|
Name |
Accession |
Description |
Interval |
E-value |
| thiE |
PRK00043 |
thiamine phosphate synthase; |
1-209 |
1.00e-94 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 275.14 E-value: 1.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 1 MRAELAVYFIAGTQDIVRGTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALAL 80
Cdd:PRK00043 3 MMKLLRLYLITDSRDDSGRDLLEVVEAALEGGVTLVQLREKGL----DTRERLELARALKELCRRYGVPLIVNDRVDLAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 81 EIGADGIHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVSGTAILEEIRRA 160
Cdd:PRK00043 79 AVGADGVHLGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALAAGA-DYVGVGPIFPTPTKKDAKAPQGLEGLREIRAA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1214221682 161 GITIPIVGIGGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLKN 209
Cdd:PRK00043 158 VGDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLA 206
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
7-208 |
5.64e-78 |
|
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: 232.02 E-value: 5.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 7 VYFIAGTQDIVRgTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGADG 86
Cdd:cd00564 1 LYLITDRRLDGE-DLLEVVEAALKGGVTLVQLREKDL----SARELLELARALRELCRKYGVPLIINDRVDLALAVGADG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 87 IHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVSGTAILEEIRRAgITIPI 166
Cdd:cd00564 76 VHLGQDDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGA-DYVGFGPVFPTPTKPGAGPPLGLELLREIAEL-VEIPV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1214221682 167 VGIGGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLK 208
Cdd:cd00564 154 VAIGGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
7-194 |
1.18e-75 |
|
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: 225.50 E-value: 1.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 7 VYFIAGTQDIVRgTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGADG 86
Cdd:pfam02581 1 LYLVTDPGLDGE-DLLEVVEEALKGGVTIVQLREKEL----DDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 87 IHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVsGTAILEEIRRAgITIPI 166
Cdd:pfam02581 76 VHLGQDDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGA-DYIGFGPIFPTPTKPDAPPL-GLEGLKAIAEA-VEIPV 152
|
170 180
....*....|....*....|....*...
gi 1214221682 167 VGIGGINETNSAEVLAAGADGVSVISAI 194
Cdd:pfam02581 153 VAIGGITPENVPEVIEAGADGVAVVSAI 180
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
5-209 |
1.97e-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: 223.52 E-value: 1.97e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 5 LAVYFIAGTqDIVRGTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGA 84
Cdd:COG0352 4 PRLYLITDP-DLCGRDLLEVLEAALAGGVDLVQLREKDL----DERELLALARALRALCRAYGVPLIINDRVDLALALGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 85 DGIHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVSGTAILEEIRRAgITI 164
Cdd:COG0352 79 DGVHLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGA-DYVGFGPVFPTPTKPGAPPPLGLEGLAWWAEL-VEI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1214221682 165 PIVGIGGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLKN 209
Cdd:COG0352 157 PVVAIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRA 201
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
7-207 |
1.99e-70 |
|
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: 212.88 E-value: 1.99e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 7 VYFIAGTQDiVRGTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGADG 86
Cdd:TIGR00693 2 LYLITDPQD-GPADLLNRVEAALKGGVTLVQLRDKGS----NTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 87 IHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVSGTAILEEIRRAGITIPI 166
Cdd:TIGR00693 77 VHLGQDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGA-DYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1214221682 167 VGIGGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQL 207
Cdd:TIGR00693 156 VAIGGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| thiE |
PRK00043 |
thiamine phosphate synthase; |
1-209 |
1.00e-94 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 275.14 E-value: 1.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 1 MRAELAVYFIAGTQDIVRGTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALAL 80
Cdd:PRK00043 3 MMKLLRLYLITDSRDDSGRDLLEVVEAALEGGVTLVQLREKGL----DTRERLELARALKELCRRYGVPLIVNDRVDLAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 81 EIGADGIHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVSGTAILEEIRRA 160
Cdd:PRK00043 79 AVGADGVHLGQDDLPVADARALLGPDAIIGLSTHTLEEAAAALAAGA-DYVGVGPIFPTPTKKDAKAPQGLEGLREIRAA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1214221682 161 GITIPIVGIGGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLKN 209
Cdd:PRK00043 158 VGDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLA 206
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
7-208 |
5.64e-78 |
|
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: 232.02 E-value: 5.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 7 VYFIAGTQDIVRgTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGADG 86
Cdd:cd00564 1 LYLITDRRLDGE-DLLEVVEAALKGGVTLVQLREKDL----SARELLELARALRELCRKYGVPLIINDRVDLALAVGADG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 87 IHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVSGTAILEEIRRAgITIPI 166
Cdd:cd00564 76 VHLGQDDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGA-DYVGFGPVFPTPTKPGAGPPLGLELLREIAEL-VEIPV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1214221682 167 VGIGGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLK 208
Cdd:cd00564 154 VAIGGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
7-194 |
1.18e-75 |
|
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: 225.50 E-value: 1.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 7 VYFIAGTQDIVRgTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGADG 86
Cdd:pfam02581 1 LYLVTDPGLDGE-DLLEVVEEALKGGVTIVQLREKEL----DDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 87 IHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVsGTAILEEIRRAgITIPI 166
Cdd:pfam02581 76 VHLGQDDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGA-DYIGFGPIFPTPTKPDAPPL-GLEGLKAIAEA-VEIPV 152
|
170 180
....*....|....*....|....*...
gi 1214221682 167 VGIGGINETNSAEVLAAGADGVSVISAI 194
Cdd:pfam02581 153 VAIGGITPENVPEVIEAGADGVAVVSAI 180
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
5-209 |
1.97e-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: 223.52 E-value: 1.97e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 5 LAVYFIAGTqDIVRGTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGA 84
Cdd:COG0352 4 PRLYLITDP-DLCGRDLLEVLEAALAGGVDLVQLREKDL----DERELLALARALRALCRAYGVPLIINDRVDLALALGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 85 DGIHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVSGTAILEEIRRAgITI 164
Cdd:COG0352 79 DGVHLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGA-DYVGFGPVFPTPTKPGAPPPLGLEGLAWWAEL-VEI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1214221682 165 PIVGIGGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLKN 209
Cdd:COG0352 157 PVVAIGGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRA 201
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
7-207 |
1.99e-70 |
|
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: 212.88 E-value: 1.99e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 7 VYFIAGTQDiVRGTLPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGADG 86
Cdd:TIGR00693 2 LYLITDPQD-GPADLLNRVEAALKGGVTLVQLRDKGS----NTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 87 IHVGQTDEAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVSGTAILEEIRRAGITIPI 166
Cdd:TIGR00693 77 VHLGQDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGA-DYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIDIPI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1214221682 167 VGIGGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQL 207
Cdd:TIGR00693 156 VAIGGITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
|
|
| PRK02615 |
PRK02615 |
thiamine phosphate synthase; |
21-207 |
9.55e-53 |
|
thiamine phosphate synthase;
Pssm-ID: 235054 [Multi-domain] Cd Length: 347 Bit Score: 172.76 E-value: 9.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 21 LPSVLEEALKAGITCFQYREKGAgslqTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGADGIHVGQTD---EAIR 97
Cdd:PRK02615 159 LLEVVEAALKGGVTLVQYRDKTA----DDRQRLEEAKKLKELCHRYGALFIVNDRVDIALAVDADGVHLGQEDlplAVAR 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 98 QVIAscSGKMkIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVsGTAILEEIRRAgITIPIVGIGGINETNS 177
Cdd:PRK02615 235 QLLG--PEKI-IGRSTTNPEEMAKAIAEGA-DYIGVGPVFPTPTKPGKAPA-GLEYLKYAAKE-APIPWFAIGGIDKSNI 308
|
170 180 190
....*....|....*....|....*....|
gi 1214221682 178 AEVLAAGADGVSVISAITRSEDCQSVIKQL 207
Cdd:PRK02615 309 PEVLQAGAKRVAVVRAIMGAEDPKQATQEL 338
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
25-208 |
4.85e-33 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 123.73 E-value: 4.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 25 LEEALKAGITCFQYREKGAGSLQTASERKEMalefQKLCAKYQVPFIINDDVALALEIGADGIHVGQTDEAIRQVIASCS 104
Cdd:PLN02898 313 VRAAIEGGATIVQLREKEAETREFIEEAKAC----LAICRSYGVPLLINDRVDVALACDADGVHLGQSDMPVRLARSLLG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 105 GKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAePVSGTAILEEIRRAgITIPIVGIGGINETNSAEVLAAG 184
Cdd:PLN02898 389 PGKIIGVSCKTPEQAEQAWKDGA-DYIGCGGVFPTNTKANN-KTIGLDGLREVCEA-SKLPVVAIGGISASNAASVMESG 465
|
170 180
....*....|....*....|....*..
gi 1214221682 185 A---DGVSVISAITRSEDCQSVIKQLK 208
Cdd:PLN02898 466 ApnlKGVAVVSALFDQEDVLKATRKLH 492
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
39-208 |
7.60e-25 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 96.63 E-value: 7.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 39 REKGagslQTASErkemALEFQKLCAKYQVP---FIINDDVALALEIGADGIHVGQTDEAIRQVIASCSgKMKIGLSVHS 115
Cdd:PRK07695 34 RERE----KSAKE----LYEGVESLLKKGVPaskLIINDRVDIALLLNIHRVQLGYRSFSVRSVREKFP-YLHVGYSVHS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 116 VSEAKEAERLGAvDYIGVGPIFPTISKADAEPvSGTAILEEIRRAgITIPIVGIGGINETNSAEVLAAGADGVSVISAIT 195
Cdd:PRK07695 105 LEEAIQAEKNGA-DYVVYGHVFPTDCKKGVPA-RGLEELSDIARA-LSIPVIAIGGITPENTRDVLAAGVSGIAVMSGIF 181
|
170
....*....|...
gi 1214221682 196 RSEDCQSVIKQLK 208
Cdd:PRK07695 182 SSANPYSKAKRYA 194
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
21-207 |
9.21e-25 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 101.20 E-value: 9.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 21 LPSVLEEALKAGITCFQYREKGAGslqtASERKEMALEFQKLCAKYQVPFIINDDVALALEIGADgIHVGQTDEAIRQVI 100
Cdd:PRK09517 21 VAGIVDSAISGGVSVVQLRDKNAG----VEDVRAAAKELKELCDARGVALVVNDRLDVAVELGLH-VHIGQGDTPYTQAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 101 ASCSGKMKIGLS------VHSVSEAKEAERLGAVDYIGVGPIFPTISKADAEP---VSGTAILEEIRRAGiTIPIVGIGG 171
Cdd:PRK09517 96 RLLPAHLELGLTietldqLEAVIAQCAETGVALPDVIGIGPVASTATKPDAPPalgVDGIAEIAAVAQDH-GIASVAIGG 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 1214221682 172 INETNSAEVLAAGADGVSVISAITRSEDCQSVIKQL 207
Cdd:PRK09517 175 VGLRNAAELAATGIDGLCVVSAIMAAANPAAAAREL 210
|
|
| PRK08999 |
PRK08999 |
Nudix family hydrolase; |
3-194 |
3.26e-22 |
|
Nudix family hydrolase;
Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 91.86 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 3 AELAVY-FIAGTQDIVRG-TLPSV-----------------LEEALKAGITCFQYREKGAGSLQtaseRKEMALEFQKLC 63
Cdd:PRK08999 109 DELAVYpFPPANQPIVRAlRLPDTylitpegedgdaaflarLERALAAGIRLIQLRAPQLPPAA----YRALARAALGLC 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 64 AKYQVPFIINDDVALALEIGADGIHVGQTD---------EAIRQVIASCsgkmkiglsvHSVSEAKEAERLGaVDYIGVG 134
Cdd:PRK08999 185 RRAGAQLLLNGDPELAEDLGADGVHLTSAQlaalaarplPAGRWVAASC----------HDAEELARAQRLG-VDFAVLS 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 135 PIFPTISKADAEPVsGTAILEEIrRAGITIPIVGIGGINETNSAEVLAAGADGVSVISAI 194
Cdd:PRK08999 254 PVQPTASHPGAAPL-GWEGFAAL-IAGVPLPVYALGGLGPGDLEEAREHGAQGIAGIRGL 311
|
|
| PRK03512 |
PRK03512 |
thiamine phosphate synthase; |
25-207 |
8.35e-22 |
|
thiamine phosphate synthase;
Pssm-ID: 179586 Cd Length: 211 Bit Score: 88.57 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 25 LEEALKAGITCFQYREKGagslQTASERKEMALEFQKLCAKYQVPFIINDDVALALEIGADGIHVGQTD------EAIRQ 98
Cdd:PRK03512 25 IERLLDAGVRTLQLRIKD----RRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQAYGVHLGQEDletadlNAIRA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 99 viascSGkMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKA-DAEPVSGTAILEEIRRAGiTIPIVGIGGINETNS 177
Cdd:PRK03512 101 -----AG-LRLGVSTHDDMEIDVALAARP-SYIALGHVFPTQTKQmPSAPQGLAQLARHVERLA-DYPTVAIGGISLERA 172
|
170 180 190
....*....|....*....|....*....|
gi 1214221682 178 AEVLAAGADGVSVISAITRSEDCQSVIKQL 207
Cdd:PRK03512 173 PAVLATGVGSIAVVSAITQAADWRAATAQL 202
|
|
| thiE |
PRK12290 |
thiamine phosphate synthase; |
25-214 |
6.18e-18 |
|
thiamine phosphate synthase;
Pssm-ID: 237041 [Multi-domain] Cd Length: 437 Bit Score: 81.38 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 25 LEEALKAGITCFQYREKGA--GSLQTASERkemALEfqkLCAKYQVPFIINDDVALALEIGADGIHVGQTDEAIRQVIAS 102
Cdd:PRK12290 223 IERLLPLGINTVQLRIKDPqqADLEQQIIR---AIA---LGREYNAQVFINDYWQLAIKHQAYGVHLGQEDLEEANLAQL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 103 CSGKMKIGLSVHSVSEAKEAERLGAvDYIGVGPIFPTISKADAEPVSGTAIL-------EEIRRAGIT-IPIVGIGGINE 174
Cdd:PRK12290 297 TDAGIRLGLSTHGYYELLRIVQIQP-SYIALGHIFPTTTKQMPSKPQGLVRLalyqkliDTIPYQGQTgFPTVAIGGIDQ 375
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1214221682 175 TNSAEVLAAGADGVSVISAITRSEDCQSVI---KQLKNPGSPS 214
Cdd:PRK12290 376 SNAEQVWQCGVSSLAVVRAITLAEDPQLVIeffDQVMAENQLL 418
|
|
| UlaD |
COG0269 |
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism]; |
76-209 |
1.79e-06 |
|
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
Pssm-ID: 440039 Cd Length: 212 Bit Score: 46.69 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 76 VALALEIGADGIHV--GQTDEAIRQVIASCS---GKMKIGLSVHS--VSEAKEAERLGaVDYIGVgpifpTISK-ADAEP 147
Cdd:COG0269 73 AEMAFKAGADIVTVlgAADDATIKGAVKAAKkygKEVQVDLIGVWdpVERAKELEELG-VDIVIL-----HRGIdAQAAG 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1214221682 148 VSGTAILEEIRR-AGITIPIVGigGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLKN 209
Cdd:COG0269 147 GSPLDDLKKIKElVGVPVAVAG--GINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIRE 207
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
116-199 |
6.61e-06 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 45.78 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 116 VSEAKEAERLGaVDYIG--VGPIFPTISKadaEPVSgtaILEEIRRAgITIPIVGIGGINETNSAEVLAAGADGVSVISA 193
Cdd:PRK07028 121 VKRAVELEELG-VDYINvhVGIDQQMLGK---DPLE---LLKEVSEE-VSIPIAVAGGLDAETAAKAVAAGADIVIVGGN 192
|
....*.
gi 1214221682 194 ITRSED 199
Cdd:PRK07028 193 IIKSAD 198
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
71-192 |
2.15e-05 |
|
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: 43.73 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 71 IINDDVALALEIGADGIHVGQTD-----------EAIRQVIASCSGKMKIGLSVHSVSEAKEAERLGAVDYIGVGPIFPT 139
Cdd:cd04722 72 AVDIAAAAARAAGADGVEIHGAVgylaredleliRELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGG 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1214221682 140 IskadaEPVSGTAILEEIRRAGITIPIVGIGGINETNSA-EVLAAGADGVSVIS 192
Cdd:cd04722 152 R-----DAVPIADLLLILAKRGSKVPVIAGGGINDPEDAaEALALGADGVIVGS 200
|
|
| PRK06512 |
PRK06512 |
thiamine phosphate synthase; |
13-206 |
5.47e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 180598 Cd Length: 221 Bit Score: 42.74 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 13 TQDIVRGTLPSVLEEALKAG-ITC---FQYrEKGAGSLQTASERkemaleFQKLCAKYQVPFIINDDVALALEIGADGIH 88
Cdd:PRK06512 20 PPIADGAELAKLLRAALQGGdVASvilPQY-GLDEATFQKQAEK------LVPVIQEAGAAALIAGDSRIAGRVKADGLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 89 VGQTDEAIRQVIASCSGKMKIGL----SVHSVSEAKEAErlgaVDYIGVGPIFPTIsKADAEPVSGTaiLEEIRRAGITI 164
Cdd:PRK06512 93 IEGNLAALAEAIEKHAPKMIVGFgnlrDRHGAMEIGELR----PDYLFFGKLGADN-KPEAHPRNLS--LAEWWAEMIEI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1214221682 165 PIVGIGGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQ 206
Cdd:PRK06512 166 PCIVQAGSDLASAVEVAETGAEFVALERAVFDAHDPPLAVAQ 207
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
115-196 |
1.51e-04 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 41.41 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 115 SVSEAKEAERLGAvDYIG---VGPIFPTISKADAepvsGTAILEEIRRAgITIPIVGIGGINE-TNSAEVLAAGADGVSV 190
Cdd:cd04729 132 TLEEALNAAKLGF-DIIGttlSGYTEETAKTEDP----DFELLKELRKA-LGIPVIAEGRINSpEQAAKALELGADAVVV 205
|
....*.
gi 1214221682 191 ISAITR 196
Cdd:cd04729 206 GSAITR 211
|
|
| PRK01130 |
PRK01130 |
putative N-acetylmannosamine-6-phosphate 2-epimerase; |
85-196 |
1.52e-04 |
|
putative N-acetylmannosamine-6-phosphate 2-epimerase;
Pssm-ID: 234907 Cd Length: 221 Bit Score: 41.29 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 85 DGIHVGQTDEAIRQ-----VIASCSgkmkiglsvhSVSEAKEAERLGAvDYIGVgpifpTIS------KADAEPvsGTAI 153
Cdd:PRK01130 103 DGETLAELVKRIKEypgqlLMADCS----------TLEEGLAAQKLGF-DFIGT-----TLSgyteetKKPEEP--DFAL 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1214221682 154 LEEIRRAgITIPIVGIGGINE-TNSAEVLAAGADGVSVISAITR 196
Cdd:PRK01130 165 LKELLKA-VGCPVIAEGRINTpEQAKKALELGAHAVVVGGAITR 207
|
|
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
170-209 |
8.53e-04 |
|
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: 38.90 E-value: 8.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1214221682 170 GGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLKN 209
Cdd:COG0036 174 GGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALRE 213
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
86-194 |
1.06e-03 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 38.90 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 86 GIHVGQTDEAIRQVIASCSGK------MKIGLSVHSVSE-AKEAERLGAvDyiGVGPIFPTISKA----DAEPV------ 148
Cdd:COG0167 135 GRALGQDPEALAELLAAVKAAtdkpvlVKLAPDLTDIVEiARAAEEAGA-D--GVIAINTTLGRAidleTRRPVlaneag 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1214221682 149 --SGTAILE-------EIRRA-GITIPIVGIGGINETNSA-EVLAAGADGVSVISAI 194
Cdd:COG0167 212 glSGPALKPialrmvrEVAQAvGGDIPIIGVGGISTAEDAlEFILAGASAVQVGTAL 268
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
42-200 |
1.08e-03 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 39.00 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 42 GAGSLQTASERKEMAlEFQKLCAKyqvPFIIN-----------DDVALALEIGADGI--HVGQTDEAIRQVIAScsgKMK 108
Cdd:cd04730 32 GAGYLTPEALRAEIR-KIRALTDK---PFGVNllvpssnpdfeALLEVALEEGVPVVsfSFGPPAEVVERLKAA---GIK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 109 IGLSVHSVSEAKEAERLGaVDYIGV-GPifptiskaDA------EPVSGTAILEEIRRAgITIPIVGIGGINETNS-AEV 180
Cdd:cd04730 105 VIPTVTSVEEARKAEAAG-ADALVAqGA--------EAgghrgtFDIGTFALVPEVRDA-VDIPVIAAGGIADGRGiAAA 174
|
170 180
....*....|....*....|
gi 1214221682 181 LAAGADGVSVISAITRSEDC 200
Cdd:cd04730 175 LALGADGVQMGTRFLATEES 194
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
170-208 |
1.35e-03 |
|
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: 38.23 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1214221682 170 GGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLK 208
Cdd:cd00429 173 GGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
58-207 |
1.77e-03 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 38.30 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 58 EFQKLCAKyqvpfiINDDVALALEI-------GADGIHVGQTDEAIRQVIASCSGK------MKIGLSVHSVSE-AKEAE 123
Cdd:cd04740 103 EFVEVAEK------LADAGADAIELniscpnvKGGGMAFGTDPEAVAEIVKAVKKAtdvpviVKLTPNVTDIVEiARAAE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 124 RLGA-------------VDYIGVGPIFPTISKAdaepVSGTAILE-------EIRRAgITIPIVGIGGI-NETNSAEVLA 182
Cdd:cd04740 177 EAGAdgltlintlkgmaIDIETRKPILGNVTGG----LSGPAIKPialrmvyQVYKA-VEIPIIGVGGIaSGEDALEFLM 251
|
170 180
....*....|....*....|....*.
gi 1214221682 183 AGADGVSVISAI-TRSEDCQSVIKQL 207
Cdd:cd04740 252 AGASAVQVGTANfVDPEAFKEIIEGL 277
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
94-193 |
2.99e-03 |
|
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC operons in bacteria, which are involved in molybdate transport. In general, QPRTases are part of the de novo synthesis pathway of NAD in both prokaryotes and eukaryotes. They catalyse 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.
Pssm-ID: 238807 [Multi-domain] Cd Length: 272 Bit Score: 37.66 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214221682 94 EAIRQVIASCSGKmKIGLSVHSVSEAKEAERLGAvDYIgvgpifpTISKADAEPVsgTAILEEIRRAGITIPIVGIGGIN 173
Cdd:cd01573 172 KALARLRATAPEK-KIVVEVDSLEEALAAAEAGA-DIL-------QLDKFSPEEL--AELVPKLRSLAPPVLLAAAGGIN 240
|
90 100
....*....|....*....|
gi 1214221682 174 ETNSAEVLAAGADGVsVISA 193
Cdd:cd01573 241 IENAAAYAAAGADIL-VTSA 259
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
170-209 |
4.82e-03 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 36.70 E-value: 4.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1214221682 170 GGINETNSAEVLAAGADGVSVISAITRSEDCQSVIKQLKN 209
Cdd:PRK05581 177 GGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
119-190 |
9.36e-03 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 36.40 E-value: 9.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1214221682 119 AKEAERLGaVDYIGV-----GPIFPTISKADAEPVSGTAILEEIRRAgITIPIVGIGGINETNSAE-VLAAG-ADGVSV 190
Cdd:cd02803 234 AKALEEAG-VDALHVsggsyESPPPIIPPPYVPEGYFLELAEKIKKA-VKIPVIAVGGIRDPEVAEeILAEGkADLVAL 310
|
|
| PBP1_ABC_HAAT-like |
cd06348 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
150-193 |
9.95e-03 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380571 [Multi-domain] Cd Length: 342 Bit Score: 36.06 E-value: 9.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1214221682 150 GTAILEEIRRAGITIPIVGIGGINETNSAEVLAAGADGVSVISA 193
Cdd:cd06348 204 GALIVKQARELGLKGPIVGGNGFNSPDLIKLAGKAAEGVIVGSA 247
|
|
| |
