541200110 190 AQRLGgVPLAFIHKtrdvtqpnKAVAH----RVVGDV-KGLDCVLVDDLIDTGGTIAEACNVLRKAGA 252
Cdd:COG0461    82 ARALG-LPAIFVRK--------EAKDHgtggQIEGGLlPGERVLVVEDVITTGGSVLEAVEALREAGA 140
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
 185-276 1.77e-04

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: 41.64  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541200110 185 VAEQWAQRLGGVPLAFIHKtrdvtqpnKAVAH----RVVGDVK-GLDCVLVDDLIDTGGTIAEACNVLRKAGAS---SIT 256
Cdd:TIGR00336  72 VSVKLAKPGGDIPLCFNRK--------EAKDHgeggNIEGELLeGDKVVVVEDVITTGTSILEAVEIIQAAGGQvagVII 143

                          90       100
                  ....*....|....*....|
gi 2541200110 257 IVATHGVMSGPAVQRLQDCE 276
Cdd:TIGR00336 144 AVDRQERSAGQEFEKEYGLP 163
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
 223-252 3.94e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 40.44  E-value: 3.94e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2541200110 223 KGLDCVLVDDLIDTGGTIAEACNVLRKAGA 252
Cdd:PRK02304  113 PGDRVLIVDDLLATGGTLEAAIKLLERLGA 142
apt TIGR01090
adenine phosphoribosyltransferase; A phylogenetic analysis suggested omitting the ...
 223-252 4.95e-04

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: 40.34  E-value: 4.95e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2541200110 223 KGLDCVLVDDLIDTGGTIAEACNVLRKAGA 252
Cdd:TIGR01090 108 PGQRVLIVDDLLATGGTAAATDELIKKLGG 137
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
 190-252 5.21e-04

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 40.53  E-value: 5.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541200110 190 AQRLGgVPLAFIHKtrdvtqpnKAVAH----RVVG-DVKGLDCVLVDDLIDTGGTIAEACNVLRKAGA 252
Cdd:PRK00455   83 ARALD-LPAIFVRK--------EAKDHgeggQIEGrRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGA 141
UPRTase pfam14681
Uracil phosphoribosyltransferase; This family includes the enzyme uracil ...
 228-283 8.24e-04

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


Pssm-ID: 434124  Cd Length: 204  Bit Score: 40.17  E-value: 8.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2541200110 228 VLVDDLIDTGGTIAEACNVLRKAGASSITIVATHGVMSGPAVQRLQDCEAK-EVVVT 283
Cdd:pfam14681 122 ILLDPMLATGGSAIAAIQVLREHGVPEENIVVLSVIAAPEGLHRLAAAFPDvKIVTA 178
upp PRK00129
uracil phosphoribosyltransferase; Reviewed
 217-274 1.28e-03

uracil phosphoribosyltransferase; Reviewed


Pssm-ID: 234653  Cd Length: 209  Bit Score: 39.30  E-value: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2541200110 217 RVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITIVAThgVMSGPAVQRLQD 274
Cdd:PRK00129  117 KLPEDIDERTVIVVDPMLATGGSAIAAIDLLKKRGAKNIKVLCL--VAAPEGIKALEE 172
PLN02293 PLN02293
adenine phosphoribosyltransferase
 219-252 6.31e-03

adenine phosphoribosyltransferase


Pssm-ID: 177930  Cd Length: 187  Bit Score: 37.35  E-value: 6.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2541200110 219 VGDVK-GLDCVLVDDLIDTGGTIAEACNVLRKAGA 252
Cdd:PLN02293  119 VGAVEpGERALVIDDLIATGGTLCAAINLLERAGA 153
Hpt1 COG2236
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ...
 206-257 7.09e-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: 36.75  E-value: 7.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2541200110 206 DVTQPNKAVAHRVVGDVKGLDCVLVDDLIDTGGTIAEACNVLRKAGASSITI 257
Cdd:COG2236    70 AKRLEEPVVKGPLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAEVRT 121
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
 228-252 9.16e-03

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: 36.59  E-value: 9.16e-03
                          10        20
                  ....*....|....*....|....*
gi 2541200110 228 VLVDDLIDTGGTIAEACNVLRKAGA 252
Cdd:COG0503   116 LIVDDLLATGGTAKAAIKLVEEAGA 140
 
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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