NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446206770|ref|WP_000284625|]
View 

MULTISPECIES: thiamine phosphate synthase [Salmonella]

Protein Classification

thiamine phosphate synthase( domain architecture ID 10792278)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
1-211 9.82e-160

thiamine phosphate synthase;


:

Pssm-ID: 179586  Cd Length: 211  Bit Score: 439.49  E-value: 9.82e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   1 MYQPDFPTVPFRLGLYPVVDSVAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRA 80
Cdd:PRK03512   1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  81 YGVHLGQEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARHIERLADYP 160
Cdd:PRK03512  81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446206770 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATQQLLAIAGVGDE 211
Cdd:PRK03512 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
 
Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
1-211 9.82e-160

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 439.49  E-value: 9.82e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   1 MYQPDFPTVPFRLGLYPVVDSVAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRA 80
Cdd:PRK03512   1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  81 YGVHLGQEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARHIERLADYP 160
Cdd:PRK03512  81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446206770 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATQQLLAIAGVGDE 211
Cdd:PRK03512 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 15-204 3.57e-73

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: 219.70  E-value: 3.57e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  15 LYPVVDS-------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLGQ 87
Cdd:cd00564    1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  88 EDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLaRHIERLADYPTVAIGGI 167
Cdd:cd00564   81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELL-REIAELVEIPVVAIGGI 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446206770 168 SLERAPAVLATGVGSIAVVSAITQAADWRAATQQLLA 204
Cdd:cd00564  160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 12-205 4.14e-73

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: 220.06  E-value: 4.14e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  12 RLGLYPVVDS-------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVH 84
Cdd:COG0352    3 LPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGVH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  85 LGQEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARhIERLADYPTVAI 164
Cdd:COG0352   83 LGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAW-WAELVEIPVVAI 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446206770 165 GGISLERAPAVLATGVGSIAVVSAITQAADWRAATQQLLAI 205
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 14-202 1.06e-72

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: 218.66  E-value: 1.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   14 GLYPVVDS-------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLG 86
Cdd:TIGR00693   1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   87 QEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARHIERLADYPTVAIGG 166
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446206770  167 ISLERAPAVLATGVGSIAVVSAITQAADWRAATQQL 202
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 15-189 4.15e-61

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: 188.53  E-value: 4.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   15 LYPVVDS-------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLGQ 87
Cdd:pfam02581   1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   88 EDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSaPQGLAQLARHIERLAdYPTVAIGGI 167
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158

                         170       180
                  ....*....|....*....|..
gi 446206770  168 SLERAPAVLATGVGSIAVVSAI 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
 
Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
1-211 9.82e-160

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 439.49  E-value: 9.82e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   1 MYQPDFPTVPFRLGLYPVVDSVAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRA 80
Cdd:PRK03512   1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  81 YGVHLGQEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARHIERLADYP 160
Cdd:PRK03512  81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446206770 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATQQLLAIAGVGDE 211
Cdd:PRK03512 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
thiE PRK12290
thiamine phosphate synthase;
6-200 6.09e-90

thiamine phosphate synthase;


Pssm-ID: 237041 [Multi-domain]  Cd Length: 437  Bit Score: 270.90  E-value: 6.09e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   6 FPTV-PFRLGLYPVVDSVAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVH 84
Cdd:PRK12290 203 FPTLdKQSLGLYPVVDDVEWIERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAYGVH 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  85 LGQEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARHiERLAD------ 158
Cdd:PRK12290 283 LGQEDLEEANLAQLTDAGIRLGLSTHGYYELLRIVQIQPSYIALGHIFPTTTKQMPSKPQGLVRLALY-QKLIDtipyqg 361

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446206770 159 ---YPTVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATQ 200
Cdd:PRK12290 362 qtgFPTVAIGGIDQSNAEQVWQCGVSSLAVVRAITLAEDPQLVIE 406
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 15-204 3.57e-73

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: 219.70  E-value: 3.57e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  15 LYPVVDS-------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLGQ 87
Cdd:cd00564    1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  88 EDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLaRHIERLADYPTVAIGGI 167
Cdd:cd00564   81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELL-REIAELVEIPVVAIGGI 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446206770 168 SLERAPAVLATGVGSIAVVSAITQAADWRAATQQLLA 204
Cdd:cd00564  160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 12-205 4.14e-73

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: 220.06  E-value: 4.14e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  12 RLGLYPVVDS-------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVH 84
Cdd:COG0352    3 LPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGVH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  85 LGQEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARhIERLADYPTVAI 164
Cdd:COG0352   83 LGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAW-WAELVEIPVVAI 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446206770 165 GGISLERAPAVLATGVGSIAVVSAITQAADWRAATQQLLAI 205
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 14-202 1.06e-72

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: 218.66  E-value: 1.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   14 GLYPVVDS-------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLG 86
Cdd:TIGR00693   1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   87 QEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARHIERLADYPTVAIGG 166
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446206770  167 ISLERAPAVLATGVGSIAVVSAITQAADWRAATQQL 202
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
thiE PRK00043
thiamine phosphate synthase;
13-205 1.29e-63

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 196.17  E-value: 1.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  13 LGLYPVVDS--------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVH 84
Cdd:PRK00043   7 LRLYLITDSrddsgrdlLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVGADGVH 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  85 LGQEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSAPQGLAQLARHIERLADYPTVAI 164
Cdd:PRK00043  87 LGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAVGDIPIVAI 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446206770 165 GGISLERAPAVLATGVGSIAVVSAITQAADWRAATQQLLAI 205
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAA 207
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 15-189 4.15e-61

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: 188.53  E-value: 4.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   15 LYPVVDS-------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLGQ 87
Cdd:pfam02581   1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770   88 EDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQMPSaPQGLAQLARHIERLAdYPTVAIGGI 167
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158

                         170       180
                  ....*....|....*....|..
gi 446206770  168 SLERAPAVLATGVGSIAVVSAI 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
PRK02615 PRK02615
thiamine phosphate synthase;
25-205 7.94e-34

thiamine phosphate synthase;


Pssm-ID: 235054 [Multi-domain]  Cd Length: 347  Bit Score: 123.45  E-value: 7.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  25 IERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLGQEDLETTDLEAIQAAGLR 104
Cdd:PRK02615 163 VEAALKGGVTLVQYRDKTADDRQRLEEAKKLKELCHRYGALFIVNDRVDIALAVDADGVHLGQEDLPLAVARQLLGPEKI 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770 105 LGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQ--MPSAPQGLAQLARHIERladyPTVAIGGISLERAPAVLATGVGS 182
Cdd:PRK02615 243 IGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKPgkAPAGLEYLKYAAKEAPI----PWFAIGGIDKSNIPEVLQAGAKR 318

                        170       180
                 ....*....|....*....|...
gi 446206770 183 IAVVSAITQAADWRAATQQLLAI 205
Cdd:PRK02615 319 VAVVRAIMGAEDPKQATQELLKQ 341
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 10-205 2.11e-23

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 96.76  E-value: 2.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  10 PFRLGLYPVVDS----------VAWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHR 79
Cdd:PLN02898 288 PRNLFLYAVTDSgmnkkwgrstVDAVRAAIEGGATIVQLREKEAETREFIEEAKACLAICRSYGVPLLINDRVDVALACD 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  80 AYGVHLGQEDLETTDLEAIQAAGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQmpSAPQ-GLAQLaRHIERLAD 158
Cdd:PLN02898 368 ADGVHLGQSDMPVRLARSLLGPGKIIGVSCKTPEQAEQAWKDGADYIGCGGVFPTNTKA--NNKTiGLDGL-REVCEASK 444

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446206770 159 YPTVAIGGISLERAPAVLATGVGS---IAVVSAITQAADWRAATQQLLAI 205
Cdd:PLN02898 445 LPVVAIGGISASNAASVMESGAPNlkgVAVVSALFDQEDVLKATRKLHAI 494
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 13-203 8.80e-18

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 81.17  E-value: 8.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  13 LGLYPVVDSV---------AWIERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYgV 83
Cdd:PRK09517   4 FSLYLVTDPVlgggpekvaGIVDSAISGGVSVVQLRDKNAGVEDVRAAAKELKELCDARGVALVVNDRLDVAVELGLH-V 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  84 HLGQEDLETTDLEAIQAAGLRLGVS--THDDMEIDIALAAK-----PSYIALGHVFPTQTKqmPSAPQ-----GLAQLAR 151
Cdd:PRK09517  83 HIGQGDTPYTQARRLLPAHLELGLTieTLDQLEAVIAQCAEtgvalPDVIGIGPVASTATK--PDAPPalgvdGIAEIAA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446206770 152 hIERLADYPTVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATQQLL 203
Cdd:PRK09517 161 -VAQDHGIASVAIGGVGLRNAAELAATGIDGLCVVSAIMAAANPAAAARELR 211
PRK07695 PRK07695
thiazole tautomerase TenI;
19-202 3.36e-15

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 70.82  E-value: 3.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  19 VDSVAWIERLLEAGVRTIQLRIKDKRDEEVeADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLGQEDLettDLEAI 98
Cdd:PRK07695  14 FEELVAVAMQIHSEVDYIHIREREKSAKEL-YEGVESLLKKGVPASKLIINDRVDIALLLNIHRVQLGYRSF---SVRSV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  99 QA--AGLRLGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKQ-MPsaPQGLaQLARHIERLADYPTVAIGGISLERAPAV 175
Cdd:PRK07695  90 REkfPYLHVGYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKKgVP--ARGL-EELSDIARALSIPVIAIGGITPENTRDV 166

                        170       180
                 ....*....|....*....|....*..
gi 446206770 176 LATGVGSIAVVSAITQAADWRAATQQL 202
Cdd:PRK07695 167 LAAGVSGIAVMSGIFSSANPYSKAKRY 193
PRK08999 PRK08999
Nudix family hydrolase;
25-183 9.68e-13

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 65.67  E-value: 9.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770  25 IERLLEAGVRTIQLRIKDKRDEEVEADIIAAIALGRRYDARLFINDYWRLAIKHRAYGVHLGQEDLETTDlEAIQAAGLR 104
Cdd:PRK08999 150 LERALAAGIRLIQLRAPQLPPAAYRALARAALGLCRRAGAQLLLNGDPELAEDLGADGVHLTSAQLAALA-ARPLPAGRW 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206770 105 LGVSTHDDMEIDIALAAKPSYIALGHVFPTQTKqmPSAP----QGLAQLARHIerlaDYPTVAIGGIS---LERAPAVLA 177
Cdd:PRK08999 229 VAASCHDAEELARAQRLGVDFAVLSPVQPTASH--PGAAplgwEGFAALIAGV----PLPVYALGGLGpgdLEEAREHGA 302


                 ....*.
gi 446206770 178 TGVGSI 183
Cdd:PRK08999 303 QGIAGI 308
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 141-202 1.39e-04

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


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 41.03  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446206770 141 SAPQGLAQLARHIERLADYPTVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATQQL 202
Cdd:cd04726  141 AGGWWPEDDLKKVKKLLGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 146-195 4.35e-03

Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.


Pssm-ID: 238802 [Multi-domain]  Cd Length: 269  Bit Score: 37.07  E-value: 4.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446206770 146 LAQLARHIERLADYPTVAI---GGISLERAPAVLATGVGSIaVVSAITQAADW 195
Cdd:cd01568  212 PEELKEAVKLLKGLPRVLLeasGGITLENIRAYAETGVDVI-STGALTHSAPA 263
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
142-205 7.18e-03

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 36.29  E-value: 7.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446206770 142 APQGLAQLARHIERLADYPTVAIGGISLERAPAVLATGVgSIAVV-SAITQAADWRAATQQLLAI 205
Cdd:COG0269  145 AGGSPLDDLKKIKELVGVPVAVAGGINPETLPEFLGAGA-DIVIVgRAITGAKDPAAAAREIREA 208
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH