|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03512 |
PRK03512 |
thiamine phosphate synthase; |
1-211 |
2.89e-160 |
|
thiamine phosphate synthase;
Pssm-ID: 179586 Cd Length: 211 Bit Score: 441.03 E-value: 2.89e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 1 MYQPDFPSVPFRLGLYPVVDSVEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQA 80
Cdd:PRK03512 1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 81 YGVHLGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAHVKRLADYP 160
Cdd:PRK03512 81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737326176 161 TVAIGGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLKLAGAGDE 211
Cdd:PRK03512 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
14-202 |
5.08e-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: 222.12 E-value: 5.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 14 GLYPVVDS-------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVHLG 86
Cdd:TIGR00693 1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 87 QEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAHVKRLADYPTVAIGG 166
Cdd:TIGR00693 81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1737326176 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 |
1.15e-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: 218.54 E-value: 1.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 15 LYPVVDS-------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVHLGQ 87
Cdd:cd00564 1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 88 EDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAhVKRLADYPTVAIGGI 167
Cdd:cd00564 81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLRE-IAELVEIPVVAIGGI 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1737326176 168 SLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLK 204
Cdd:cd00564 160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
12-205 |
3.12e-72 |
|
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: 217.75 E-value: 3.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 12 RLGLYPVVDS-------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVH 84
Cdd:COG0352 3 LPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGVH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 85 LGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAhVKRLADYPTVAI 164
Cdd:COG0352 83 LGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAW-WAELVEIPVVAI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737326176 165 GGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLKL 205
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
15-189 |
1.06e-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: 192.76 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 15 LYPVVDS-------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVHLGQ 87
Cdd:pfam02581 1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 88 EDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSaPQGLTQLAAHVKRLAdYPTVAIGGI 167
Cdd:pfam02581 81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158
|
170 180
....*....|....*....|..
gi 1737326176 168 SLERAPAVLETGVGSIAVVSAI 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03512 |
PRK03512 |
thiamine phosphate synthase; |
1-211 |
2.89e-160 |
|
thiamine phosphate synthase;
Pssm-ID: 179586 Cd Length: 211 Bit Score: 441.03 E-value: 2.89e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 1 MYQPDFPSVPFRLGLYPVVDSVEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQA 80
Cdd:PRK03512 1 MYQPDFPPVPFRLGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 81 YGVHLGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAHVKRLADYP 160
Cdd:PRK03512 81 YGVHLGQEDLETADLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737326176 161 TVAIGGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLKLAGAGDE 211
Cdd:PRK03512 161 TVAIGGISLERAPAVLATGVGSIAVVSAITQAADWRAATAQLLELAEVGDE 211
|
|
| thiE |
PRK12290 |
thiamine phosphate synthase; |
8-198 |
5.21e-89 |
|
thiamine phosphate synthase;
Pssm-ID: 237041 [Multi-domain] Cd Length: 437 Bit Score: 268.59 E-value: 5.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 8 SVPF------RLGLYPVVDSVEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAY 81
Cdd:PRK12290 200 TRAFptldkqSLGLYPVVDDVEWIERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAY 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 82 GVHLGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAHvKRLAD--- 158
Cdd:PRK12290 280 GVHLGQEDLEEANLAQLTDAGIRLGLSTHGYYELLRIVQIQPSYIALGHIFPTTTKQMPSKPQGLVRLALY-QKLIDtip 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1737326176 159 ------YPTVAIGGISLERAPAVLETGVGSIAVVSAITQAADWQAA 198
Cdd:PRK12290 359 yqgqtgFPTVAIGGIDQSNAEQVWQCGVSSLAVVRAITLAEDPQLV 404
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
14-202 |
5.08e-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: 222.12 E-value: 5.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 14 GLYPVVDS-------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVHLG 86
Cdd:TIGR00693 1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 87 QEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAHVKRLADYPTVAIGG 166
Cdd:TIGR00693 81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIVAIGG 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1737326176 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 |
1.15e-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: 218.54 E-value: 1.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 15 LYPVVDS-------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVHLGQ 87
Cdd:cd00564 1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 88 EDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAhVKRLADYPTVAIGGI 167
Cdd:cd00564 81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLRE-IAELVEIPVVAIGGI 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1737326176 168 SLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLK 204
Cdd:cd00564 160 TPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
12-205 |
3.12e-72 |
|
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: 217.75 E-value: 3.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 12 RLGLYPVVDS-------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVH 84
Cdd:COG0352 3 LPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGVH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 85 LGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAhVKRLADYPTVAI 164
Cdd:COG0352 83 LGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAW-WAELVEIPVVAI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737326176 165 GGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLKL 205
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
13-208 |
1.02e-62 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 193.86 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 13 LGLYPVVDS--------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVH 84
Cdd:PRK00043 7 LRLYLITDSrddsgrdlLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVGADGVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 85 LGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLTQLAAHVKRLADYPTVAI 164
Cdd:PRK00043 87 LGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAVGDIPIVAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737326176 165 GGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLKLAGA 208
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRA 210
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
15-189 |
1.06e-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: 192.76 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 15 LYPVVDS-------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVHLGQ 87
Cdd:pfam02581 1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 88 EDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSaPQGLTQLAAHVKRLAdYPTVAIGGI 167
Cdd:pfam02581 81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAVE-IPVVAIGGI 158
|
170 180
....*....|....*....|..
gi 1737326176 168 SLERAPAVLETGVGSIAVVSAI 189
Cdd:pfam02581 159 TPENVPEVIEAGADGVAVVSAI 180
|
|
| PRK02615 |
PRK02615 |
thiamine phosphate synthase; |
15-205 |
4.12e-33 |
|
thiamine phosphate synthase;
Pssm-ID: 235054 [Multi-domain] Cd Length: 347 Bit Score: 121.53 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 15 LYPVVDSVEWIAR----LLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVHLGQEDL 90
Cdd:PRK02615 149 LYLITSPSENLLEvveaALKGGVTLVQYRDKTADDRQRLEEAKKLKELCHRYGALFIVNDRVDIALAVDADGVHLGQEDL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 91 ettDLNAIRD---AGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQ--MPSAPQGLTQLAAHVKRladyPTVAIG 165
Cdd:PRK02615 229 ---PLAVARQllgPEKIIGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKPgkAPAGLEYLKYAAKEAPI----PWFAIG 301
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1737326176 166 GISLERAPAVLETGVGSIAVVSAITQAADWQAATAQLLKL 205
Cdd:PRK02615 302 GIDKSNIPEVLQAGAKRVAVVRAIMGAEDPKQATQELLKQ 341
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
10-213 |
1.18e-22 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 94.84 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 10 PFRLGLYPVVDS----------VEWIARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQ 79
Cdd:PLN02898 288 PRNLFLYAVTDSgmnkkwgrstVDAVRAAIEGGATIVQLREKEAETREFIEEAKACLAICRSYGVPLLINDRVDVALACD 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 80 AYGVHLGQEDLETTDLNAIRDAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQmpSAPQ-GLTQLAAhVKRLAD 158
Cdd:PLN02898 368 ADGVHLGQSDMPVRLARSLLGPGKIIGVSCKTPEQAEQAWKDGADYIGCGGVFPTNTKA--NNKTiGLDGLRE-VCEASK 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737326176 159 YPTVAIGGISLERAPAVLETGVGS---IAVVSAITQAADWQAATAQLLKLAGAGDERS 213
Cdd:PLN02898 445 LPVVAIGGISASNAASVMESGAPNlkgVAVVSALFDQEDVLKATRKLHAILTEALSES 502
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
25-203 |
1.17e-18 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 83.48 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 25 IARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYgVHLGQEDLETTDLNAIRDAGLR 104
Cdd:PRK09517 25 VDSAISGGVSVVQLRDKNAGVEDVRAAAKELKELCDARGVALVVNDRLDVAVELGLH-VHIGQGDTPYTQARRLLPAHLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 105 LGVS--THDDMEIDVALAAR-----PSYIALGHVFPTQTKQMPSAPQGLTQLA--AHVKRLADYPTVAIGGISLERAPAV 175
Cdd:PRK09517 104 LGLTieTLDQLEAVIAQCAEtgvalPDVIGIGPVASTATKPDAPPALGVDGIAeiAAVAQDHGIASVAIGGVGLRNAAEL 183
|
170 180
....*....|....*....|....*...
gi 1737326176 176 LETGVGSIAVVSAITQAADWQAATAQLL 203
Cdd:PRK09517 184 AATGIDGLCVVSAIMAAANPAAAARELR 211
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
19-194 |
8.37e-16 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 72.36 E-value: 8.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 19 VDSVEWIARLLEAGVRTLQLRIKDKHDEEVeADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVHLGQEDLettDLNAI 98
Cdd:PRK07695 14 FEELVAVAMQIHSEVDYIHIREREKSAKEL-YEGVESLLKKGVPASKLIINDRVDIALLLNIHRVQLGYRSF---SVRSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 99 RD--AGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQ-MPsaPQGLTQLAaHVKRLADYPTVAIGGISLERAPAV 175
Cdd:PRK07695 90 REkfPYLHVGYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKKgVP--ARGLEELS-DIARALSIPVIAIGGITPENTRDV 166
|
170
....*....|....*....
gi 1737326176 176 LETGVGSIAVVSAITQAAD 194
Cdd:PRK07695 167 LAAGVSGIAVMSGIFSSAN 185
|
|
| PRK08999 |
PRK08999 |
Nudix family hydrolase; |
25-170 |
1.33e-13 |
|
Nudix family hydrolase;
Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 67.98 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 25 IARLLEAGVRTLQLRIKDKHDEEVEADVVAAIALGRRYHARLFINDYWRLAVKHQAYGVHLGQEDLETTDLNAIRDAGLr 104
Cdd:PRK08999 150 LERALAAGIRLIQLRAPQLPPAAYRALARAALGLCRRAGAQLLLNGDPELAEDLGADGVHLTSAQLAALAARPLPAGRW- 228
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737326176 105 LGVSTHDDMEIDVALAARPSYIALGHVFPTQTKqmPSAP----QGLTQLAAHVkrlaDYPTVAIGGISLE 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 |
4.63e-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: 4.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737326176 141 SAPQGLTQLAAHVKRLADYPTVAIGGISLERAPAVLETGVGSIAVVSAITQAADWQAATAQL 202
Cdd:cd04726 141 AGGWWPEDDLKKVKKLLGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
148-195 |
8.76e-04 |
|
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: 39.38 E-value: 8.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1737326176 148 QLAAHVKRLADYPTVAI---GGISLERAPAVLETGVGSIaVVSAITQAADW 195
Cdd:cd01568 214 ELKEAVKLLKGLPRVLLeasGGITLENIRAYAETGVDVI-STGALTHSAPA 263
|
|
| UlaD |
COG0269 |
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism]; |
153-204 |
3.02e-03 |
|
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
Pssm-ID: 440039 Cd Length: 212 Bit Score: 37.45 E-value: 3.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1737326176 153 VKRLADYPTVAIGGISLERAPAVLETGVgSIAVV-SAITQAADWQAATAQLLK 204
Cdd:COG0269 156 IKELVGVPVAVAGGINPETLPEFLGAGA-DIVIVgRAITGAKDPAAAAREIRE 207
|
|
| |
