NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2058562109|gb|QXB33672|]
View 

thiamine phosphate synthase [Enterobacter hormaechei]

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 1.15e-161

thiamine phosphate synthase;


:

Pssm-ID: 179586  Cd Length: 211  Bit Score: 444.50  E-value: 1.15e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109   1 MYQPDFPPVPFRLGLYPVVDSVEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQA 80
Cdd:PRK03512    1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  81 YGVHLGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLASHVKRLADYP 160
Cdd:PRK03512   81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2058562109 161 TVAIGGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQLAGAGDE 211
Cdd:PRK03512  161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
 
Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
1-211 1.15e-161

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 444.50  E-value: 1.15e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109   1 MYQPDFPPVPFRLGLYPVVDSVEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQA 80
Cdd:PRK03512    1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  81 YGVHLGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLASHVKRLADYP 160
Cdd:PRK03512   81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2058562109 161 TVAIGGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQLAGAGDE 211
Cdd:PRK03512  161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
14-202 2.76e-74

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: 222.89  E-value: 2.76e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  14 GLYPVVDS-------VEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLG 86
Cdd:TIGR00693   1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  87 QEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLASHVKRLADYPTVAIGG 166
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2058562109 167 ISLERAPAVLETGVGSIAVVSAITQAADWQAATAQL 202
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
15-204 2.63e-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: 220.08  E-value: 2.63e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  15 LYPVVDS-------VEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLGQ 87
Cdd:cd00564     1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  88 EDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAsHVKRLADYPTVAIGGI 167
Cdd:cd00564    81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLR-EIAELVEIPVVAIGGI 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2058562109 168 SLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQ 204
Cdd:cd00564   160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
12-205 7.96e-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: 219.29  E-value: 7.96e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  12 RLGLYPVVDS-------VEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVH 84
Cdd:COG0352     3 LPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGVH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  85 LGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAsHVKRLADYPTVAI 164
Cdd:COG0352    83 LGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLA-WWAELVEIPVVAI 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2058562109 165 GGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQL 205
Cdd:COG0352   162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
15-189 1.47e-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: 192.38  E-value: 1.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  15 LYPVVDS-------VEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLGQ 87
Cdd:pfam02581   1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  88 EDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSaPQGLTQLASHVKRLAdYPTVAIGGI 167
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158
                         170       180
                  ....*....|....*....|..
gi 2058562109 168 SLERAPAVLETGVGSIAVVSAI 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
 
Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
1-211 1.15e-161

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 444.50  E-value: 1.15e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109   1 MYQPDFPPVPFRLGLYPVVDSVEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQA 80
Cdd:PRK03512    1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  81 YGVHLGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLASHVKRLADYP 160
Cdd:PRK03512   81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2058562109 161 TVAIGGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQLAGAGDE 211
Cdd:PRK03512  161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
thiE PRK12290
thiamine phosphate synthase;
13-205 3.13e-89

thiamine phosphate synthase;


Pssm-ID: 237041 [Multi-domain]  Cd Length: 437  Bit Score: 268.97  E-value: 3.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  13 LGLYPVVDSVEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLGQEDLET 92
Cdd:PRK12290  211 LGLYPVVDDVEWIERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAYGVHLGQEDLEE 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  93 TDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLASHvKRLAD---------YPTVA 163
Cdd:PRK12290  291 ANLAQLTDAGIRLGLSTHGYYELLRIVQIQPSYIALGHIFPTTTKQMPSKPQGLVRLALY-QKLIDtipyqgqtgFPTVA 369
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2058562109 164 IGGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQL 205
Cdd:PRK12290  370 IGGIDQSNAEQVWQCGVSSLAVVRAITLAEDPQLVIEFFDQV 411
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
14-202 2.76e-74

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: 222.89  E-value: 2.76e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  14 GLYPVVDS-------VEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLG 86
Cdd:TIGR00693   1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  87 QEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLASHVKRLADYPTVAIGG 166
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2058562109 167 ISLERAPAVLETGVGSIAVVSAITQAADWQAATAQL 202
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
15-204 2.63e-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: 220.08  E-value: 2.63e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  15 LYPVVDS-------VEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLGQ 87
Cdd:cd00564     1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  88 EDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAsHVKRLADYPTVAIGGI 167
Cdd:cd00564    81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLR-EIAELVEIPVVAIGGI 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2058562109 168 SLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQ 204
Cdd:cd00564   160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
12-205 7.96e-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: 219.29  E-value: 7.96e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  12 RLGLYPVVDS-------VEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVH 84
Cdd:COG0352     3 LPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGVH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  85 LGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAsHVKRLADYPTVAI 164
Cdd:COG0352    83 LGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLA-WWAELVEIPVVAI 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2058562109 165 GGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQL 205
Cdd:COG0352   162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
thiE PRK00043
thiamine phosphate synthase;
13-208 6.39e-63

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 194.25  E-value: 6.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  13 LGLYPVVDS--------VEWIARLLEAGVRTLQLRIKDK--RDEEVEADVVAAIAlgRRYDARLFINDYWRLAVKHQAYG 82
Cdd:PRK00043    7 LRLYLITDSrddsgrdlLEVVEAALEGGVTLVQLREKGLdtRERLELARALKELC--RRYGVPLIVNDRVDLALAVGADG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  83 VHLGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLASHVKRLADYPTV 162
Cdd:PRK00043   85 VHLGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAVGDIPIV 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2058562109 163 AIGGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQLAGA 208
Cdd:PRK00043  165 AIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRA 210
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
15-189 1.47e-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: 192.38  E-value: 1.47e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  15 LYPVVDS-------VEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLGQ 87
Cdd:pfam02581   1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  88 EDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSaPQGLTQLASHVKRLAdYPTVAIGGI 167
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158
                         170       180
                  ....*....|....*....|..
gi 2058562109 168 SLERAPAVLETGVGSIAVVSAI 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
PRK02615 PRK02615
thiamine phosphate synthase;
15-205 4.73e-33

thiamine phosphate synthase;


Pssm-ID: 235054 [Multi-domain]  Cd Length: 347  Bit Score: 121.53  E-value: 4.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  15 LYPVVDSVEWIAR----LLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLGQEDL 90
Cdd:PRK02615  149 LYLITSPSENLLEvveaALKGGVTLVQYRDKTADDRQRLEEAKKLKELCHRYGALFIVNDRVDIALAVDADGVHLGQEDL 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  91 ettDLNAIRD---AGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQ--MPSAPQGLTQLASHVKRladyPTVAIG 165
Cdd:PRK02615  229 ---PLAVARQllgPEKIIGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKPgkAPAGLEYLKYAAKEAPI----PWFAIG 301
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2058562109 166 GISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLQL 205
Cdd:PRK02615  302 GIDKSNIPEVLQAGAKRVAVVRAIMGAEDPKQATQELLKQ 341
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
10-213 3.11e-22

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 93.68  E-value: 3.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  10 PFRLGLYPVVDS----------VEWIARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQ 79
Cdd:PLN02898  288 PRNLFLYAVTDSgmnkkwgrstVDAVRAAIEGGATIVQLREKEAETREFIEEAKACLAICRSYGVPLLINDRVDVALACD 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  80 AYGVHLGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQmpSAPQ-GLTQLAShVKRLAD 158
Cdd:PLN02898  368 ADGVHLGQSDMPVRLARSLLGPGKIIGVSCKTPEQAEQAWKDGADYIGCGGVFPTNTKA--NNKTiGLDGLRE-VCEASK 444
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2058562109 159 YPTVAIGGISLERAPAVLETGVGS---IAVVSAITQAADWQAATAQLLQLAGAGDERS 213
Cdd:PLN02898  445 LPVVAIGGISASNAASVMESGAPNlkgVAVVSALFDQEDVLKATRKLHAILTEALSES 502
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
25-204 3.01e-18

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 82.33  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  25 IARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYgVHLGQEDLETTDLNAIRDAGLR 104
Cdd:PRK09517   25 VDSAISGGVSVVQLRDKNAGVEDVRAAAKELKELCDARGVALVVNDRLDVAVELGLH-VHIGQGDTPYTQARRLLPAHLE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109 105 LGVS--THDDMEIDVALAAR-----PSYIALGHVFPTQTKQMPSAPQGLTQLA--SHVKRLADYPTVAIGGISLERAPAV 175
Cdd:PRK09517  104 LGLTieTLDQLEAVIAQCAEtgvalPDVIGIGPVASTATKPDAPPALGVDGIAeiAAVAQDHGIASVAIGGVGLRNAAEL 183
                         170       180
                  ....*....|....*....|....*....
gi 2058562109 176 LETGVGSIAVVSAITQAADWQAATAQLLQ 204
Cdd:PRK09517  184 AATGIDGLCVVSAIMAAANPAAAARELRT 212
PRK07695 PRK07695
thiazole tautomerase TenI;
19-194 1.46e-16

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 74.67  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  19 VDSVEWIARLLEAGVRTLQLRIKDKRDEEVeADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLGQEDLettDLNAI 98
Cdd:PRK07695   14 FEELVAVAMQIHSEVDYIHIREREKSAKEL-YEGVESLLKKGVPASKLIINDRVDIALLLNIHRVQLGYRSF---SVRSV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  99 RD--AGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQ-MPsaPQGLTQLaSHVKRLADYPTVAIGGISLERAPAV 175
Cdd:PRK07695   90 REkfPYLHVGYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKKgVP--ARGLEEL-SDIARALSIPVIAIGGITPENTRDV 166
                         170
                  ....*....|....*....
gi 2058562109 176 LETGVGSIAVVSAITQAAD 194
Cdd:PRK07695  167 LAAGVSGIAVMSGIFSSAN 185
PRK08999 PRK08999
Nudix family hydrolase;
25-170 5.11e-12

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 63.74  E-value: 5.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109  25 IARLLEAGVRTLQLRIKDKRDEEVEADVVAAIALGRRYDARLFINDYWRLAVKHQAYGVHLGQEDLETTDLNAIRDAGLr 104
Cdd:PRK08999  150 LERALAAGIRLIQLRAPQLPPAAYRALARAALGLCRRAGAQLLLNGDPELAEDLGADGVHLTSAQLAALAARPLPAGRW- 228
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2058562109 105 LGVSTHDDMEIDVALAARPSYIALGHVFPTQTKqmPSAP----QGLTQLASHVkrlaDYPTVAIGGISLE 170
Cdd:PRK08999  229 VAASCHDAEELARAQRLGVDFAVLSPVQPTASH--PGAAplgwEGFAALIAGV----PLPVYALGGLGPG 292
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
141-202 8.06e-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: 39.10  E-value: 8.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2058562109 141 SAPQGLTQLASHVKRLADYPTVAIGGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQL 202
Cdd:cd04726   141 AGGWWPEDDLKKVKKLLGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
148-195 2.13e-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: 38.22  E-value: 2.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2058562109 148 QLASHVKRLADYPTVAI---GGISLERAPAVLETGVGSIaVVSAITQAADW 195
Cdd:cd01568   214 ELKEAVKLLKGLPRVLLeasGGITLENIRAYAETGVDVI-STGALTHSAPA 263
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
153-204 2.62e-03

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 37.45  E-value: 2.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2058562109 153 VKRLADYPTVAIGGISLERAPAVLETGVgSIAVV-SAITQAADWQAATAQLLQ 204
Cdd:COG0269   156 IKELVGVPVAVAGGINPETLPEFLGAGA-DIVIVgRAITGAKDPAAAAREIRE 207
 
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