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Conserved domains on  [gi|4699824]
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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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
thiE PRK00043
thiamine-phosphate pyrophosphorylase; Reviewed
13-224 1.74e-97

thiamine-phosphate pyrophosphorylase; Reviewed


:

Pssm-ID: 234590  Cd Length: 212  Bit Score: 282.46  E-value: 1.74e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    13 MMKELLSVYFIMGSNN-TKADPVTVVQKALKGGATLYQFREKGgdaLTGEARIKFAEKAQAACREAGVPFIVNDDVELAL 91
Cdd:PRK00043   2 MMMKLLRLYLITDSRDdSGRDLLEVVEAALEGGVTLVQLREKG---LDTRERLELARALKELCRRYGVPLIVNDRVDLAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    92 NLKADGIHIGQEDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGVSLIEAVRRQG 170
Cdd:PRK00043  79 AVGADGVHLGQDDLPVADARALLGpDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAV 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4699824   171 ISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQTYK 224
Cdd:PRK00043 159 GDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
 
Name Accession Description Interval E-value
thiE PRK00043
thiamine-phosphate pyrophosphorylase; Reviewed
13-224 1.74e-97

thiamine-phosphate pyrophosphorylase; Reviewed


Pssm-ID: 234590  Cd Length: 212  Bit Score: 282.46  E-value: 1.74e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    13 MMKELLSVYFIMGSNN-TKADPVTVVQKALKGGATLYQFREKGgdaLTGEARIKFAEKAQAACREAGVPFIVNDDVELAL 91
Cdd:PRK00043   2 MMMKLLRLYLITDSRDdSGRDLLEVVEAALEGGVTLVQLREKG---LDTRERLELARALKELCRRYGVPLIVNDRVDLAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    92 NLKADGIHIGQEDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGVSLIEAVRRQG 170
Cdd:PRK00043  79 AVGADGVHLGQDDLPVADARALLGpDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAV 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4699824   171 ISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQTYK 224
Cdd:PRK00043 159 GDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
19-216 2.98e-88

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: 258.72  E-value: 2.98e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824     19 SVYFIMGSNNTKADPVTVVQKALKGGATLYQFREKGGDAltgEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGI 98
Cdd:TIGR00693   1 GLYLITDPQDGPADLLNRVEAALKGGVTLVQLRDKGSNT---RERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824     99 HIGQEDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGVSLIEAVRRQGISIPIVG 177
Cdd:TIGR00693  78 HLGQDDLPASEARALLGpDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVA 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 4699824    178 IGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKF 216
Cdd:TIGR00693 158 IGGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
20-218 2.86e-84

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: 248.59  E-value: 2.86e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   20 VYFIMGSNNTKADPVTVVQKALKGGATLYQFREKGGDAltgEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIH 99
Cdd:cd00564   1 LYLITDRRLDGEDLLEVVEAALKGGVTLVQLREKDLSA---RELLELARALRELCRKYGVPLIINDRVDLALAVGADGVH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824  100 IGQEDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGVSLIEAVRRQgISIPIVGI 178
Cdd:cd00564  78 LGQDDLPVAEARALLGpDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAEL-VEIPVVAI 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4699824  179 GGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFRE 218
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism];
13-224 1.77e-77

Thiamine monophosphate synthase [Coenzyme transport and metabolism];


Pssm-ID: 223429  Cd Length: 211  Bit Score: 231.76  E-value: 1.77e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   13 MMKELLSVYFIMGSNNTK--ADPVTVVQKALKGGATLYQFREKGGDAltgEARIKFAEKAQAACREAGVPFIVNDDVELA 90
Cdd:COG0352   1 MSMELLRLYLVTDRPLIYdgVDLLEWVEAALKGGVTAVQLREKDLSD---EEYLALAEKLRALCQKYGVPLIINDRVDLA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   91 LNLKADGIHIGQEDANAKEVRAAIGD-MILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDtRAVQGVSLIEAVrRQ 169
Cdd:COG0352  78 LAVGADGVHLGQDDMPLAEARELLGPgLIIGLSTHDLEEALEAEELGADYVGLGPIFPTSTKPD-APPLGLEGLREI-RE 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4699824  170 GISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQTYK 224
Cdd:COG0352 156 LVNIPVVAIGGINLENVPEVLEAGADGVAVVSAITSAADPAAAAKALRNALEDEK 210
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
20-203 1.24e-73

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: 280703 [Multi-domain]  Cd Length: 180  Bit Score: 220.88  E-value: 1.24e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824     20 VYFIMGSNNTKADPVTVVQKALKGGATLYQFREKGGDAltgEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIH 99
Cdd:pfam02581   1 LYLVTDPGLDGEDLLEVVEEALKGGVTIVQLREKDLDD---REFLELARRLRALCRKYGVPLIINDRVDLALAVGADGVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    100 IGQEDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDtRAVQGVSLIEAVrRQGISIPIVGI 178
Cdd:pfam02581  78 LGQDDLPVAEARELLGpDLIIGVSTHTLEEALEAEALGADYIGFGPVFPTPTKPD-APPLGLEGLKAI-AEAVNIPVVAI 155
                         170       180
                  ....*....|....*....|....*
gi 4699824    179 GGITIDNAAPVIQAGADGVSMISAI 203
Cdd:pfam02581 156 GGITPENVPEVIEAGADGVAVVSAI 180
 
Name Accession Description Interval E-value
thiE PRK00043
thiamine-phosphate pyrophosphorylase; Reviewed
13-224 1.74e-97

thiamine-phosphate pyrophosphorylase; Reviewed


Pssm-ID: 234590  Cd Length: 212  Bit Score: 282.46  E-value: 1.74e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    13 MMKELLSVYFIMGSNN-TKADPVTVVQKALKGGATLYQFREKGgdaLTGEARIKFAEKAQAACREAGVPFIVNDDVELAL 91
Cdd:PRK00043   2 MMMKLLRLYLITDSRDdSGRDLLEVVEAALEGGVTLVQLREKG---LDTRERLELARALKELCRRYGVPLIVNDRVDLAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    92 NLKADGIHIGQEDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGVSLIEAVRRQG 170
Cdd:PRK00043  79 AVGADGVHLGQDDLPVADARALLGpDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAV 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4699824   171 ISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQTYK 224
Cdd:PRK00043 159 GDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
19-216 2.98e-88

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: 258.72  E-value: 2.98e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824     19 SVYFIMGSNNTKADPVTVVQKALKGGATLYQFREKGGDAltgEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGI 98
Cdd:TIGR00693   1 GLYLITDPQDGPADLLNRVEAALKGGVTLVQLRDKGSNT---RERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824     99 HIGQEDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGVSLIEAVRRQGISIPIVG 177
Cdd:TIGR00693  78 HLGQDDLPASEARALLGpDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVA 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 4699824    178 IGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKF 216
Cdd:TIGR00693 158 IGGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
20-218 2.86e-84

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: 248.59  E-value: 2.86e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   20 VYFIMGSNNTKADPVTVVQKALKGGATLYQFREKGGDAltgEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIH 99
Cdd:cd00564   1 LYLITDRRLDGEDLLEVVEAALKGGVTLVQLREKDLSA---RELLELARALRELCRKYGVPLIINDRVDLALAVGADGVH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824  100 IGQEDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGVSLIEAVRRQgISIPIVGI 178
Cdd:cd00564  78 LGQDDLPVAEARALLGpDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAEL-VEIPVVAI 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 4699824  179 GGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFRE 218
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism];
13-224 1.77e-77

Thiamine monophosphate synthase [Coenzyme transport and metabolism];


Pssm-ID: 223429  Cd Length: 211  Bit Score: 231.76  E-value: 1.77e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   13 MMKELLSVYFIMGSNNTK--ADPVTVVQKALKGGATLYQFREKGGDAltgEARIKFAEKAQAACREAGVPFIVNDDVELA 90
Cdd:COG0352   1 MSMELLRLYLVTDRPLIYdgVDLLEWVEAALKGGVTAVQLREKDLSD---EEYLALAEKLRALCQKYGVPLIINDRVDLA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   91 LNLKADGIHIGQEDANAKEVRAAIGD-MILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDtRAVQGVSLIEAVrRQ 169
Cdd:COG0352  78 LAVGADGVHLGQDDMPLAEARELLGPgLIIGLSTHDLEEALEAEELGADYVGLGPIFPTSTKPD-APPLGLEGLREI-RE 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4699824  170 GISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQTYK 224
Cdd:COG0352 156 LVNIPVVAIGGINLENVPEVLEAGADGVAVVSAITSAADPAAAAKALRNALEDEK 210
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
20-203 1.24e-73

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: 280703 [Multi-domain]  Cd Length: 180  Bit Score: 220.88  E-value: 1.24e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824     20 VYFIMGSNNTKADPVTVVQKALKGGATLYQFREKGGDAltgEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIH 99
Cdd:pfam02581   1 LYLVTDPGLDGEDLLEVVEEALKGGVTIVQLREKDLDD---REFLELARRLRALCRKYGVPLIINDRVDLALAVGADGVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    100 IGQEDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDtRAVQGVSLIEAVrRQGISIPIVGI 178
Cdd:pfam02581  78 LGQDDLPVAEARELLGpDLIIGVSTHTLEEALEAEALGADYIGFGPVFPTPTKPD-APPLGLEGLKAI-AEAVNIPVVAI 155
                         170       180
                  ....*....|....*....|....*
gi 4699824    179 GGITIDNAAPVIQAGADGVSMISAI 203
Cdd:pfam02581 156 GGITPENVPEVIEAGADGVAVVSAI 180
PRK02615 PRK02615
thiamine-phosphate pyrophosphorylase; Provisional
36-225 2.06e-58

thiamine-phosphate pyrophosphorylase; Provisional


Pssm-ID: 235054  Cd Length: 347  Bit Score: 187.78  E-value: 2.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    36 VVQKALKGGATLYQFREKGGDALTgeaRIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIHIGQEDANAKEVRAAIG 115
Cdd:PRK02615 162 VVEAALKGGVTLVQYRDKTADDRQ---RLEEAKKLKELCHRYGALFIVNDRVDIALAVDADGVHLGQEDLPLAVARQLLG 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   116 -DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVqGVSLIEAVrRQGISIPIVGIGGITIDNAAPVIQAGA 194
Cdd:PRK02615 239 pEKIIGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKPGKAPA-GLEYLKYA-AKEAPIPWFAIGGIDKSNIPEVLQAGA 316
                        170       180       190
                 ....*....|....*....|....*....|.
gi 4699824   195 DGVSMISAISQAEDPESAARKFREEIQTYKT 225
Cdd:PRK02615 317 KRVAVVRAIMGAEDPKQATQELLKQLSRENA 347
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
28-217 1.02e-46

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 161.09  E-value: 1.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    28 NTKADPVTV--VQKALKGGATLYQFREKggDALTGEarikFAEKAQA---ACREAGVPFIVNDDVELALNLKADGIHIGQ 102
Cdd:PLN02898 302 NKKWGRSTVdaVRAAIEGGATIVQLREK--EAETRE----FIEEAKAclaICRSYGVPLLINDRVDVALACDADGVHLGQ 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   103 EDANAKEVRAAIG-DMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVqGVSLIEAVRRqGISIPIVGIGGI 181
Cdd:PLN02898 376 SDMPVRLARSLLGpGKIIGVSCKTPEQAEQAWKDGADYIGCGGVFPTNTKANNKTI-GLDGLREVCE-ASKLPVVAIGGI 453
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4699824   182 TIDNAAPVIQAGA---DGVSMISAISQAEDPESAARKFR 217
Cdd:PLN02898 454 SASNAASVMESGApnlKGVAVVSALFDQEDVLKATRKLH 492
PRK07695 PRK07695
transcriptional regulator TenI; Provisional
76-221 5.66e-35

transcriptional regulator TenI; Provisional


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 122.82  E-value: 5.66e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    76 EAGVP---FIVNDDVELALNLKADGIHIGQEDANAKEVRAAIGDMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKK 152
Cdd:PRK07695  52 KKGVPaskLIINDRVDIALLLNIHRVQLGYRSFSVRSVREKFPYLHVGYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKK 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4699824   153 DTRAvQGVSLIEAVRRQgISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQ 221
Cdd:PRK07695 132 GVPA-RGLEELSDIARA-LSIPVIAIGGITPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAESIK 198
PRK08999 PRK08999
hypothetical protein; Provisional
37-203 1.58e-29

hypothetical protein; Provisional


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 111.50  E-value: 1.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    37 VQKALKGGATLYQFREKGGDAltgEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIHIGQEDANAKEVRAAIGD 116
Cdd:PRK08999 150 LERALAAGIRLIQLRAPQLPP---AAYRALARAALGLCRRAGAQLLLNGDPELAEDLGADGVHLTSAQLAALAARPLPAG 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   117 MILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAV--QGVslieAVRRQGISIPIVGIGGITIDNAAPVIQAGA 194
Cdd:PRK08999 227 RWVAASCHDAEELARAQRLGVDFAVLSPVQPTASHPGAAPLgwEGF----AALIAGVPLPVYALGGLGPGDLEEAREHGA 302

                 ....*....
gi 4699824   195 DGVSMISAI 203
Cdd:PRK08999 303 QGIAGIRGL 311
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
36-218 1.21e-28

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 112.76  E-value: 1.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    36 VVQKALKGGATLYQFREKGGDALTGEARIKfaeKAQAACREAGVPFIVNDDVELALNLKADgIHIGQEDANAKEVRAAI- 114
Cdd:PRK09517  24 IVDSAISGGVSVVQLRDKNAGVEDVRAAAK---ELKELCDARGVALVVNDRLDVAVELGLH-VHIGQGDTPYTQARRLLp 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   115 GDMILGVSAHTMSEVKQAEEDGA-------DYVGLGPIYPTETKKDTRA---VQGVSLIEAVRRQGiSIPIVGIGGITID 184
Cdd:PRK09517 100 AHLELGLTIETLDQLEAVIAQCAetgvalpDVIGIGPVASTATKPDAPPalgVDGIAEIAAVAQDH-GIASVAIGGVGLR 178
                        170       180       190
                 ....*....|....*....|....*....|....
gi 4699824   185 NAAPVIQAGADGVSMISAISQAEDPESAARKFRE 218
Cdd:PRK09517 179 NAAELAATGIDGLCVVSAIMAAANPAAAARELRT 212
PRK03512 PRK03512
thiamine-phosphate pyrophosphorylase; Provisional
32-215 3.78e-24

thiamine-phosphate pyrophosphorylase; Provisional


Pssm-ID: 179586  Cd Length: 211  Bit Score: 95.12  E-value: 3.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    32 DPVTVVQKALKGGATLYQFREKGGDALTGEARIkfaEKAQAACREAGVPFIVNDDVELALNLKADGIHIGQED---ANAK 108
Cdd:PRK03512  20 DSVQWIERLLDAGVRTLQLRIKDRRDEEVEADV---VAAIALGRRYQARLFINDYWRLAIKHQAYGVHLGQEDletADLN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   109 EVRAAigDMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGVS-LIEAVRRQGiSIPIVGIGGITIDNAA 187
Cdd:PRK03512  97 AIRAA--GLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAqLARHVERLA-DYPTVAIGGISLERAP 173
                        170       180
                 ....*....|....*....|....*...
gi 4699824   188 PVIQAGADGVSMISAISQAEDPESAARK 215
Cdd:PRK03512 174 AVLATGVGSIAVVSAITQAADWRAATAQ 201
thiE PRK12290
thiamine-phosphate pyrophosphorylase; Reviewed
32-225 2.41e-21

thiamine-phosphate pyrophosphorylase; Reviewed


Pssm-ID: 237041  Cd Length: 437  Bit Score: 91.01  E-value: 2.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    32 DPVTVVQKALKGGATLYQFREKGGDALTGEARIkfaEKAQAACREAGVPFIVNDDVELALNLKADGIHIGQED---ANAK 108
Cdd:PRK12290 218 DDVEWIERLLPLGINTVQLRIKDPQQADLEQQI---IRAIALGREYNAQVFINDYWQLAIKHQAYGVHLGQEDleeANLA 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   109 EV-RAAIGdmiLGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQGV-------SLIEAVRRQGI-SIPIVGIG 179
Cdd:PRK12290 295 QLtDAGIR---LGLSTHGYYELLRIVQIQPSYIALGHIFPTTTKQMPSKPQGLvrlalyqKLIDTIPYQGQtGFPTVAIG 371
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 4699824   180 GITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQTYKT 225
Cdd:PRK12290 372 GIDQSNAEQVWQCGVSSLAVVRAITLAEDPQLVIEFFDQVMAENQL 417
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
20-201 5.26e-17

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 76.09  E-value: 5.26e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   20 VYFIMGSNNTKADPVTVVQKALKGGATLYQFREKGGDALTGEARIKfaEKAQAACREAGVPFIVND-----------DVE 88
Cdd:cd04722   1 VILALLAGGPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDK--EVLKEVAAETDLPLGVQLaindaaaavdiAAA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   89 LALNLKADGIHIGQE--------DANAKEVRAAIGDMILGV--SAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRAVQ 158
Cdd:cd04722  79 AARAAGADGVEIHGAvgylaredLELIRELREAVPDVKVVVklSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIA 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4699824  159 GVSLIEAvrRQGISIPIVGIGGITI-DNAAPVIQAGADGVSMIS 201
Cdd:cd04722 159 DLLLILA--KRGSKVPVIAGGGINDpEDAAEALALGADGVIVGS 200
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
129-220 2.86e-07

3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate synthase (HPS), or the HPS domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis, at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin. In these species, the enzyme is viewed as a lyase rather than a synthase and is called D-arabino 3-hexulose 6-phosphate formaldehyde lyase. Note that there is some overlap in specificity with the Escherichia coli enzyme 3-keto-L-gulonate 6-phosphate decarboxylase.


Pssm-ID: 132172  Cd Length: 206  Bit Score: 48.91  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    129 VKQAEEDGADYVGLGPIYPTETKKDTRAVQGVSLIEAVRRQGISIPivgiGGITIDNAAPVIQAGADGVSMISAISQAED 208
Cdd:TIGR03128 119 AKELKELGADYIGVHTGLDEQAKGQNPFEDLQTILKLVKEARVAVA----GGINLDTIPDVIKLGPDIVIVGGAITKAAD 194
                          90
                  ....*....|..
gi 4699824    209 PESAARKFREEI 220
Cdd:TIGR03128 195 PAEAARQIRKLI 206
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
116-216 1.06e-06

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  Cd Length: 202  Bit Score: 47.58  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824  116 DMIlgvSAHTMSEVKQAEEDGADYVGLgpiyptETKKDTRAVQGVSLIEAVRRQG--ISIPIVGIGGITIDNAAPVIQAG 193
Cdd:cd04726 109 DLI---GVEDPEKRAKLLKLGVDIVIL------HRGIDAQAAGGWWPEDDLKKVKklLGVKVAVAGGITPDTLPEFKKAG 179
                        90       100
                ....*....|....*....|...
gi 4699824  194 ADGVSMISAISQAEDPESAARKF 216
Cdd:cd04726 180 ADIVIVGRAITGAADPAEAAREF 202
PRK06512 PRK06512
thiamine-phosphate pyrophosphorylase; Provisional
31-212 1.73e-05

thiamine-phosphate pyrophosphorylase; Provisional


Pssm-ID: 180598  Cd Length: 221  Bit Score: 43.90  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824    31 ADPVTVVQKALKGGAT----LYQFrekGGDALTGEariKFAEKAQAACREAGVPFIVNDDVELALNLKADGIHIgqeDAN 106
Cdd:PRK06512  26 AELAKLLRAALQGGDVasviLPQY---GLDEATFQ---KQAEKLVPVIQEAGAAALIAGDSRIAGRVKADGLHI---EGN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   107 AKEVRAAIG----DMILGVSA-----HTMsevkQAEEDGADYVGLGPIypTETKKDTRAVQGVSLIE--AvrrQGISIPI 175
Cdd:PRK06512  97 LAALAEAIEkhapKMIVGFGNlrdrhGAM----EIGELRPDYLFFGKL--GADNKPEAHPRNLSLAEwwA---EMIEIPC 167
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 4699824   176 VGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESA 212
Cdd:PRK06512 168 IVQAGSDLASAVEVAETGAEFVALERAVFDAHDPPLA 204
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
28-219 1.83e-05

KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.


Pssm-ID: 188632  Cd Length: 190  Bit Score: 43.66  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   28 NTKADPVTVVQKALKGGAT--------------LYQFREKGGDALTGEARIKFAEKAQAAcREAGVPFIV--NDDVELAL 91
Cdd:cd00452  13 DDAEDALALAEALIEGGIRaieitlrtpgaleaIRALRKEFPEALIGAGTVLTPEQADAA-IAAGAQFIVspGLDPEVVK 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   92 NLKADGIHIgqedanakevraaigdmILGVSahTMSEVKQAEEDGADYVGLGPIyptetkkdtrAVQGVSLIEAVRRQGI 171
Cdd:cd00452  92 AANRAGIPL-----------------LPGVA--TPTEIMQALELGADIVKLFPA----------EAVGPAYIKALKGPFP 142
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 4699824  172 SIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREE 219
Cdd:cd00452 143 QVRFMPTGGVSLDNAAEWLAAGVVAVGGGSLLPKDAVAAGDWAAITAL 190
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
130-224 3.68e-05

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 43.86  E-value: 3.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   130 KQAEEDGADY----VGLgpiyptetkkdTRAVQGVSLIEAVR--RQGISIPIVGIGGITIDNAAPVIQAGADGVSMISAI 203
Cdd:PRK07028 125 VELEELGVDYinvhVGI-----------DQQMLGKDPLELLKevSEEVSIPIAVAGGLDAETAAKAVAAGADIVIVGGNI 193
                         90       100
                 ....*....|....*....|.
gi 4699824   204 SQAEDPESAARKFREEIQTYK 224
Cdd:PRK07028 194 IKSADVTEAARKIREAIDSGK 214
PRK07455 PRK07455
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
117-197 3.95e-05

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


Pssm-ID: 180985  Cd Length: 187  Bit Score: 42.72  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   117 MILGvsAHTMSEVKQAEEDGADYVGLGPIyptetkkdtRAVQGVSLIEAVRRQGISIPIVGIGGITIDNAAPVIQAGADG 196
Cdd:PRK07455 108 IIPG--ALTPTEIVTAWQAGASCVKVFPV---------QAVGGADYIKSLQGPLGHIPLIPTGGVTLENAQAFIQAGAIA 176

                 .
gi 4699824   197 V 197
Cdd:PRK07455 177 V 177
PBP1_ABC_ligand_binding_like_13 cd06348
Type I periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
156-221 3.23e-04

Type I periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type I periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine/isoleucine/valine binding protein (LIVBP); however its ligand specificity has not been determined experimentally.


Pssm-ID: 107343 [Multi-domain]  Cd Length: 344  Bit Score: 40.92  E-value: 3.23e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4699824  156 AVQGVSLIEAVRRQGISIPIVGIGGITIDNAAPVIQAGADGVSMISAISqAEDPESAARKFREEIQ 221
Cdd:cd06348 202 AADGGNLVRQLRELGYNGLIVGGNGFNTPNVFPVCQAACDGVLVAQAYS-PENDTPVNRDFVEAYK 266
ThiG COG2022
Thiamin biosynthesis thiazole synthase ThiGH, ThiG subunit [Coenzyme transport and metabolism]; ...
168-221 4.31e-04

Thiamin biosynthesis thiazole synthase ThiGH, ThiG subunit [Coenzyme transport and metabolism];


Pssm-ID: 224933  Cd Length: 262  Bit Score: 40.31  E-value: 4.31e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4699824  168 RQGISIPIV---GIGgiTIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQ 221
Cdd:COG2022 178 IEEADVPVIvdaGIG--TPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFALAVE 232
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
108-199 4.68e-04

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 40.25  E-value: 4.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824  108 KEVRAAIG-DMILGV--SAH-------TMSE----VKQAEEDGADY--VGLGPIYPTETKKDTRAVQGVSLIEAVR--RQ 169
Cdd:cd02803 199 AAVREAVGpDFPVGVrlSADdfvpgglTLEEaieiAKALEEAGVDAlhVSGGSYESPPPIIPPPYVPEGYFLELAEkiKK 278
                        90       100       110
                ....*....|....*....|....*....|..
gi 4699824  170 GISIPIVGIGGI-TIDNAAPVIQAG-ADGVSM 199
Cdd:cd02803 279 AVKIPVIAVGGIrDPEVAEEILAEGkADLVAL 310
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
165-223 5.79e-04

Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240091  Cd Length: 296  Bit Score: 39.84  E-value: 5.79e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4699824  165 AVR-----RQGISIPIVGIGGI-TIDNAAPVIQAGADGVSMISAISqaEDPEsAARKFREEIQTY 223
Cdd:cd04740 219 ALRmvyqvYKAVEIPIIGVGGIaSGEDALEFLMAGASAVQVGTANF--VDPE-AFKEIIEGLEAY 280
ThiG pfam05690
Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole ...
168-221 6.11e-04

Thiazole biosynthesis protein ThiG; This family consists of several bacterial thiazole biosynthesis protein G sequences. ThiG, together with ThiF and ThiH, is proposed to be involved in the synthesis of 4-methyl-5-(b-hydroxyethyl)thiazole (THZ) which is an intermediate in the thiazole production pathway. This family also includes triosephosphate isomerase and pyridoxal 5'-phosphate synthase subunit PdxS.


Pssm-ID: 336186  Cd Length: 247  Bit Score: 39.53  E-value: 6.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4699824    168 RQGISIPIV---GIGgiTIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQ 221
Cdd:pfam05690 171 IEEADVPVIvdaGIG--TPSDAAQAMELGADAVLLNTAIARAKDPVAMARAFKLAVE 225
SgbH COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
179-220 7.13e-04

3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];


Pssm-ID: 223347  Cd Length: 217  Bit Score: 39.16  E-value: 7.13e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 4699824  179 GGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEI 220
Cdd:COG0269 171 GGITPEDIPLFKGIGADIVIVGRAITGAKDPAEAARKFKEEI 212
thiG PRK00208
thiazole synthase; Reviewed
163-221 7.21e-04

thiazole synthase; Reviewed


Pssm-ID: 234687  Cd Length: 250  Bit Score: 39.27  E-value: 7.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4699824   163 IEAVRRQgISIPIV---GIGgiTIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQ 221
Cdd:PRK00208 167 LRIIIEQ-ADVPVIvdaGIG--TPSDAAQAMELGADAVLLNTAIAVAGDPVAMARAFKLAVE 225
ThiG cd04728
Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the ...
162-217 7.85e-04

Thiazole synthase (ThiG) is the tetrameric enzyme that is involved in the formation of the thiazole moiety of thiamin pyrophosphate, an essential ubiquitous cofactor that plays an important role in carbohydrate and amino acid metabolism. ThiG catalyzes the formation of thiazole from 1-deoxy-D-xylulose 5-phosphate (DXP) and dehydroglycine, with the help of the sulfur carrier protein ThiS that carries the sulfur needed for thiazole assembly on its carboxy terminus (ThiS-COSH).


Pssm-ID: 240079  Cd Length: 248  Bit Score: 39.39  E-value: 7.85e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4699824  162 LIEAVRRQgISIPIV---GIGgiTIDNAAPVIQAGADGVSMISAISQAEDPESAARKFR 217
Cdd:cd04728 166 NLRIIIER-ADVPVIvdaGIG--TPSDAAQAMELGADAVLLNTAIAKAKDPVAMARAFK 221
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
185-221 1.72e-03

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 38.04  E-value: 1.72e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 4699824   185 NAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQ 221
Cdd:PRK13813 177 KAADAIKAGADYVIVGRSIYNAADPREAAKAINEEIR 213
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
179-217 1.95e-03

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 37.84  E-value: 1.95e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 4699824  179 GGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKFR 217
Cdd:cd00429 173 GGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK01130 PRK01130
N-acetylmannosamine-6-phosphate 2-epimerase; Provisional
125-221 2.11e-03

N-acetylmannosamine-6-phosphate 2-epimerase; Provisional


Pssm-ID: 234907  Cd Length: 221  Bit Score: 37.82  E-value: 2.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824   125 TMSEVKQAEEDGADYVGL---GpiYPTETKKdtRAVQGVSLIEAVRRQgISIPIVGIGGI-TIDNAAPVIQAGADGVSMI 200
Cdd:PRK01130 128 TLEEGLAAQKLGFDFIGTtlsG--YTEETKK--PEEPDFALLKELLKA-VGCPVIAEGRInTPEQAKKALELGAHAVVVG 202
                         90       100
                 ....*....|....*....|.
gi 4699824   201 SAISqaeDPESAARKFREEIQ 221
Cdd:PRK01130 203 GAIT---RPEEITKWFVDALK 220
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
125-216 5.47e-03

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080  Cd Length: 219  Bit Score: 36.78  E-value: 5.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4699824  125 TMSEVKQAEEDGADYVG---LGpiYPTETKKDTRAvqGVSLIEAVRRQgISIPIVGIGGI-TIDNAAPVIQAGADGVSMI 200
Cdd:cd04729 132 TLEEALNAAKLGFDIIGttlSG--YTEETAKTEDP--DFELLKELRKA-LGIPVIAEGRInSPEQAAKALELGADAVVVG 206
                        90
                ....*....|....*.
gi 4699824  201 SAISqaeDPESAARKF 216
Cdd:cd04729 207 SAIT---RPEHITGWF 219
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
169-227 5.89e-03

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 37.03  E-value: 5.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4699824   169 QGISIPIV---GIGgiTIDNAAPVIQAGADGVSMISAISQAEDPESAARKFREEIQ----TYKTGR 227
Cdd:PRK11840 246 EGATVPVLvdaGVG--TASDAAVAMELGCDGVLMNTAIAEAKNPVLMARAMKLAVEagrlAYLAGR 309
PRK13307 PRK13307
bifunctional formaldehyde-activating enzyme/3-hexulose-6-phosphate synthase; Provisional
162-224 7.17e-03

bifunctional formaldehyde-activating enzyme/3-hexulose-6-phosphate synthase; Provisional


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 36.53  E-value: 7.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4699824   162 LIEAVRRQGISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAEDPESAARKF----REEIQTYK 224
Cdd:PRK13307 320 NIKEIKKAGGKILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDFlnklKPDIDQFR 386
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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