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Conserved domains on  [gi|2293747833|ref|WP_259003796|]
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thiamine phosphate synthase [Serratia sp. AKBS12]

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;
6-212 3.91e-151

thiamine phosphate synthase;


:

Pssm-ID: 179586  Cd Length: 211  Bit Score: 417.92  E-value: 3.91e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833   6 TPFPATPHRLGLYPVVDSVVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGV 85
Cdd:PRK03512    4 PDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQAYGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  86 HLGQEDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELKRHVAGLADYPTVA 165
Cdd:PRK03512   84 HLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYPTVA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2293747833 166 IGGIGIDRVPAVLACGVGSIAVVSAITQAADWRAATGELLRLIEGKE 212
Cdd:PRK03512  164 IGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGD 210
 
Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
6-212 3.91e-151

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 417.92  E-value: 3.91e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833   6 TPFPATPHRLGLYPVVDSVVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGV 85
Cdd:PRK03512    4 PDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQAYGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  86 HLGQEDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELKRHVAGLADYPTVA 165
Cdd:PRK03512   84 HLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYPTVA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2293747833 166 IGGIGIDRVPAVLACGVGSIAVVSAITQAADWRAATGELLRLIEGKE 212
Cdd:PRK03512  164 IGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGD 210
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 13-210 7.10e-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: 7.10e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  13 HRLGLYPVVDS-------VVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGV 85
Cdd:COG0352     2 TLPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  86 HLGQEDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELkRHVAGLADYPTVA 165
Cdd:COG0352    82 HLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGL-AWWAELVEIPVVA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2293747833 166 IGGIGIDRVPAVLACGVGSIAVVSAITQAADWRAATGELLRLIEG 210
Cdd:COG0352   161 IGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEA 205
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 17-206 7.16e-72

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: 216.62  E-value: 7.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  17 LYPVVDS-------VVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGVHLGQ 89
Cdd:cd00564     1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  90 EDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELKRHVAgLADYPTVAIGGI 169
Cdd:cd00564    81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAE-LVEIPVVAIGGI 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2293747833 170 GIDRVPAVLACGVGSIAVVSAITQAADWRAATGELLR 206
Cdd:cd00564   160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 16-204 7.09e-66

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: 201.32  E-value: 7.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  16 GLYPVVDS-------VVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGVHLG 88
Cdd:TIGR00693   1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  89 QEDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELKRHVAGLADYPTVAIGG 168
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2293747833 169 IGIDRVPAVLACGVGSIAVVSAITQAADWRAATGEL 204
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 17-191 9.00e-59

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: 182.75  E-value: 9.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  17 LYPVVDS-------VVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGVHLGQ 89
Cdd:pfam02581   1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  90 EDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSaPQGLAELKRHVAGLAdYPTVAIGGI 169
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158

                         170       180
                  ....*....|....*....|..
gi 2293747833 170 GIDRVPAVLACGVGSIAVVSAI 191
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
 
Name Accession Description Interval E-value
PRK03512 PRK03512
thiamine phosphate synthase;
6-212 3.91e-151

thiamine phosphate synthase;


Pssm-ID: 179586  Cd Length: 211  Bit Score: 417.92  E-value: 3.91e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833   6 TPFPATPHRLGLYPVVDSVVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGV 85
Cdd:PRK03512    4 PDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQAYGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  86 HLGQEDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELKRHVAGLADYPTVA 165
Cdd:PRK03512   84 HLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYPTVA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2293747833 166 IGGIGIDRVPAVLACGVGSIAVVSAITQAADWRAATGELLRLIEGKE 212
Cdd:PRK03512  164 IGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGD 210
thiE PRK12290
thiamine phosphate synthase;
7-196 2.14e-88

thiamine phosphate synthase;


Pssm-ID: 237041 [Multi-domain]  Cd Length: 437  Bit Score: 267.05  E-value: 2.14e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833   7 PFPAT-PHRLGLYPVVDSVVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGV 85
Cdd:PRK12290  202 AFPTLdKQSLGLYPVVDDVEWIERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAYGV 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  86 HLGQEDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELKRH--------VAG 157
Cdd:PRK12290  282 HLGQEDLEEANLAQLTDAGIRLGLSTHGYYELLRIVQIQPSYIALGHIFPTTTKQMPSKPQGLVRLALYqklidtipYQG 361

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2293747833 158 LADYPTVAIGGIGIDRVPAVLACGVGSIAVVSAITQAAD 196
Cdd:PRK12290  362 QTGFPTVAIGGIDQSNAEQVWQCGVSSLAVVRAITLAED 400
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 13-210 7.10e-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: 7.10e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  13 HRLGLYPVVDS-------VVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGV 85
Cdd:COG0352     2 TLPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  86 HLGQEDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELkRHVAGLADYPTVA 165
Cdd:COG0352    82 HLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGL-AWWAELVEIPVVA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2293747833 166 IGGIGIDRVPAVLACGVGSIAVVSAITQAADWRAATGELLRLIEG 210
Cdd:COG0352   161 IGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEA 205
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 17-206 7.16e-72

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: 216.62  E-value: 7.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  17 LYPVVDS-------VVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGVHLGQ 89
Cdd:cd00564     1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  90 EDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELKRHVAgLADYPTVAIGGI 169
Cdd:cd00564    81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAE-LVEIPVVAIGGI 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2293747833 170 GIDRVPAVLACGVGSIAVVSAITQAADWRAATGELLR 206
Cdd:cd00564   160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
 16-204 7.09e-66

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: 201.32  E-value: 7.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  16 GLYPVVDS-------VVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGVHLG 88
Cdd:TIGR00693   1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  89 QEDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELKRHVAGLADYPTVAIGG 168
Cdd:TIGR00693  81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2293747833 169 IGIDRVPAVLACGVGSIAVVSAITQAADWRAATGEL 204
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
thiE PRK00043
thiamine phosphate synthase;
15-209 2.01e-61

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 190.39  E-value: 2.01e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  15 LGLYPVVDS--------VVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGVH 86
Cdd:PRK00043    7 LRLYLITDSrddsgrdlLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVGADGVH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  87 LGQEDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSAPQGLAELKRHVAGLADYPTVAI 166
Cdd:PRK00043   87 LGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAVGDIPIVAI 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2293747833 167 GGIGIDRVPAVLACGVGSIAVVSAITQAADWRAATGELLRLIE 209
Cdd:PRK00043  167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFR 209
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
 17-191 9.00e-59

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: 182.75  E-value: 9.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  17 LYPVVDS-------VVWIERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGVHLGQ 89
Cdd:pfam02581   1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  90 EDLDDTDLAAIHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDMPSaPQGLAELKRHVAGLAdYPTVAIGGI 169
Cdd:pfam02581  81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158

                         170       180
                  ....*....|....*....|..
gi 2293747833 170 GIDRVPAVLACGVGSIAVVSAI 191
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
PRK02615 PRK02615
thiamine phosphate synthase;
27-209 1.06e-31

thiamine phosphate synthase;


Pssm-ID: 235054 [Multi-domain]  Cd Length: 347  Bit Score: 117.68  E-value: 1.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  27 IERLLAAGVTTIQLRIKNLPeDQVEADIAAAI-DLGKQYQARVFINDYWRLAIKHRAYGVHLGQEDLDdTDLA-AIHQAG 104
Cdd:PRK02615  163 VEAALKGGVTLVQYRDKTAD-DRQRLEEAKKLkELCHRYGALFIVNDRVDIALAVDADGVHLGQEDLP-LAVArQLLGPE 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833 105 LRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKDmPSAPQGLAELKrHVAGLADYPTVAIGGIGIDRVPAVLACGVGS 184
Cdd:PRK02615  241 KIIGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKP-GKAPAGLEYLK-YAAKEAPIPWFAIGGIDKSNIPEVLQAGAKR 318

                         170       180
                  ....*....|....*....|....*
gi 2293747833 185 IAVVSAITQAADWRAATGELLRLIE 209
Cdd:PRK02615  319 VAVVRAIMGAEDPKQATQELLKQLS 343
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 12-208 7.71e-19

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 84.05  E-value: 7.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  12 PHRLGLYPVVDSVV---W-------IERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHR 81
Cdd:PLN02898  288 PRNLFLYAVTDSGMnkkWgrstvdaVRAAIEGGATIVQLREKEAETREFIEEAKACLAICRSYGVPLLINDRVDVALACD 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  82 AYGVHLGQEDLDDTDLAAIHQAGLRLGVSTHdDVELAR-AKAVKPSYIALGHIFPTQTK-DMPSApqGLAELkRHVAGLA 159
Cdd:PLN02898  368 ADGVHLGQSDMPVRLARSLLGPGKIIGVSCK-TPEQAEqAWKDGADYIGCGGVFPTNTKaNNKTI--GLDGL-REVCEAS 443

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2293747833 160 DYPTVAIGGIGIDRVPAVLACGVGS---IAVVSAITQAADWRAATGELLRLI 208
Cdd:PLN02898  444 KLPVVAIGGISASNAASVMESGAPNlkgVAVVSALFDQEDVLKATRKLHAIL 495
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 27-205 1.02e-16

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 78.09  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  27 IERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYgVHLGQEDLDDTDLAAIHQAGLR 106
Cdd:PRK09517   25 VDSAISGGVSVVQLRDKNAGVEDVRAAAKELKELCDARGVALVVNDRLDVAVELGLH-VHIGQGDTPYTQARRLLPAHLE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833 107 LGVS--THDDVEL-----ARAKAVKPSYIALGHIFPTQTKdmPSAPQ-----GLAELKRhVAGLADYPTVAIGGIGIDRV 174
Cdd:PRK09517  104 LGLTieTLDQLEAviaqcAETGVALPDVIGIGPVASTATK--PDAPPalgvdGIAEIAA-VAQDHGIASVAIGGVGLRNA 180

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2293747833 175 PAVLACGVGSIAVVSAITQAADWRAATGELL 205
Cdd:PRK09517  181 AELAATGIDGLCVVSAIMAAANPAAAARELR 211
PRK08999 PRK08999
Nudix family hydrolase;
27-191 2.18e-15

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 72.98  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  27 IERLLAAGVTTIQLRIKNLPEDQVEADIAAAIDLGKQYQARVFINDYWRLAIKHRAYGVHLGQEdlddtDLAAIHQ---- 102
Cdd:PRK08999  150 LERALAAGIRLIQLRAPQLPPAAYRALARAALGLCRRAGAQLLLNGDPELAEDLGADGVHLTSA-----QLAALAArplp 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833 103 AGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKdmPSAP----QGLAELKRHVAgladYPTVAIGGIGIDRVPAVL 178
Cdd:PRK08999  225 AGRWVAASCHDAEELARAQRLGVDFAVLSPVQPTASH--PGAAplgwEGFAALIAGVP----LPVYALGGLGPGDLEEAR 298

                         170
                  ....*....|...
gi 2293747833 179 ACGVGSIAVVSAI 191
Cdd:PRK08999  299 EHGAQGIAGIRGL 311
PRK07695 PRK07695
thiazole tautomerase TenI;
67-210 9.45e-13

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 64.27  E-value: 9.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833  67 RVFINDYWRLAIKHRAYGVHLGQEDLDDTDLAAiHQAGLRLGVSTHDDVELARAKAVKPSYIALGHIFPTQTKD-MPsaP 145
Cdd:PRK07695   59 KLIINDRVDIALLLNIHRVQLGYRSFSVRSVRE-KFPYLHVGYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKKgVP--A 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2293747833 146 QGLAELKRhVAGLADYPTVAIGGIGIDRVPAVLACGVGSIAVVSAITQAADWRAATGELLRLIEG 210
Cdd:PRK07695  136 RGLEELSD-IARALSIPVIAIGGITPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAESIKK 199
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 110-204 4.01e-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: 39.87  E-value: 4.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833 110 STHDDVELARAKAVKPSYIALgHIfptqTKDMPSA-PQGLAELKRHVAGLADYPTVAIGGIGIDRVPAVLACGVGSIAVV 188
Cdd:cd04726   112 GVEDPEKRAKLLKLGVDIVIL-HR----GIDAQAAgGWWPEDDLKKVKKLLGVKVAVAGGITPDTLPEFKKAGADIVIVG 186

                          90
                  ....*....|....*.
gi 2293747833 189 SAITQAADWRAATGEL 204
Cdd:cd04726   187 RAITGAADPAEAAREF 202
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
110-210 2.26e-03

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 37.83  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2293747833 110 STHDDVELARA-KAVKPSYIALgHIfptqTKDMPSAPQGLAELKRHVAGLADYPTVAIGGIGIDRVPAVLACGVgSIAVV 188
Cdd:COG0269   115 GVWDPVERAKElEELGVDIVIL-HR----GIDAQAAGGSPLDDLKKIKELVGVPVAVAGGINPETLPEFLGAGA-DIVIV 188

                          90       100
                  ....*....|....*....|...
gi 2293747833 189 -SAITQAADWRAATGELLRLIEG 210
Cdd:COG0269   189 gRAITGAKDPAAAAREIREAIDK 211
UgpQ COG0584
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];
72-120 6.02e-03

Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism];


Pssm-ID: 440349 [Multi-domain]  Cd Length: 238  Bit Score: 36.77  E-value: 6.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2293747833  72 DYWRLAIKHRAYGVHLGQEDLDDTDLAAIHQAGLRLGVSTHDDVELARA 120
Cdd:COG0584   167 DPLELARALGADGVGPDYDLLTPELVAAAHAAGLKVHVWTVNDPEEMRR 215
 
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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