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Conserved domains on  [gi|664303366|ref|WP_030832760|]
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MULTISPECIES: thiamine phosphate synthase [Streptomyces]

Protein Classification

thiamine phosphate synthase( domain architecture ID 10791628)

thiamine phosphate synthase (TP synthase) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole in the thiamine biosynthesis pathway

CATH:  3.20.20.70
EC:  2.5.1.3
Gene Ontology:  GO:0000287|GO:0009228|GO:0004789|GO:0009229
PubMed:  10382260
SCOP:  4003094

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
thiE PRK00043
thiamine phosphate synthase;
1-210 2.50e-82

thiamine phosphate synthase;


:

Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 243.55  E-value: 2.50e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   1 MQLSDARLYLCTDAR-KRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIG 79
Cdd:PRK00043   2 MMMKLLRLYLITDSRdDSGRDLLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  80 SDVLHLGQGDIPVPAARAILGGQVLIGRSCHaEDEVAAAAAEPGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAASLKQD 158
Cdd:PRK00043  82 ADGVHLGQDDLPVADARALLGPDAIIGLSTH-TLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPqGLEGLREIRAAVGD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 664303366 159 RPWFAIGGIDATNLDEVLDAGATRVVVVRALTEASDPGAAAADLAKRVRARL 210
Cdd:PRK00043 161 IPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
 
Name Accession Description Interval E-value
thiE PRK00043
thiamine phosphate synthase;
1-210 2.50e-82

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 243.55  E-value: 2.50e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   1 MQLSDARLYLCTDAR-KRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIG 79
Cdd:PRK00043   2 MMMKLLRLYLITDSRdDSGRDLLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  80 SDVLHLGQGDIPVPAARAILGGQVLIGRSCHaEDEVAAAAAEPGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAASLKQD 158
Cdd:PRK00043  82 ADGVHLGQDDLPVADARALLGPDAIIGLSTH-TLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPqGLEGLREIRAAVGD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 664303366 159 RPWFAIGGIDATNLDEVLDAGATRVVVVRALTEASDPGAAAADLAKRVRARL 210
Cdd:PRK00043 161 IPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 7-202 2.14e-63

thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273222 [Multi-domain]  Cd Length: 196  Bit Score: 195.16  E-value: 2.14e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366    7 RLYLCTDARKRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVLHLG 86
Cdd:TIGR00693   1 GLYLITDPQDGPADLLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   87 QGDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAASLKQDRPWFAIG 165
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAE-GADYIGFGPIFPTPTKKDPAPPaGVELLREIAATLIDIPIVAIG 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 664303366  166 GIDATNLDEVLDAGATRVVVVRALTEASDPGAAAADL 202
Cdd:TIGR00693 160 GITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 4-209 4.35e-62

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 191.94  E-value: 4.35e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   4 SDARLYLCTDARKRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVL 83
Cdd:COG0352    2 TLPRLYLITDPDLCGRDLLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  84 HLGQGDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAASLKqDRPWF 162
Cdd:COG0352   82 HLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEA-GADYVGFGPVFPTPTKPGAPPPlGLEGLAWWAELV-EIPVV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 664303366 163 AIGGIDATNLDEVLDAGATRVVVVRALTEASDPGAAAADLAKRVRAR 209
Cdd:COG0352  160 AIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 8-204 2.55e-60

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 187.34  E-value: 2.55e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   8 LYLCTDARKRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVLHLGQ 87
Cdd:cd00564    1 LYLITDRRLDGEDLLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  88 GDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAASLKqDRPWFAIGG 166
Cdd:cd00564   81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEEL-GADYVGFGPVFPTPTKPGAGPPlGLELLREIAELV-EIPVVAIGG 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 664303366 167 IDATNLDEVLDAGATRVVVVRALTEASDPGAAAADLAK 204
Cdd:cd00564  159 ITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 8-189 2.10e-53

Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.


Pssm-ID: 426849 [Multi-domain]  Cd Length: 180  Bit Score: 168.88  E-value: 2.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366    8 LYLCTDARKRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVLHLGQ 87
Cdd:pfam02581   1 LYLVTDPGLDGEDLLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   88 GDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAPGLDLVRYAASLKQdRPWFAIGGI 167
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEAL-GADYIGFGPIFPTPTKPDAPPLGLEGLKAIAEAVE-IPVVAIGGI 158

                         170       180
                  ....*....|....*....|..
gi 664303366  168 DATNLDEVLDAGATRVVVVRAL 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
 
Name Accession Description Interval E-value
thiE PRK00043
thiamine phosphate synthase;
1-210 2.50e-82

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 243.55  E-value: 2.50e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   1 MQLSDARLYLCTDAR-KRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIG 79
Cdd:PRK00043   2 MMMKLLRLYLITDSRdDSGRDLLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  80 SDVLHLGQGDIPVPAARAILGGQVLIGRSCHaEDEVAAAAAEPGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAASLKQD 158
Cdd:PRK00043  82 ADGVHLGQDDLPVADARALLGPDAIIGLSTH-TLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPqGLEGLREIRAAVGD 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 664303366 159 RPWFAIGGIDATNLDEVLDAGATRVVVVRALTEASDPGAAAADLAKRVRARL 210
Cdd:PRK00043 161 IPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 7-202 2.14e-63

thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273222 [Multi-domain]  Cd Length: 196  Bit Score: 195.16  E-value: 2.14e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366    7 RLYLCTDARKRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVLHLG 86
Cdd:TIGR00693   1 GLYLITDPQDGPADLLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   87 QGDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAASLKQDRPWFAIG 165
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAE-GADYIGFGPIFPTPTKKDPAPPaGVELLREIAATLIDIPIVAIG 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 664303366  166 GIDATNLDEVLDAGATRVVVVRALTEASDPGAAAADL 202
Cdd:TIGR00693 160 GITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 4-209 4.35e-62

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 191.94  E-value: 4.35e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   4 SDARLYLCTDARKRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVL 83
Cdd:COG0352    2 TLPRLYLITDPDLCGRDLLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  84 HLGQGDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAASLKqDRPWF 162
Cdd:COG0352   82 HLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEA-GADYVGFGPVFPTPTKPGAPPPlGLEGLAWWAELV-EIPVV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 664303366 163 AIGGIDATNLDEVLDAGATRVVVVRALTEASDPGAAAADLAKRVRAR 209
Cdd:COG0352  160 AIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
PRK02615 PRK02615
thiamine phosphate synthase;
2-208 1.67e-61

thiamine phosphate synthase;


Pssm-ID: 235054 [Multi-domain]  Cd Length: 347  Bit Score: 195.10  E-value: 1.67e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   2 QLSDARLYLCTDARKrqgDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSD 81
Cdd:PRK02615 143 RLKDARLYLITSPSE---NLLEVVEAALKGGVTLVQYRDKTADDRQRLEEAKKLKELCHRYGALFIVNDRVDIALAVDAD 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  82 VLHLGQGDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAPGLDLVRYAASLKQdRPW 161
Cdd:PRK02615 220 GVHLGQEDLPLAVARQLLGPEKIIGRSTTNPEEMAKAIAE-GADYIGVGPVFPTPTKPGKAPAGLEYLKYAAKEAP-IPW 297

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 664303366 162 FAIGGIDATNLDEVLDAGATRVVVVRALTEASDPGAAAADLAKRVRA 208
Cdd:PRK02615 298 FAIGGIDKSNIPEVLQAGAKRVAVVRAIMGAEDPKQATQELLKQLSR 344
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 8-204 2.55e-60

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 187.34  E-value: 2.55e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   8 LYLCTDARKRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVLHLGQ 87
Cdd:cd00564    1 LYLITDRRLDGEDLLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  88 GDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAASLKqDRPWFAIGG 166
Cdd:cd00564   81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEEL-GADYVGFGPVFPTPTKPGAGPPlGLELLREIAELV-EIPVVAIGG 158

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 664303366 167 IDATNLDEVLDAGATRVVVVRALTEASDPGAAAADLAK 204
Cdd:cd00564  159 ITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 8-189 2.10e-53

Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.


Pssm-ID: 426849 [Multi-domain]  Cd Length: 180  Bit Score: 168.88  E-value: 2.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366    8 LYLCTDARKRQGDLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVLHLGQ 87
Cdd:pfam02581   1 LYLVTDPGLDGEDLLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   88 GDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAPGLDLVRYAASLKQdRPWFAIGGI 167
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEAL-GADYIGFGPIFPTPTKPDAPPLGLEGLKAIAEAVE-IPVVAIGGI 158

                         170       180
                  ....*....|....*....|..
gi 664303366  168 DATNLDEVLDAGATRVVVVRAL 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 4-202 6.37e-34

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 126.04  E-value: 6.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   4 SDARLYLCTDAR--KRQG-DLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGS 80
Cdd:PLN02898 289 RNLFLYAVTDSGmnKKWGrSTVDAVRAAIEGGATIVQLREKEAETREFIEEAKACLAICRSYGVPLLINDRVDVALACDA 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  81 DVLHLGQGDIPVPAARAILGGQVLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAPGLDLVRyAASLKQDRP 160
Cdd:PLN02898 369 DGVHLGQSDMPVRLARSLLGPGKIIGVSCKTPEQAEQAWKD-GADYIGCGGVFPTNTKANNKTIGLDGLR-EVCEASKLP 446

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 664303366 161 WFAIGGIDATNLDEVLDAGATR---VVVVRALTEASDPGAAAADL 202
Cdd:PLN02898 447 VVAIGGISASNAASVMESGAPNlkgVAVVSALFDQEDVLKATRKL 491
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 3-211 5.79e-26

multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 104.67  E-value: 5.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366   3 LSDARLYLCTDARKRQGD--LPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGS 80
Cdd:PRK09517   1 MTDFSLYLVTDPVLGGGPekVAGIVDSAISGGVSVVQLRDKNAGVEDVRAAAKELKELCDARGVALVVNDRLDVAVELGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  81 DVlHLGQGDIPVPAARAILGGQVLIGRSC------HAEDEVAAAAAEPGVDYFCTGPCWPTPTKPGRHAP-GLDLVRYAA 153
Cdd:PRK09517  81 HV-HIGQGDTPYTQARRLLPAHLELGLTIetldqlEAVIAQCAETGVALPDVIGIGPVASTATKPDAPPAlGVDGIAEIA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664303366 154 SLKQDR--PWFAIGGIDATNLDEVLDAGATRVVVVRALTEASDPGAAAADLA---KRVRARLG 211
Cdd:PRK09517 160 AVAQDHgiASVAIGGVGLRNAAELAATGIDGLCVVSAIMAAANPAAAARELRtafQPTRSPET 222
PRK07695 PRK07695
thiazole tautomerase TenI;
33-209 2.54e-15

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 71.20  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  33 VDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLaVNDRADVAHAIGSDVLHLGQGDIPVPAARAILGgQVLIGRSCHAE 112
Cdd:PRK07695  28 VDYIHIREREKSAKELYEGVESLLKKGVPASKLI-INDRVDIALLLNIHRVQLGYRSFSVRSVREKFP-YLHVGYSVHSL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366 113 DEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAPGLDLVRYAASLKQdRPWFAIGGIDATNLDEVLDAGATRVVVVRALTEA 192
Cdd:PRK07695 106 EEAIQAEKN-GADYVVYGHVFPTDCKKGVPARGLEELSDIARALS-IPVIAIGGITPENTRDVLAAGVSGIAVMSGIFSS 183

                        170
                 ....*....|....*..
gi 664303366 193 SDPGAAAADLAKRVRAR 209
Cdd:PRK07695 184 ANPYSKAKRYAESIKKW 200
thiE PRK12290
thiamine phosphate synthase;
20-198 5.26e-14

thiamine phosphate synthase;


Pssm-ID: 237041 [Multi-domain]  Cd Length: 437  Bit Score: 69.82  E-value: 5.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  20 DLPEFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVLHLGQGDIPVPAARAIL 99
Cdd:PRK12290 218 DDVEWIERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAYGVHLGQEDLEEANLAQLT 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366 100 GGQVLIGRSCHAE-DEVAAAAAEPgvDYFCTGPCWPTPTKPGRHAPGlDLVRYAA------SLKQDR----PWFAIGGID 168
Cdd:PRK12290 298 DAGIRLGLSTHGYyELLRIVQIQP--SYIALGHIFPTTTKQMPSKPQ-GLVRLALyqklidTIPYQGqtgfPTVAIGGID 374

                        170       180       190
                 ....*....|....*....|....*....|
gi 664303366 169 ATNLDEVLDAGATRVVVVRALTEASDPGAA 198
Cdd:PRK12290 375 QSNAEQVWQCGVSSLAVVRAITLAEDPQLV 404
PRK08999 PRK08999
Nudix family hydrolase;
19-189 1.47e-12

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 64.89  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  19 GDLPEFLDAV---LAGGVDIVQLRDKGMEAgeelEHLQVFAEAA----RRHGRLLAVNDRADVAHAIGSDVLHLGQGDIP 91
Cdd:PRK08999 141 DGDAAFLARLeraLAAGIRLIQLRAPQLPP----AAYRALARAAlglcRRAGAQLLLNGDPELAEDLGADGVHLTSAQLA 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  92 VPAARAILGGQVLiGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGrhAPGLDLVRYAASLKQ-DRPWFAIGGIDAT 170
Cdd:PRK08999 217 ALAARPLPAGRWV-AASCHDAEELARAQRL-GVDFAVLSPVQPTASHPG--AAPLGWEGFAALIAGvPLPVYALGGLGPG 292

                        170
                 ....*....|....*....
gi 664303366 171 NLDEVLDAGATRVVVVRAL 189
Cdd:PRK08999 293 DLEEAREHGAQGIAGIRGL 311
PRK03512 PRK03512
thiamine phosphate synthase;
23-209 9.81e-11

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 58.91  E-value: 9.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366  23 EFLDAVLAGGVDIVQLRDKGMEAGEELEHLQVFAEAARRHGRLLAVNDRADVAHAIGSDVLHLGQGDIPVPAARAILGGQ 102
Cdd:PRK03512  23 QWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQAYGVHLGQEDLETADLNAIRAAG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664303366 103 VLIGRSCHAEDEVAAAAAEpGVDYFCTGPCWPTPTKPGRHAP-GL-DLVRYAASLkQDRPWFAIGGIDATNLDEVLDAGA 180
Cdd:PRK03512 103 LRLGVSTHDDMEIDVALAA-RPSYIALGHVFPTQTKQMPSAPqGLaQLARHVERL-ADYPTVAIGGISLERAPAVLATGV 180

                        170       180
                 ....*....|....*....|....*....
gi 664303366 181 TRVVVVRALTEASDPGAAAADLAKRVRAR 209
Cdd:PRK03512 181 GSIAVVSAITQAADWRAATAQLLELAEVG 209
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 165-199 1.74e-03

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 37.95  E-value: 1.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 664303366 165 GGIDATNLDEVLDAGATRVVVVRALTEASDPGAAA 199
Cdd:cd04726  165 GGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
165-201 4.95e-03

bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 37.30  E-value: 4.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 664303366 165 GGIDATNLDEVLDAGATRVVVVRALTEASDPGAAAAD 201
Cdd:PRK13307 337 GGVRVENVEEALKAGADILVVGRAITKSKDVRRAAED 373
 
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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