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Conserved domains on  [gi|489183710|ref|WP_003093148|]
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MULTISPECIES: thiamine phosphate synthase [Pseudomonas]

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;
1-209 3.20e-77

thiamine phosphate synthase;


:

Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 230.45  E-value: 3.20e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   1 MKLRGLYAITDSQLLDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV- 79
Cdd:PRK00043   4 MKLLRLYLITDSRDDSGRDLLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVGAd 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  80 GLHLGQTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGAPAAS-VELLDQARPRL-HLP 157
Cdd:PRK00043  84 GVHLGQDDLPVADARALLGPDAIIGLSTHT-LEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQgLEGLREIRAAVgDIP 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489183710 158 ITAIGGISLDTAPGLIARGVDLVAVIHalfAAASAAEVERRARAFSALFEPA 209
Cdd:PRK00043 163 IVAIGGITPENAPEVLEAGADGVAVVS---AITGAEDPEAAARALLAAFRAA 211
 
Name Accession Description Interval E-value
thiE PRK00043
thiamine phosphate synthase;
1-209 3.20e-77

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 230.45  E-value: 3.20e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   1 MKLRGLYAITDSQLLDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV- 79
Cdd:PRK00043   4 MKLLRLYLITDSRDDSGRDLLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVGAd 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  80 GLHLGQTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGAPAAS-VELLDQARPRL-HLP 157
Cdd:PRK00043  84 GVHLGQDDLPVADARALLGPDAIIGLSTHT-LEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQgLEGLREIRAAVgDIP 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489183710 158 ITAIGGISLDTAPGLIARGVDLVAVIHalfAAASAAEVERRARAFSALFEPA 209
Cdd:PRK00043 163 IVAIGGITPENAPEVLEAGADGVAVVS---AITGAEDPEAAARALLAAFRAA 211
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 5-184 9.50e-69

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: 208.64  E-value: 9.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710    5 GLYAITDSQLlDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV-GLHL 83
Cdd:TIGR00693   1 GLYLITDPQD-GPADLLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGAdGVHL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   84 GQTDGSLSAARALLGRQAIIGATCHAQLELAEqAVAEGASYVAFGRFFNSSTKPG-APAASVELLDQARPRL-HLPITAI 161
Cdd:TIGR00693  80 GQDDLPASEARALLGPDKIIGVSTHNLEELAE-AEAEGADYIGFGPIFPTPTKKDpAPPAGVELLREIAATLiDIPIVAI 158

                         170       180
                  ....*....|....*....|...
gi 489183710  162 GGISLDTAPGLIARGVDLVAVIH 184
Cdd:TIGR00693 159 GGITLENAAEVLAAGADGVAVVS 181
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 6-183 3.13e-64

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: 196.97  E-value: 3.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   6 LYAITDSQLlDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV-GLHLG 84
Cdd:cd00564    1 LYLITDRRL-DGEDLLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGAdGVHLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  85 QTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGA-PAASVELLDQARPRLHLPITAIGG 163
Cdd:cd00564   80 QDDLPVAEARALLGPDLIIGVSTHS-LEEALRAEELGADYVGFGPVFPTPTKPGAgPPLGLELLREIAELVEIPVVAIGG 158

                        170       180
                 ....*....|....*....|
gi 489183710 164 ISLDTAPGLIARGVDLVAVI 183
Cdd:cd00564  159 ITPENAAEVLAAGADGVAVI 178
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 1-209 4.28e-63

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: 194.63  E-value: 4.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   1 MKLRGLYAITDSQLLDDgRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV- 79
Cdd:COG0352    1 MTLPRLYLITDPDLCGR-DLLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGAd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  80 GLHLGQTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGA-PAASVELLDQARPRLHLPI 158
Cdd:COG0352   80 GVHLGQEDLPVAEARALLGPDLIIGVSCHS-LEEALRAEEAGADYVGFGPVFPTPTKPGApPPLGLEGLAWWAELVEIPV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489183710 159 TAIGGISLDTAPGLIARGVDLVAVIhalFAAASAAEVERRARAFSALFEPA 209
Cdd:COG0352  159 VAIGGITPENAAEVLAAGADGVAVI---SAIWGAPDPAAAARELRAALEAA 206
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 6-183 7.04e-62

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: 190.45  E-value: 7.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710    6 LYAITDSQLlDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV-GLHLG 84
Cdd:pfam02581   1 LYLVTDPGL-DGEDLLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGAdGVHLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   85 QTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGAPAASVELLDQARPRLHLPITAIGGI 164
Cdd:pfam02581  80 QDDLPVAEARELLGPDLIIGVSTHT-LEEALEAEALGADYIGFGPIFPTPTKPDAPPLGLEGLKAIAEAVEIPVVAIGGI 158

                         170
                  ....*....|....*....
gi 489183710  165 SLDTAPGLIARGVDLVAVI 183
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVV 177
 
Name Accession Description Interval E-value
thiE PRK00043
thiamine phosphate synthase;
1-209 3.20e-77

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 230.45  E-value: 3.20e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   1 MKLRGLYAITDSQLLDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV- 79
Cdd:PRK00043   4 MKLLRLYLITDSRDDSGRDLLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVGAd 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  80 GLHLGQTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGAPAAS-VELLDQARPRL-HLP 157
Cdd:PRK00043  84 GVHLGQDDLPVADARALLGPDAIIGLSTHT-LEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQgLEGLREIRAAVgDIP 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489183710 158 ITAIGGISLDTAPGLIARGVDLVAVIHalfAAASAAEVERRARAFSALFEPA 209
Cdd:PRK00043 163 IVAIGGITPENAPEVLEAGADGVAVVS---AITGAEDPEAAARALLAAFRAA 211
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 5-184 9.50e-69

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: 208.64  E-value: 9.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710    5 GLYAITDSQLlDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV-GLHL 83
Cdd:TIGR00693   1 GLYLITDPQD-GPADLLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGAdGVHL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   84 GQTDGSLSAARALLGRQAIIGATCHAQLELAEqAVAEGASYVAFGRFFNSSTKPG-APAASVELLDQARPRL-HLPITAI 161
Cdd:TIGR00693  80 GQDDLPASEARALLGPDKIIGVSTHNLEELAE-AEAEGADYIGFGPIFPTPTKKDpAPPAGVELLREIAATLiDIPIVAI 158

                         170       180
                  ....*....|....*....|...
gi 489183710  162 GGISLDTAPGLIARGVDLVAVIH 184
Cdd:TIGR00693 159 GGITLENAAEVLAAGADGVAVVS 181
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 6-183 3.13e-64

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: 196.97  E-value: 3.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   6 LYAITDSQLlDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV-GLHLG 84
Cdd:cd00564    1 LYLITDRRL-DGEDLLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGAdGVHLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  85 QTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGA-PAASVELLDQARPRLHLPITAIGG 163
Cdd:cd00564   80 QDDLPVAEARALLGPDLIIGVSTHS-LEEALRAEELGADYVGFGPVFPTPTKPGAgPPLGLELLREIAELVEIPVVAIGG 158

                        170       180
                 ....*....|....*....|
gi 489183710 164 ISLDTAPGLIARGVDLVAVI 183
Cdd:cd00564  159 ITPENAAEVLAAGADGVAVI 178
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 1-209 4.28e-63

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: 194.63  E-value: 4.28e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   1 MKLRGLYAITDSQLLDDgRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV- 79
Cdd:COG0352    1 MTLPRLYLITDPDLCGR-DLLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGAd 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  80 GLHLGQTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGA-PAASVELLDQARPRLHLPI 158
Cdd:COG0352   80 GVHLGQEDLPVAEARALLGPDLIIGVSCHS-LEEALRAEEAGADYVGFGPVFPTPTKPGApPPLGLEGLAWWAELVEIPV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489183710 159 TAIGGISLDTAPGLIARGVDLVAVIhalFAAASAAEVERRARAFSALFEPA 209
Cdd:COG0352  159 VAIGGITPENAAEVLAAGADGVAVI---SAIWGAPDPAAAARELRAALEAA 206
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 6-183 7.04e-62

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: 190.45  E-value: 7.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710    6 LYAITDSQLlDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV-GLHLG 84
Cdd:pfam02581   1 LYLVTDPGL-DGEDLLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGAdGVHLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   85 QTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGAPAASVELLDQARPRLHLPITAIGGI 164
Cdd:pfam02581  80 QDDLPVAEARELLGPDLIIGVSTHT-LEEALEAEALGADYIGFGPIFPTPTKPDAPPLGLEGLKAIAEAVEIPVVAIGGI 158

                         170
                  ....*....|....*....
gi 489183710  165 SLDTAPGLIARGVDLVAVI 183
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVV 177
PRK02615 PRK02615
thiamine phosphate synthase;
6-183 7.82e-49

thiamine phosphate synthase;


Pssm-ID: 235054 [Multi-domain]  Cd Length: 347  Bit Score: 162.36  E-value: 7.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   6 LYAITDsqllDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAarLGV---GLH 82
Cdd:PRK02615 149 LYLITS----PSENLLEVVEAALKGGVTLVQYRDKTADDRQRLEEAKKLKELCHRYGALFIVNDRVDIA--LAVdadGVH 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  83 LGQTDGSLSAARALLGRQAIIGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGAPAASVELLDQARPRLHLPITAIG 162
Cdd:PRK02615 223 LGQEDLPLAVARQLLGPEKIIGRSTTN-PEEMAKAIAEGADYIGVGPVFPTPTKPGKAPAGLEYLKYAAKEAPIPWFAIG 301

                        170       180
                 ....*....|....*....|.
gi 489183710 163 GISLDTAPGLIARGVDLVAVI 183
Cdd:PRK02615 302 GIDKSNIPEVLQAGAKRVAVV 322
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 6-183 1.73e-30

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 116.79  E-value: 1.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   6 LYAITDSQLLDD-GRLLP-YVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELA-ARLGVGLH 82
Cdd:PLN02898 293 LYAVTDSGMNKKwGRSTVdAVRAAIEGGATIVQLREKEAETREFIEEAKACLAICRSYGVPLLINDRVDVAlACDADGVH 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  83 LGQTDGSLSAARALLGRQAIIGATCHaQLELAEQAVAEGASYVAFGRFFNSSTKPGAPAASVELLDQARPRLHLPITAIG 162
Cdd:PLN02898 373 LGQSDMPVRLARSLLGPGKIIGVSCK-TPEQAEQAWKDGADYIGCGGVFPTNTKANNKTIGLDGLREVCEASKLPVVAIG 451

                        170       180
                 ....*....|....*....|....
gi 489183710 163 GISLDTAPGLIARGVDL---VAVI 183
Cdd:PLN02898 452 GISASNAASVMESGAPNlkgVAVV 475
PRK03512 PRK03512
thiamine phosphate synthase;
5-183 3.29e-20

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 84.34  E-value: 3.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   5 GLYAITDSqllddgrlLPYVEAALRGGARLLQYR--DKSSDQArrlrEAESLR--ELCERHGAQLIVNDDAELAARLGV- 79
Cdd:PRK03512  14 GLYPVVDS--------VQWIERLLDAGVRTLQLRikDRRDEEV----EADVVAaiALGRRYQARLFINDYWRLAIKHQAy 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  80 GLHLGQTD---GSLSAARALLGRqaiIGATCHAQLELAEqAVAEGASYVAFGRFFNSSTK--PGAPAASVELLDQARPRL 154
Cdd:PRK03512  82 GVHLGQEDletADLNAIRAAGLR---LGVSTHDDMEIDV-ALAARPSYIALGHVFPTQTKqmPSAPQGLAQLARHVERLA 157

                        170       180
                 ....*....|....*....|....*....
gi 489183710 155 HLPITAIGGISLDTAPGLIARGVDLVAVI 183
Cdd:PRK03512 158 DYPTVAIGGISLERAPAVLATGVGSIAVV 186
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 6-209 7.73e-20

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 86.95  E-value: 7.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   6 LYAITDSQLLDDGRLLP-YVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGVGLHLG 84
Cdd:PRK09517   6 LYLVTDPVLGGGPEKVAgIVDSAISGGVSVVQLRDKNAGVEDVRAAAKELKELCDARGVALVVNDRLDVAVELGLHVHIG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  85 QTDGSLSAARALLGRQAIIGATC------HAQLELAEQAVAEGASYVAFGRFFNSSTKPGAPAA----SVELLDQARPRL 154
Cdd:PRK09517  86 QGDTPYTQARRLLPAHLELGLTIetldqlEAVIAQCAETGVALPDVIGIGPVASTATKPDAPPAlgvdGIAEIAAVAQDH 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489183710 155 HLPITAIGGISLDTAPGLIARGVDLVAVIHALFAAASAAEVERR-ARAFSALFEPA 209
Cdd:PRK09517 166 GIASVAIGGVGLRNAAELAATGIDGLCVVSAIMAAANPAAAARElRTAFQPTRSPE 221
PRK08999 PRK08999
Nudix family hydrolase;
7-168 7.21e-19

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 82.61  E-value: 7.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   7 YAITDSQLLDDGRLLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV-GLHLGQ 85
Cdd:PRK08999 133 YLITPEGEDGDAAFLARLERALAAGIRLIQLRAPQLPPAAYRALARAALGLCRRAGAQLLLNGDPELAEDLGAdGVHLTS 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  86 TDGSLSAARALLGRQaIIGATCHAQLELAeQAVAEGASYVAFGRFFNSSTKPGAPAASVELLDQARPRLHLPITAIGGIS 165
Cdd:PRK08999 213 AQLAALAARPLPAGR-WVAASCHDAEELA-RAQRLGVDFAVLSPVQPTASHPGAAPLGWEGFAALIAGVPLPVYALGGLG 290


                 ...
gi 489183710 166 LDT 168
Cdd:PRK08999 291 PGD 293
PRK07695 PRK07695
thiazole tautomerase TenI;
64-183 1.32e-16

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 74.67  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  64 QLIVNDDAELAARLGV-GLHLGQTDGSLSAARALLGRQAIiGATCHAqLELAEQAVAEGASYVAFGRFFNSSTKPGAPAA 142
Cdd:PRK07695  59 KLIINDRVDIALLLNIhRVQLGYRSFSVRSVREKFPYLHV-GYSVHS-LEEAIQAEKNGADYVVYGHVFPTDCKKGVPAR 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489183710 143 SVELLDQARPRLHLPITAIGGISLDTAPGLIARGVDLVAVI 183
Cdd:PRK07695 137 GLEELSDIARALSIPVIAIGGITPENTRDVLAAGVSGIAVM 177
thiE PRK12290
thiamine phosphate synthase;
5-183 2.02e-11

thiamine phosphate synthase;


Pssm-ID: 237041 [Multi-domain]  Cd Length: 437  Bit Score: 62.12  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710   5 GLYAITDSqllddgrlLPYVEAALRGGARLLQYRDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV-GLHL 83
Cdd:PRK12290 212 GLYPVVDD--------VEWIERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAyGVHL 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  84 GQTDGSLSAARALLGRQAIIGATCHAQLELAeQAVAEGASYVAFGRFFNSSTK--PGAP------AASVELLDQA--RPR 153
Cdd:PRK12290 284 GQEDLEEANLAQLTDAGIRLGLSTHGYYELL-RIVQIQPSYIALGHIFPTTTKqmPSKPqglvrlALYQKLIDTIpyQGQ 362

                        170       180       190
                 ....*....|....*....|....*....|
gi 489183710 154 LHLPITAIGGISLDTAPGLIARGVDLVAVI 183
Cdd:PRK12290 363 TGFPTVAIGGIDQSNAEQVWQCGVSSLAVV 392
PRK06512 PRK06512
thiamine phosphate synthase;
14-182 1.32e-03

thiamine phosphate synthase;


Pssm-ID: 180598  Cd Length: 221  Bit Score: 38.50  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  14 LLDDGRLLP-YVEAALRGG--ARLLQYrDKSSDQARRLREAESLRELCERHGAQLIVNDDAELAARLGV-GLHLGQTDGS 89
Cdd:PRK06512  21 PIADGAELAkLLRAALQGGdvASVILP-QYGLDEATFQKQAEKLVPVIQEAGAAALIAGDSRIAGRVKAdGLHIEGNLAA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489183710  90 LSAARALLGRQAIIGA----TCHAQLELAEQavaeGASYVAFGRfFNSSTKPGAPAASVELLDQARPRLHLPITAIGGIS 165
Cdd:PRK06512 100 LAEAIEKHAPKMIVGFgnlrDRHGAMEIGEL----RPDYLFFGK-LGADNKPEAHPRNLSLAEWWAEMIEIPCIVQAGSD 174

                        170
                 ....*....|....*..
gi 489183710 166 LDTAPGLIARGVDLVAV 182
Cdd:PRK06512 175 LASAVEVAETGAEFVAL 191
 
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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