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Conserved domains on  [gi|446206727|ref|WP_000284582|]
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MULTISPECIES: thiamine phosphate synthase [Escherichia]

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

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List of domain hits

 Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
1-211 3.37e-157

thiamine phosphate synthase;


:

Pssm-ID: 179586  Cd Length: 211  Bit Score: 432.94  E-value: 3.37e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   1 MYQPDFPPVPFHLGLYPVVDSAQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQA 80
Cdd:PRK03512   1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  81 YGVHLGQEDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVERLADYP 160
Cdd:PRK03512  81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446206727 161 TVAIGGISLARAPAVMATGVGSIAVVSAITQAADWRLATAQLLEIAGVGDE 211
Cdd:PRK03512 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
 
Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
1-211 3.37e-157

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 432.94  E-value: 3.37e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   1 MYQPDFPPVPFHLGLYPVVDSAQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQA 80
Cdd:PRK03512   1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  81 YGVHLGQEDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVERLADYP 160
Cdd:PRK03512  81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446206727 161 TVAIGGISLARAPAVMATGVGSIAVVSAITQAADWRLATAQLLEIAGVGDE 211
Cdd:PRK03512 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 14-202 2.42e-77

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: 230.60  E-value: 2.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   14 GLYPVVDS-------AQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHLG 86
Cdd:TIGR00693   1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   87 QEDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVERLADYPTVAIGG 166
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446206727  167 ISLARAPAVMATGVGSIAVVSAITQAADWRLATAQL 202
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 15-204 8.20e-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: 218.93  E-value: 8.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  15 LYPVVDS-------AQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHLGQ 87
Cdd:cd00564    1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  88 EDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVErLADYPTVAIGGI 167
Cdd:cd00564   81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAE-LVEIPVVAIGGI 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446206727 168 SLARAPAVMATGVGSIAVVSAITQAADWRLATAQLLE 204
Cdd:cd00564  160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 13-205 4.24e-71

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: 215.05  E-value: 4.24e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  13 LGLYPVVDS-------AQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHL 85
Cdd:COG0352    4 PRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGVHL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  86 GQEDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVErLADYPTVAIG 165
Cdd:COG0352   84 GQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAWWAE-LVEIPVVAIG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446206727 166 GISLARAPAVMATGVGSIAVVSAITQAADWRLATAQLLEI 205
Cdd:COG0352  163 GITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 15-189 3.34e-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: 191.61  E-value: 3.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   15 LYPVVDS-------AQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHLGQ 87
Cdd:pfam02581   1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   88 EDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSaPQGLEQLARHVERLAdYPTVAIGGI 167
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158

                         170       180
                  ....*....|....*....|..
gi 446206727  168 SLARAPAVMATGVGSIAVVSAI 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
 
Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
1-211 3.37e-157

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 432.94  E-value: 3.37e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   1 MYQPDFPPVPFHLGLYPVVDSAQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQA 80
Cdd:PRK03512   1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  81 YGVHLGQEDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVERLADYP 160
Cdd:PRK03512  81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446206727 161 TVAIGGISLARAPAVMATGVGSIAVVSAITQAADWRLATAQLLEIAGVGDE 211
Cdd:PRK03512 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
thiE PRK12290
thiamine phosphate synthase;
13-198 1.37e-85

thiamine phosphate synthase;


Pssm-ID: 237041 [Multi-domain]  Cd Length: 437  Bit Score: 259.73  E-value: 1.37e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  13 LGLYPVVDSAQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHLGQEDLQA 92
Cdd:PRK12290 211 LGLYPVVDDVEWIERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAYGVHLGQEDLEE 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  93 TDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHvERLAD---------YPTVA 163
Cdd:PRK12290 291 ANLAQLTDAGIRLGLSTHGYYELLRIVQIQPSYIALGHIFPTTTKQMPSKPQGLVRLALY-QKLIDtipyqgqtgFPTVA 369

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446206727 164 IGGISLARAPAVMATGVGSIAVVSAITQAADWRLA 198
Cdd:PRK12290 370 IGGIDQSNAEQVWQCGVSSLAVVRAITLAEDPQLV 404
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 14-202 2.42e-77

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: 230.60  E-value: 2.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   14 GLYPVVDS-------AQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHLG 86
Cdd:TIGR00693   1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   87 QEDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVERLADYPTVAIGG 166
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446206727  167 ISLARAPAVMATGVGSIAVVSAITQAADWRLATAQL 202
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 15-204 8.20e-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: 218.93  E-value: 8.20e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  15 LYPVVDS-------AQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHLGQ 87
Cdd:cd00564    1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  88 EDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVErLADYPTVAIGGI 167
Cdd:cd00564   81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAE-LVEIPVVAIGGI 159

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446206727 168 SLARAPAVMATGVGSIAVVSAITQAADWRLATAQLLE 204
Cdd:cd00564  160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 13-205 4.24e-71

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: 215.05  E-value: 4.24e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  13 LGLYPVVDS-------AQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHL 85
Cdd:COG0352    4 PRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGVHL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  86 GQEDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVErLADYPTVAIG 165
Cdd:COG0352   84 GQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAWWAE-LVEIPVVAIG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446206727 166 GISLARAPAVMATGVGSIAVVSAITQAADWRLATAQLLEI 205
Cdd:COG0352  163 GITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
thiE PRK00043
thiamine phosphate synthase;
13-205 1.67e-62

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 193.48  E-value: 1.67e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  13 LGLYPVVDS--------AQWIERLLDAGVRTLQLRIKDR--RDEEVEADVVAAITlgRRYNARLFINDYWRLAIKHQAYG 82
Cdd:PRK00043   7 LRLYLITDSrddsgrdlLEVVEAALEGGVTLVQLREKGLdtRERLELARALKELC--RRYGVPLIVNDRVDLALAVGADG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  83 VHLGQEDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVERLADYPTV 162
Cdd:PRK00043  85 VHLGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAVGDIPIV 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446206727 163 AIGGISLARAPAVMATGVGSIAVVSAITQAADWRLATAQLLEI 205
Cdd:PRK00043 165 AIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAA 207
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 15-189 3.34e-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: 191.61  E-value: 3.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   15 LYPVVDS-------AQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHLGQ 87
Cdd:pfam02581   1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727   88 EDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSaPQGLEQLARHVERLAdYPTVAIGGI 167
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158

                         170       180
                  ....*....|....*....|..
gi 446206727  168 SLARAPAVMATGVGSIAVVSAI 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
PRK02615 PRK02615
thiamine phosphate synthase;
25-205 3.88e-33

thiamine phosphate synthase;


Pssm-ID: 235054 [Multi-domain]  Cd Length: 347  Bit Score: 121.53  E-value: 3.88e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  25 IERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHLGQEDLqatDLSAIRA---A 101
Cdd:PRK02615 163 VEAALKGGVTLVQYRDKTADDRQRLEEAKKLKELCHRYGALFIVNDRVDIALAVDADGVHLGQEDL---PLAVARQllgP 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727 102 GLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQmPSAPQGLEQLaRHVERLADYPTVAIGGISLARAPAVMATGVG 181
Cdd:PRK02615 240 EKIIGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKP-GKAPAGLEYL-KYAAKEAPIPWFAIGGIDKSNIPEVLQAGAK 317

                        170       180
                 ....*....|....*....|....
gi 446206727 182 SIAVVSAITQAADWRLATAQLLEI 205
Cdd:PRK02615 318 RVAVVRAIMGAEDPKQATQELLKQ 341
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 10-205 7.13e-24

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 98.30  E-value: 7.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  10 PFHLGLYPVVDSA---QWIERLLDA-------GVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQ 79
Cdd:PLN02898 288 PRNLFLYAVTDSGmnkKWGRSTVDAvraaiegGATIVQLREKEAETREFIEEAKACLAICRSYGVPLLINDRVDVALACD 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  80 AYGVHLGQEDLQATDLSAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQmpSAPQ-GLEQLaRHVERLAD 158
Cdd:PLN02898 368 ADGVHLGQSDMPVRLARSLLGPGKIIGVSCKTPEQAEQAWKDGADYIGCGGVFPTNTKA--NNKTiGLDGL-REVCEASK 444

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446206727 159 YPTVAIGGISLARAPAVMATGVGS---IAVVSAITQAADWRLATAQLLEI 205
Cdd:PLN02898 445 LPVVAIGGISASNAASVMESGAPNlkgVAVVSALFDQEDVLKATRKLHAI 494
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 25-204 1.89e-18

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 83.10  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  25 IERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYgVHLGQEDLQATDLSAIRAAGLR 104
Cdd:PRK09517  25 VDSAISGGVSVVQLRDKNAGVEDVRAAAKELKELCDARGVALVVNDRLDVAVELGLH-VHIGQGDTPYTQARRLLPAHLE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727 105 LGVS--THDDMEIDVALAAR-----PSYIALGHVFPTQTKQMPSAPQGLEQLA--RHVERLADYPTVAIGGISLARAPAV 175
Cdd:PRK09517 104 LGLTieTLDQLEAVIAQCAEtgvalPDVIGIGPVASTATKPDAPPALGVDGIAeiAAVAQDHGIASVAIGGVGLRNAAEL 183

                        170       180
                 ....*....|....*....|....*....
gi 446206727 176 MATGVGSIAVVSAITQAADWRLATAQLLE 204
Cdd:PRK09517 184 AATGIDGLCVVSAIMAAANPAAAARELRT 212
PRK08999 PRK08999
Nudix family hydrolase;
25-183 5.19e-15

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 71.83  E-value: 5.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  25 IERLLDAGVRTLQLRIKDRRDEEVEADVVAAITLGRRYNARLFINDYWRLAIKHQAYGVHLGQEDLQATDlSAIRAAGLR 104
Cdd:PRK08999 150 LERALAAGIRLIQLRAPQLPPAAYRALARAALGLCRRAGAQLLLNGDPELAEDLGADGVHLTSAQLAALA-ARPLPAGRW 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727 105 LGVSTHDDMEIDVALAARPSYIALGHVFPTQTKqmPSA-PQGLEQLARHVERLAdYPTVAIGGIS---LARAPAVMATGV 180
Cdd:PRK08999 229 VAASCHDAEELARAQRLGVDFAVLSPVQPTASH--PGAaPLGWEGFAALIAGVP-LPVYALGGLGpgdLEEAREHGAQGI 305


                 ...
gi 446206727 181 GSI 183
Cdd:PRK08999 306 AGI 308
PRK07695 PRK07695
thiazole tautomerase TenI;
65-207 9.21e-15

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 69.66  E-value: 9.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206727  65 RLFINDYWRLAIKHQAYGVHLGQEDLqatDLSAIRA--AGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQ-MPs 141
Cdd:PRK07695  59 KLIINDRVDIALLLNIHRVQLGYRSF---SVRSVREkfPYLHVGYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKKgVP- 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446206727 142 aPQGLEQLARHVERLAdYPTVAIGGISLARAPAVMATGVGSIAVVSAITQAADWRLATAQLLEIAG 207
Cdd:PRK07695 135 -ARGLEELSDIARALS-IPVIAIGGITPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAESIK 198
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 146-195 1.92e-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: 1.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446206727 146 LEQLARHVERLADYPTVAI---GGISLARAPAVMATGVGSIaVVSAITQAADW 195
Cdd:cd01568  212 PEELKEAVKLLKGLPRVLLeasGGITLENIRAYAETGVDVI-STGALTHSAPA 263
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 141-194 1.95e-03

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: 37.95  E-value: 1.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446206727 141 SAPQGLEQLARHVERLADYPTVAIGGISLARAPAVMATGVGSIAVVSAITQAAD 194
Cdd:cd04726  141 AGGWWPEDDLKKVKKLLGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAAD 194
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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