|
Name |
Accession |
Description |
Interval |
E-value |
| thiE |
PRK00043 |
thiamine phosphate synthase; |
1-212 |
6.05e-91 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 265.51 E-value: 6.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 1 MFNQSYLNVYFICGTSDVPShRTIHEVLEAALKAGITLFQFREKGesaLKGNDKLVLAKELQHLCHQYDVPFIVNDDVSL 80
Cdd:PRK00043 1 MMMMKLLRLYLITDSRDDSG-RDLLEVVEAALEGGVTLVQLREKG---LDTRERLELARALKELCRRYGVPLIVNDRVDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 81 AKEINADGIHVGQDDAKVKEIAQYFT-DKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKE 159
Cdd:PRK00043 77 ALAVGADGVHLGQDDLPVADARALLGpDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446405306 160 MNPQLPIVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKDFFN 212
Cdd:PRK00043 157 AVGDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFR 209
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
9-209 |
3.97e-77 |
|
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: 230.10 E-value: 3.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 9 VYFIcgTSDVPSHRTIHEVLEAALKAGITLFQFREKGESAlkgNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINADG 88
Cdd:cd00564 1 LYLI--TDRRLDGEDLLEVVEAALKGGVTLVQLREKDLSA---RELLELARALRELCRKYGVPLIINDRVDLALAVGADG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 89 IHVGQDDAKVKEI-AQYFTDKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKEMnPQLPIV 167
Cdd:cd00564 76 VHLGQDDLPVAEArALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAEL-VEIPVV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446405306 168 AIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKD 209
Cdd:cd00564 155 AIGGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
9-194 |
3.08e-74 |
|
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: 222.04 E-value: 3.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 9 VYFICGTSDVPshRTIHEVLEAALKAGITLFQFREKGESAlkgNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINADG 88
Cdd:pfam02581 1 LYLVTDPGLDG--EDLLEVVEEALKGGVTIVQLREKELDD---REFLELAKELRALCRKYGVPLIINDRVDLALAVGADG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 89 IHVGQDDAKVKEIAQYFT-DKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHtPVGPEMIATFKEMNpQLPIV 167
Cdd:pfam02581 76 VHLGQDDLPVAEARELLGpDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAV-EIPVV 153
|
170 180
....*....|....*....|....*..
gi 446405306 168 AIGGINTSNVAPIVEAGANGISVISAI 194
Cdd:pfam02581 154 AIGGITPENVPEVIEAGADGVAVVSAI 180
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
7-212 |
8.58e-74 |
|
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: 221.98 E-value: 8.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 7 LNVYFIcgTSDVPSHRTIHEVLEAALKAGITLFQFREKGESAlkgNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINA 86
Cdd:COG0352 4 PRLYLI--TDPDLCGRDLLEVLEAALAGGVDLVQLREKDLDE---RELLALARALRALCRAYGVPLIINDRVDLALALGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 87 DGIHVGQDDAKVKEIAQYF-TDKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKEMNPqLP 165
Cdd:COG0352 79 DGVHLGQEDLPVAEARALLgPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAWWAELVE-IP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446405306 166 IVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKDFFN 212
Cdd:COG0352 158 VVAIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALE 204
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
9-207 |
8.73e-71 |
|
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: 214.03 E-value: 8.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 9 VYFIcgTSDVPSHRTIHEVLEAALKAGITLFQFREKGESAlkgNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINADG 88
Cdd:TIGR00693 2 LYLI--TDPQDGPADLLNRVEAALKGGVTLVQLRDKGSNT---RERLALAEKLQELCRRYGVPFIVNDRVDLALALGADG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 89 IHVGQDDAKVKEIAQYF-TDKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKEMNPQLPIV 167
Cdd:TIGR00693 77 VHLGQDDLPASEARALLgPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446405306 168 AIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRF 207
Cdd:TIGR00693 157 AIGGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| thiE |
PRK00043 |
thiamine phosphate synthase; |
1-212 |
6.05e-91 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 265.51 E-value: 6.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 1 MFNQSYLNVYFICGTSDVPShRTIHEVLEAALKAGITLFQFREKGesaLKGNDKLVLAKELQHLCHQYDVPFIVNDDVSL 80
Cdd:PRK00043 1 MMMMKLLRLYLITDSRDDSG-RDLLEVVEAALEGGVTLVQLREKG---LDTRERLELARALKELCRRYGVPLIVNDRVDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 81 AKEINADGIHVGQDDAKVKEIAQYFT-DKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKE 159
Cdd:PRK00043 77 ALAVGADGVHLGQDDLPVADARALLGpDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446405306 160 MNPQLPIVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKDFFN 212
Cdd:PRK00043 157 AVGDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFR 209
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
9-209 |
3.97e-77 |
|
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: 230.10 E-value: 3.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 9 VYFIcgTSDVPSHRTIHEVLEAALKAGITLFQFREKGESAlkgNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINADG 88
Cdd:cd00564 1 LYLI--TDRRLDGEDLLEVVEAALKGGVTLVQLREKDLSA---RELLELARALRELCRKYGVPLIINDRVDLALAVGADG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 89 IHVGQDDAKVKEI-AQYFTDKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKEMnPQLPIV 167
Cdd:cd00564 76 VHLGQDDLPVAEArALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAEL-VEIPVV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446405306 168 AIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKD 209
Cdd:cd00564 155 AIGGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
9-194 |
3.08e-74 |
|
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: 222.04 E-value: 3.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 9 VYFICGTSDVPshRTIHEVLEAALKAGITLFQFREKGESAlkgNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINADG 88
Cdd:pfam02581 1 LYLVTDPGLDG--EDLLEVVEEALKGGVTIVQLREKELDD---REFLELAKELRALCRKYGVPLIINDRVDLALAVGADG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 89 IHVGQDDAKVKEIAQYFT-DKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHtPVGPEMIATFKEMNpQLPIV 167
Cdd:pfam02581 76 VHLGQDDLPVAEARELLGpDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAP-PLGLEGLKAIAEAV-EIPVV 153
|
170 180
....*....|....*....|....*..
gi 446405306 168 AIGGINTSNVAPIVEAGANGISVISAI 194
Cdd:pfam02581 154 AIGGITPENVPEVIEAGADGVAVVSAI 180
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
7-212 |
8.58e-74 |
|
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: 221.98 E-value: 8.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 7 LNVYFIcgTSDVPSHRTIHEVLEAALKAGITLFQFREKGESAlkgNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINA 86
Cdd:COG0352 4 PRLYLI--TDPDLCGRDLLEVLEAALAGGVDLVQLREKDLDE---RELLALARALRALCRAYGVPLIINDRVDLALALGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 87 DGIHVGQDDAKVKEIAQYF-TDKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKEMNPqLP 165
Cdd:COG0352 79 DGVHLGQEDLPVAEARALLgPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAWWAELVE-IP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446405306 166 IVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKDFFN 212
Cdd:COG0352 158 VVAIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALE 204
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
9-207 |
8.73e-71 |
|
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: 214.03 E-value: 8.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 9 VYFIcgTSDVPSHRTIHEVLEAALKAGITLFQFREKGESAlkgNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINADG 88
Cdd:TIGR00693 2 LYLI--TDPQDGPADLLNRVEAALKGGVTLVQLRDKGSNT---RERLALAEKLQELCRRYGVPFIVNDRVDLALALGADG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 89 IHVGQDDAKVKEIAQYF-TDKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKEMNPQLPIV 167
Cdd:TIGR00693 77 VHLGQDDLPASEARALLgPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPIV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446405306 168 AIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRF 207
Cdd:TIGR00693 157 AIGGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
|
|
| PRK02615 |
PRK02615 |
thiamine phosphate synthase; |
21-204 |
3.91e-56 |
|
thiamine phosphate synthase;
Pssm-ID: 235054 [Multi-domain] Cd Length: 347 Bit Score: 181.23 E-value: 3.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 21 HRTIHEVLEAALKAGITLFQFREKGesaLKGNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINADGIHVGQDDAKVKE 100
Cdd:PRK02615 156 SENLLEVVEAALKGGVTLVQYRDKT---ADDRQRLEEAKKLKELCHRYGALFIVNDRVDIALAVDADGVHLGQEDLPLAV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 101 IAQYF-TDKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHtPVGPEMIATFKEmNPQLPIVAIGGINTSNVAP 179
Cdd:PRK02615 233 ARQLLgPEKIIGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKPGKA-PAGLEYLKYAAK-EAPIPWFAIGGIDKSNIPE 310
|
170 180
....*....|....*....|....*
gi 446405306 180 IVEAGANGISVISAISKSENIEKTV 204
Cdd:PRK02615 311 VLQAGAKRVAVVRAIMGAEDPKQAT 335
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
2-204 |
4.62e-37 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 134.90 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 2 FNQSYLNVYFI-CGTSDVPSHRTIHEVLEAALKAGITLFQFREKGESALkgnDKLVLAKELQHLCHQYDVPFIVNDDVSL 80
Cdd:PLN02898 286 FNPRNLFLYAVtDSGMNKKWGRSTVDAVRAAIEGGATIVQLREKEAETR---EFIEEAKACLAICRSYGVPLLINDRVDV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 81 AKEINADGIHVGQDDAKVKEIAQYF-TDKIIGLSIS--DLGEYAKSDltHVDYIGVGPIYPTPSKNDAHTpVGPEMIATF 157
Cdd:PLN02898 363 ALACDADGVHLGQSDMPVRLARSLLgPGKIIGVSCKtpEQAEQAWKD--GADYIGCGGVFPTNTKANNKT-IGLDGLREV 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446405306 158 KEMNPqLPIVAIGGINTSNVAPIVEAGA---NGISVISAISKSENIEKTV 204
Cdd:PLN02898 440 CEASK-LPVVAIGGISASNAASVMESGApnlKGVAVVSALFDQEDVLKAT 488
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
7-211 |
3.05e-26 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 105.44 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 7 LNVYFICGTSDVPSHRTIHEVLEAALKAGITLFQFREKGESAlkgNDKLVLAKELQHLCHQYDVPFIVNDDVSLAKEINA 86
Cdd:PRK09517 4 FSLYLVTDPVLGGGPEKVAGIVDSAISGGVSVVQLRDKNAGV---EDVRAAAKELKELCDARGVALVVNDRLDVAVELGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 87 DgIHVGQDDAKVKEIAQYFTDKI-IGLSISDLGEY-------AKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFK 158
Cdd:PRK09517 81 H-VHIGQGDTPYTQARRLLPAHLeLGLTIETLDQLeaviaqcAETGVALPDVIGIGPVASTATKPDAPPALGVDGIAEIA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446405306 159 EMNPQ--LPIVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKDFF 211
Cdd:PRK09517 160 AVAQDhgIASVAIGGVGLRNAAELAATGIDGLCVVSAIMAAANPAAAARELRTAF 214
|
|
| PRK08999 |
PRK08999 |
Nudix family hydrolase; |
28-194 |
3.37e-19 |
|
Nudix family hydrolase;
Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 83.77 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 28 LEAALKAGITLFQFREKGESALKGNDklvLAKELQHLCHQYDVPFIVNDDVSLAKEINADGIHVGQDDAKVKEIAQYFTD 107
Cdd:PRK08999 150 LERALAAGIRLIQLRAPQLPPAAYRA---LARAALGLCRRAGAQLLLNGDPELAEDLGADGVHLTSAQLAALAARPLPAG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 108 KIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAhTPVGPEMIATFKEMNPqLPIVAIGGINTSNVAPIVEAGANG 187
Cdd:PRK08999 227 RWVAASCHDAEELARAQRLGVDFAVLSPVQPTASHPGA-APLGWEGFAALIAGVP-LPVYALGGLGPGDLEEAREHGAQG 304
|
....*..
gi 446405306 188 ISVISAI 194
Cdd:PRK08999 305 IAGIRGL 311
|
|
| PRK03512 |
PRK03512 |
thiamine phosphate synthase; |
28-199 |
8.74e-18 |
|
thiamine phosphate synthase;
Pssm-ID: 179586 Cd Length: 211 Bit Score: 78.17 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 28 LEAALKAGITLFQFREKGESALKGNDKLVLAKELQHlchQYDVPFIVNDDVSLAKEINADGIHVGQDDAKVKEIAQYFTD 107
Cdd:PRK03512 25 IERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGR---RYQARLFINDYWRLAIKHQAYGVHLGQEDLETADLNAIRAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 108 KI-IGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKEMNPQLPIVAIGGINTSNVAPIVEAGAN 186
Cdd:PRK03512 102 GLrLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLADYPTVAIGGISLERAPAVLATGVG 181
|
170
....*....|...
gi 446405306 187 GISVISAISKSEN 199
Cdd:PRK03512 182 SIAVVSAITQAAD 194
|
|
| thiE |
PRK12290 |
thiamine phosphate synthase; |
28-208 |
1.41e-15 |
|
thiamine phosphate synthase;
Pssm-ID: 237041 [Multi-domain] Cd Length: 437 Bit Score: 74.45 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 28 LEAALKAGITLFQFREKGESALKGNDKLVLAKELQHlchQYDVPFIVNDDVSLAKEINADGIHVGQDDAKVKEIAQYFTD 107
Cdd:PRK12290 223 IERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGR---EYNAQVFINDYWQLAIKHQAYGVHLGQEDLEEANLAQLTDA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 108 KI-IGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDAHTPVGPEMIATFKEMNPQL--------PIVAIGGINTSNVA 178
Cdd:PRK12290 300 GIrLGLSTHGYYELLRIVQIQPSYIALGHIFPTTTKQMPSKPQGLVRLALYQKLIDTIpyqgqtgfPTVAIGGIDQSNAE 379
|
170 180 190
....*....|....*....|....*....|
gi 446405306 179 PIVEAGANGISVISAISKSENIEKTVNRFK 208
Cdd:PRK12290 380 QVWQCGVSSLAVVRAITLAEDPQLVIEFFD 409
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
73-209 |
2.85e-15 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 71.20 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 73 IVNDDVSLAKEINADGIHVGQDDAKVKEIAQYFTDKIIGLSISDLGEYAKSDLTHVDYIGVGPIYPTPSKNDahtpVGPE 152
Cdd:PRK07695 61 IINDRVDIALLLNIHRVQLGYRSFSVRSVREKFPYLHVGYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKKG----VPAR 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446405306 153 MIATFKEMNPQL--PIVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKD 209
Cdd:PRK07695 137 GLEELSDIARALsiPVIAIGGITPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAE 195
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
12-192 |
2.82e-10 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 57.60 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 12 ICGTSDVPSHRTiHEVLEAALKAGITLFQFREKGESALK-GNDKLVLAKELqhlCHQYDVPFIVND-----------DVS 79
Cdd:cd04722 3 LALLAGGPSGDP-VELAKAAAEAGADAIIVGTRSSDPEEaETDDKEVLKEV---AAETDLPLGVQLaindaaaavdiAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446405306 80 LAKEINADGIHVGQ--------DDAKVKEIAQYFTDKIIGLSISDLGEYAKSDLT--HVDYIGVGPIYPTPSKNDAHTPV 149
Cdd:cd04722 79 AARAAGADGVEIHGavgylareDLELIRELREAVPDVKVVVKLSPTGELAAAAAEeaGVDEVGLGNGGGGGGGRDAVPIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446405306 150 GPEMIATFKEMNpqLPIVAIGGINT-SNVAPIVEAGANGISVIS 192
Cdd:cd04722 159 DLLLILAKRGSK--VPVIAGGGINDpEDAAEALALGADGVIVGS 200
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
157-208 |
6.78e-06 |
|
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.
Pssm-ID: 238244 Cd Length: 211 Bit Score: 45.16 E-value: 6.78e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446405306 157 FKEMNPQLPIVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFK 208
Cdd:cd00429 160 IPENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
152-209 |
2.50e-05 |
|
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439806 Cd Length: 218 Bit Score: 43.53 E-value: 2.50e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446405306 152 EMIatfKEMNPQLPIVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKD 209
Cdd:COG0036 159 ELI---DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALRE 213
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
151-208 |
1.25e-03 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 38.44 E-value: 1.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446405306 151 PEM---IATFKEMNPQLPIVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFK 208
Cdd:PLN02334 159 PSMmdkVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLR 219
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
149-201 |
1.48e-03 |
|
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; 2-keto-3-deoxy-6-phosphogluconate aldolase is part of the Pathway/BioSystem: Entner-Doudoroff pathway
Pssm-ID: 440563 Cd Length: 213 Bit Score: 38.14 E-value: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446405306 149 VGPEMIATFKEMNPQLPIVAIGGINTSNVAPIVEAGANGISVISAISKSENIE 201
Cdd:COG0800 138 LGPAYLKALKGPLPDVPFMPTGGVSPDNAADYLAAGAVAVGGGSWLVPKGAIA 190
|
|
| PRK04169 |
PRK04169 |
heptaprenylglyceryl phosphate synthase; |
148-209 |
2.70e-03 |
|
heptaprenylglyceryl phosphate synthase;
Pssm-ID: 235237 Cd Length: 232 Bit Score: 37.48 E-value: 2.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446405306 148 PVGPEMIATFKEMNPQLPIVAIGGINTSNVA-PIVEAGANGISVISAIskSENIEKTVNRFKD 209
Cdd:PRK04169 169 PVPPEMVKAVKKALDITPLIYGGGIRSPEQArELMAAGADTIVVGNII--EEDPKKTVKAIKK 229
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
164-209 |
7.49e-03 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 36.54 E-value: 7.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446405306 164 LPIVAIGGINTSNVAPIVEAGANGISVISAISKSENIEKTVNRFKD 209
Cdd:PRK07028 163 IPIAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIRE 208
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
149-190 |
8.57e-03 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 35.96 E-value: 8.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446405306 149 VGPEMIATFKEMNPQLPIVAIGGINTSNVAPIVEAGANGISV 190
Cdd:cd00452 129 VGPAYIKALKGPFPQVRFMPTGGVSLDNAAEWLAAGVVAVGG 170
|
|
| |
