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Conserved domains on  [gi|949496469|ref|WP_056939015|]
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thiamine phosphate synthase [Lentilactobacillus buchneri]

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

EC:  2.5.1.3
Gene Ontology:  GO:0000287|GO:0009228

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
thiE PRK00043
thiamine phosphate synthase;
9-218 4.71e-72

thiamine phosphate synthase;


:

Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 217.74  E-value: 4.71e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   9 MLRAYFIAGTQDvkDQTKTLQEIAKQAMEAGITAFQYREKGpgsLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKT 88
Cdd:PRK00043   6 LLRLYLITDSRD--DSGRDLLEVVEAALEGGVTLVQLREKG---LDTRERLELARALKELCRRYGVPLIVNDRVDLALAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  89 NADGVHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIANHiDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQ 168
Cdd:PRK00043  81 GADGVHLGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALA-AGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAVG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 949496469 169 -LPVVAIGGITEQNIVELPQTGVAGVSVISMIAQSDDIFRTVKVMNETFEK 218
Cdd:PRK00043 160 dIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRA 210
 
Name Accession Description Interval E-value
thiE PRK00043
thiamine phosphate synthase;
9-218 4.71e-72

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 217.74  E-value: 4.71e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   9 MLRAYFIAGTQDvkDQTKTLQEIAKQAMEAGITAFQYREKGpgsLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKT 88
Cdd:PRK00043   6 LLRLYLITDSRD--DSGRDLLEVVEAALEGGVTLVQLREKG---LDTRERLELARALKELCRRYGVPLIVNDRVDLALAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  89 NADGVHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIANHiDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQ 168
Cdd:PRK00043  81 GADGVHLGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALA-AGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAVG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 949496469 169 -LPVVAIGGITEQNIVELPQTGVAGVSVISMIAQSDDIFRTVKVMNETFEK 218
Cdd:PRK00043 160 dIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRA 210
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 13-214 1.74e-69

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: 210.84  E-value: 1.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  13 YFIAgtqDVKDQTKTLQEIAKQAMEAGITAFQYREKgpgSLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNADG 92
Cdd:cd00564    2 YLIT---DRRLDGEDLLEVVEAALKGGVTLVQLREK---DLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  93 VHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIANHiDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQLPVV 172
Cdd:cd00564   76 VHLGQDDLPVAEARALLGPDLIIGVSTHSLEEALRAEE-LGADYVGFGPVFPTPTKPGAGPPLGLELLREIAELVEIPVV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 949496469 173 AIGGITEQNIVELPQTGVAGVSVISMIAQSDDIFRTVKVMNE 214
Cdd:cd00564  155 AIGGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 9-218 1.31e-65

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: 201.18  E-value: 1.31e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   9 MLRAYFIAGTQDVKDqtkTLQEIAKQAMEAGITAFQYREKGpgsLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKT 88
Cdd:COG0352    3 LPRLYLITDPDLCGR---DLLEVLEAALAGGVDLVQLREKD---LDERELLALARALRALCRAYGVPLIINDRVDLALAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  89 NADGVHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIANHiDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQ 168
Cdd:COG0352   77 GADGVHLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEE-AGADYVGFGPVFPTPTKPGAPPPLGLEGLAWWAELVE 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 949496469 169 LPVVAIGGITEQNIVELPQTGVAGVSVISMIAQSDDIFRTVKVMNETFEK 218
Cdd:COG0352  156 IPVVAIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEA 205
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 13-199 2.21e-63

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: 194.69  E-value: 2.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   13 YFIAGTQDVkdqTKTLQEIAKQAMEAGITAFQYREKGpgsLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNADG 92
Cdd:pfam02581   2 YLVTDPGLD---GEDLLEVVEEALKGGVTIVQLREKE---LDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   93 VHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIANHiDGISYLGSGPVFPTGSKADADPViGVDGLATLVKASQLPVV 172
Cdd:pfam02581  76 VHLGQDDLPVAEARELLGPDLIIGVSTHTLEEALEAEA-LGADYIGFGPIFPTPTKPDAPPL-GLEGLKAIAEAVEIPVV 153

                         170       180
                  ....*....|....*....|....*..
gi 949496469  173 AIGGITEQNIVELPQTGVAGVSVISMI 199
Cdd:pfam02581 154 AIGGITPENVPEVIEAGADGVAVVSAI 180
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 11-210 7.92e-59

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: 183.60  E-value: 7.92e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   11 RAYFIAGTQDVKdqtKTLQEIAKQAMEAGITAFQYREKGpgsLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNA 90
Cdd:TIGR00693   1 GLYLITDPQDGP---ADLLNRVEAALKGGVTLVQLRDKG---SNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   91 DGVHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIAnHIDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQ-L 169
Cdd:TIGR00693  75 DGVHLGQDDLPASEARALLGPDKIIGVSTHNLEELAEA-EAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIdI 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 949496469  170 PVVAIGGITEQNIVELPQTGVAGVSVISMIAQSDDIFRTVK 210
Cdd:TIGR00693 154 PIVAIGGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAK 194
 
Name Accession Description Interval E-value
thiE PRK00043
thiamine phosphate synthase;
9-218 4.71e-72

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 217.74  E-value: 4.71e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   9 MLRAYFIAGTQDvkDQTKTLQEIAKQAMEAGITAFQYREKGpgsLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKT 88
Cdd:PRK00043   6 LLRLYLITDSRD--DSGRDLLEVVEAALEGGVTLVQLREKG---LDTRERLELARALKELCRRYGVPLIVNDRVDLALAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  89 NADGVHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIANHiDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQ 168
Cdd:PRK00043  81 GADGVHLGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALA-AGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAVG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 949496469 169 -LPVVAIGGITEQNIVELPQTGVAGVSVISMIAQSDDIFRTVKVMNETFEK 218
Cdd:PRK00043 160 dIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRA 210
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 13-214 1.74e-69

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: 210.84  E-value: 1.74e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  13 YFIAgtqDVKDQTKTLQEIAKQAMEAGITAFQYREKgpgSLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNADG 92
Cdd:cd00564    2 YLIT---DRRLDGEDLLEVVEAALKGGVTLVQLREK---DLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  93 VHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIANHiDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQLPVV 172
Cdd:cd00564   76 VHLGQDDLPVAEARALLGPDLIIGVSTHSLEEALRAEE-LGADYVGFGPVFPTPTKPGAGPPLGLELLREIAELVEIPVV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 949496469 173 AIGGITEQNIVELPQTGVAGVSVISMIAQSDDIFRTVKVMNE 214
Cdd:cd00564  155 AIGGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 9-218 1.31e-65

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: 201.18  E-value: 1.31e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   9 MLRAYFIAGTQDVKDqtkTLQEIAKQAMEAGITAFQYREKGpgsLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKT 88
Cdd:COG0352    3 LPRLYLITDPDLCGR---DLLEVLEAALAGGVDLVQLREKD---LDERELLALARALRALCRAYGVPLIINDRVDLALAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  89 NADGVHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIANHiDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQ 168
Cdd:COG0352   77 GADGVHLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEE-AGADYVGFGPVFPTPTKPGAPPPLGLEGLAWWAELVE 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 949496469 169 LPVVAIGGITEQNIVELPQTGVAGVSVISMIAQSDDIFRTVKVMNETFEK 218
Cdd:COG0352  156 IPVVAIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEA 205
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 13-199 2.21e-63

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: 194.69  E-value: 2.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   13 YFIAGTQDVkdqTKTLQEIAKQAMEAGITAFQYREKGpgsLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNADG 92
Cdd:pfam02581   2 YLVTDPGLD---GEDLLEVVEEALKGGVTIVQLREKE---LDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   93 VHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIANHiDGISYLGSGPVFPTGSKADADPViGVDGLATLVKASQLPVV 172
Cdd:pfam02581  76 VHLGQDDLPVAEARELLGPDLIIGVSTHTLEEALEAEA-LGADYIGFGPIFPTPTKPDAPPL-GLEGLKAIAEAVEIPVV 153

                         170       180
                  ....*....|....*....|....*..
gi 949496469  173 AIGGITEQNIVELPQTGVAGVSVISMI 199
Cdd:pfam02581 154 AIGGITPENVPEVIEAGADGVAVVSAI 180
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 11-210 7.92e-59

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: 183.60  E-value: 7.92e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   11 RAYFIAGTQDVKdqtKTLQEIAKQAMEAGITAFQYREKGpgsLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNA 90
Cdd:TIGR00693   1 GLYLITDPQDGP---ADLLNRVEAALKGGVTLVQLRDKG---SNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   91 DGVHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIAnHIDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQ-L 169
Cdd:TIGR00693  75 DGVHLGQDDLPASEARALLGPDKIIGVSTHNLEELAEA-EAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIdI 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 949496469  170 PVVAIGGITEQNIVELPQTGVAGVSVISMIAQSDDIFRTVK 210
Cdd:TIGR00693 154 PIVAIGGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAK 194
PRK02615 PRK02615
thiamine phosphate synthase;
21-218 9.16e-50

thiamine phosphate synthase;


Pssm-ID: 235054 [Multi-domain]  Cd Length: 347  Bit Score: 165.06  E-value: 9.16e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  21 VKDQTKTLQEIAKQAMEAGITAFQYREKgpgSLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNADGVHVGQKDE 100
Cdd:PRK02615 152 ITSPSENLLEVVEAALKGGVTLVQYRDK---TADDRQRLEEAKKLKELCHRYGALFIVNDRVDIALAVDADGVHLGQEDL 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469 101 RVTKVIEAVGQSMFVGLSCDTKEQVNIAnHIDGISYLGSGPVFPTGSKADADPViGVDGLATLVKASQLPVVAIGGITEQ 180
Cdd:PRK02615 229 PLAVARQLLGPEKIIGRSTTNPEEMAKA-IAEGADYIGVGPVFPTPTKPGKAPA-GLEYLKYAAKEAPIPWFAIGGIDKS 306

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 949496469 181 NIVELPQTGVAGVSVISMIAQSDDIFRTVKVMNETFEK 218
Cdd:PRK02615 307 NIPEVLQAGAKRVAVVRAIMGAEDPKQATQELLKQLSR 344
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 5-210 4.04e-45

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 156.47  E-value: 4.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469   5 FEPGMLRAYFIAGTQDVKDQTKTLQEIAKQAMEAGITAFQYREKGPGSlsgakRD--EMAADLREMCSDYEIPFIVDDDV 82
Cdd:PLN02898 286 FNPRNLFLYAVTDSGMNKKWGRSTVDAVRAAIEGGATIVQLREKEAET-----REfiEEAKACLAICRSYGVPLLINDRV 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  83 DLAVKTNADGVHVGQKDERVTKVIEAVGQSMFVGLSCDTKEQVNIAnHIDGISYLGSGPVFPTGSKADAdPVIGVDGLAT 162
Cdd:PLN02898 361 DVALACDADGVHLGQSDMPVRLARSLLGPGKIIGVSCKTPEQAEQA-WKDGADYIGCGGVFPTNTKANN-KTIGLDGLRE 438

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 949496469 163 LVKASQLPVVAIGGITEQNIVELPQTGVA---GVSVISMIAQSDDIFRTVK 210
Cdd:PLN02898 439 VCEASKLPVVAIGGISASNAASVMESGAPnlkGVAVVSALFDQEDVLKATR 489
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 31-204 2.54e-23

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 97.35  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  31 IAKQAMEAGITAFQYREKGPGSlsgAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNADgVHVGQKDERVTKVIEAVG 110
Cdd:PRK09517  24 IVDSAISGGVSVVQLRDKNAGV---EDVRAAAKELKELCDARGVALVVNDRLDVAVELGLH-VHIGQGDTPYTQARRLLP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469 111 QSMFVGLSCDTKEQVN--IA----NHIDGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQ---LPVVAIGGITEQN 181
Cdd:PRK09517 100 AHLELGLTIETLDQLEavIAqcaeTGVALPDVIGIGPVASTATKPDAPPALGVDGIAEIAAVAQdhgIASVAIGGVGLRN 179

                        170       180
                 ....*....|....*....|...
gi 949496469 182 IVELPQTGVAGVSVISMIAQSDD 204
Cdd:PRK09517 180 AAELAATGIDGLCVVSAIMAAAN 202
PRK07695 PRK07695
thiazole tautomerase TenI;
77-204 1.14e-15

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 72.36  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  77 IVDDDVDLAVKTNADGVHVGQKDERVTKVIEAVgQSMFVGLSCDTKEQVnIANHIDGISYLGSGPVFPTGSKADADPViG 156
Cdd:PRK07695  61 IINDRVDIALLLNIHRVQLGYRSFSVRSVREKF-PYLHVGYSVHSLEEA-IQAEKNGADYVVYGHVFPTDCKKGVPAR-G 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 949496469 157 VDGLATLVKASQLPVVAIGGITEQNIVELPQTGVAGVSVISMIAQSDD 204
Cdd:PRK07695 138 LEELSDIARALSIPVIAIGGITPENTRDVLAAGVSGIAVMSGIFSSAN 185
PRK08999 PRK08999
Nudix family hydrolase;
34-197 5.70e-14

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 69.13  E-value: 5.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  34 QAMEAGITAFQYREKgpgSLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNADGVHVG-----QKDERvtkvieA 108
Cdd:PRK08999 152 RALAAGIRLIQLRAP---QLPPAAYRALARAALGLCRRAGAQLLLNGDPELAEDLGADGVHLTsaqlaALAAR------P 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469 109 VGQSMFVGLSCDTKEQVNIANHIdGISYLGSGPVFPTGSKADAdPVIGVDGLATLVKASQLPVVAIGGITEQNIVELPQT 188
Cdd:PRK08999 223 LPAGRWVAASCHDAEELARAQRL-GVDFAVLSPVQPTASHPGA-APLGWEGFAALIAGVPLPVYALGGLGPGDLEEAREH 300


                 ....*....
gi 949496469 189 GVAGVSVIS 197
Cdd:PRK08999 301 GAQGIAGIR 309
PRK03512 PRK03512
thiamine phosphate synthase;
36-204 5.73e-14

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 67.77  E-value: 5.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  36 MEAGITAFQYREKgpgSLSGAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNADGVHVGQKDERVT--KVIEAVGqsM 113
Cdd:PRK03512  29 LDAGVRTLQLRIK---DRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQAYGVHLGQEDLETAdlNAIRAAG--L 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469 114 FVGLSCDTKEQVNIANHIdGISYLGSGPVFPTGSKADADPVIGVDGLATLVKASQ-LPVVAIGGITEQNIVELPQTGVAG 192
Cdd:PRK03512 104 RLGVSTHDDMEIDVALAA-RPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLAdYPTVAIGGISLERAPAVLATGVGS 182

                        170
                 ....*....|..
gi 949496469 193 VSVISMIAQSDD 204
Cdd:PRK03512 183 IAVVSAITQAAD 194
thiE PRK12290
thiamine phosphate synthase;
36-215 3.60e-10

thiamine phosphate synthase;


Pssm-ID: 237041 [Multi-domain]  Cd Length: 437  Bit Score: 58.65  E-value: 3.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469  36 MEAGITAFQYREKGPGSlsgAKRDEMAADLREMCSDYEIPFIVDDDVDLAVKTNADGVHVGQKDERVTKVIEAVGQSMFV 115
Cdd:PRK12290 227 LPLGINTVQLRIKDPQQ---ADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAYGVHLGQEDLEEANLAQLTDAGIRL 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949496469 116 GLSCDTKEQVNIANHIDGiSYLGSGPVFPTGSKA------------------DADPVIGVDGLatlvkasqlPVVAIGGI 177
Cdd:PRK12290 304 GLSTHGYYELLRIVQIQP-SYIALGHIFPTTTKQmpskpqglvrlalyqkliDTIPYQGQTGF---------PTVAIGGI 373

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 949496469 178 TEQNIVELPQTGVAGVSVISMIAQSDDIFRTV----KVMNET 215
Cdd:PRK12290 374 DQSNAEQVWQCGVSSLAVVRAITLAEDPQLVIeffdQVMAEN 415
 
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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