|
Name |
Accession |
Description |
Interval |
E-value |
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
11-353 |
0e+00 |
|
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 213783 [Multi-domain] Cd Length: 341 Bit Score: 547.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 11 YTRYLDPPGATPvssSPLPPFANDPDALLPLYRAMVLTRQFDLKAIAMQRTGKIGTFASALGQEAVGVGVASAMRPEDIL 90
Cdd:TIGR03181 2 LVQVLDEDGNVV---DPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 91 VPSYRDHAAQFVRGVTMTESLLYWGGDERGSGFAAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSK 170
Cdd:TIGR03181 79 FPSYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 171 GDFYEGMNMAGAWHAPLVIVVNNNQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERARAGEGP 250
Cdd:TIGR03181 159 GDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 251 SLIEAITYRLGDHTTADDASRYRDESTVKAHWQAEPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAYLALPPPD 330
Cdd:TIGR03181 239 TLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPP 318
|
330 340
....*....|....*....|...
gi 499620356 331 PAAMFDCLYATMPAALQEQLATA 353
Cdd:TIGR03181 319 VDDIFDHVYAELPPELEEQRAEL 341
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
11-355 |
1.94e-155 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 440.73 E-value: 1.94e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 11 YTRYLDPPGATPVsssplpPFANDPDALLPLYRAMVLTRQFDLKAIAMQRTGKIGTFASALGQEAVGVGVASAMRPEDIL 90
Cdd:COG1071 1 LVQVLDPDGTEAA------LPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 91 VPSYRDHAAQFVRGVTMTESLLYWGGDERGSG---------FAAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVC 161
Cdd:COG1071 75 FPTYRDHGHALARGVDPKELMAELFGKATGPSkgrggsmhfFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 162 MLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAI 241
Cdd:COG1071 155 FFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 242 ERARAGEGPSLIEAITYRLGDHTTADDASRYRDESTVKAHWQAEPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVE 321
Cdd:COG1071 235 ERARAGEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVE 314
|
330 340 350
....*....|....*....|....*....|....
gi 499620356 322 AYLALPPPDPAAMFDCLYATMPAALQEQLATARR 355
Cdd:COG1071 315 FAEASPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
41-323 |
8.22e-126 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 363.35 E-value: 8.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 41 LYRAMVLTRQFDLKAIAMQRTGKIGTF-ASALGQEAVGVGVASAMRPEDILVPSYRDHAAQFVRGVTMTESLLYWGGDER 119
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFyHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 120 GSG---------FAAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIV 190
Cdd:cd02000 81 GPCkgrggsmhiGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 191 VNNNQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERARAGEGPSLIEAITYRLGDHTTADDAS 270
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499620356 271 RYRDESTVKAHWQAEPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAY 323
Cdd:cd02000 241 RYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
42-331 |
3.71e-87 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 265.34 E-value: 3.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 42 YRAMVLTRQFDLKAIAMQRTGKIGTFASALGQEAVGVGVASAMRPEDILVPSYRDHAAQFVRGVTMTESLLYWGGDE-RG 120
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVaKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 121 SGFAAAPHD-------FGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNN 193
Cdd:pfam00676 81 KGGSMHGYYgakgnrfYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 194 NQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERARAGEGPSLIEAITYRLGDHTTADDASRYR 273
Cdd:pfam00676 161 NQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTYR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 499620356 274 DESTVKAHW-QAEPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAYLALPPPDP 331
Cdd:pfam00676 241 TRDEYEEVRkKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHP 299
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
38-340 |
9.33e-61 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 198.94 E-value: 9.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 38 LLPLYRAMVLTRQFDLKAIAMQRTGKIGTFASAL-GQEAVGVGVASAMRPEDILVPSYRDHAAQFVRGV----TMTESLL 112
Cdd:CHL00149 22 LLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVppknVMAELFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 113 YWGGDERGSGFA----AAPHDF-GNNVPIGTQVCHAAGVA----YAVQLRGEP---RVAVCMLGDGGTSKGDFYEGMNMA 180
Cdd:CHL00149 102 KETGCSRGRGGSmhifSAPHNFlGGFAFIGEGIPIALGAAfqsiYRQQVLKEVqplRVTACFFGDGTTNNGQFFECLNMA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 181 GAWHAPLVIVVNNNQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERARAGEGPSLIEAITYRL 260
Cdd:CHL00149 182 VLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEALTYRF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 261 GDHTTAD-DASRYRDEstvKAHWQA-EPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAYLALPPPDPAAMFDCL 338
Cdd:CHL00149 262 RGHSLADpDELRSKQE---KEAWVArDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDLKKYL 338
|
..
gi 499620356 339 YA 340
Cdd:CHL00149 339 FA 340
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDH_E1_alph_x |
TIGR03181 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
11-353 |
0e+00 |
|
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the alpha subunit of the E1 component of pyruvate dehydrogenase (PDH). This model represents one branch of a larger family that E1-alpha proteins from 2-oxoisovalerate dehydrogenase, acetoin dehydrogenase, another PDH clade, etc. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 213783 [Multi-domain] Cd Length: 341 Bit Score: 547.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 11 YTRYLDPPGATPvssSPLPPFANDPDALLPLYRAMVLTRQFDLKAIAMQRTGKIGTFASALGQEAVGVGVASAMRPEDIL 90
Cdd:TIGR03181 2 LVQVLDEDGNVV---DPEPAPDLSDEELVELYRDMVLTRRFDTKALALQRQGRLGTYAPNLGQEAAQVGSALALRKDDWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 91 VPSYRDHAAQFVRGVTMTESLLYWGGDERGSGFAAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSK 170
Cdd:TIGR03181 79 FPSYRDHAAMLARGVPLVEILLYWRGDERGSWDPEGVNILPPNIPIGTQYLHAAGVAYALKLRGEDNVAVTYFGDGGTSE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 171 GDFYEGMNMAGAWHAPLVIVVNNNQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERARAGEGP 250
Cdd:TIGR03181 159 GDFYEALNFAGVFKAPVVFFVQNNQWAISVPRSKQTAAPTLAQKAIAYGIPGVQVDGNDVLAVYAVTKEAVERARSGGGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 251 SLIEAITYRLGDHTTADDASRYRDESTVKAHWQAEPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAYLALPPPD 330
Cdd:TIGR03181 239 TLIEAVTYRLGPHTTADDPTRYRTKEEEEEWRKKDPILRLRKYLERKGLWDEEQEEALEEEAEAEVAEAVAEALALPPPP 318
|
330 340
....*....|....*....|...
gi 499620356 331 PAAMFDCLYATMPAALQEQLATA 353
Cdd:TIGR03181 319 VDDIFDHVYAELPPELEEQRAEL 341
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
11-355 |
1.94e-155 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 440.73 E-value: 1.94e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 11 YTRYLDPPGATPVsssplpPFANDPDALLPLYRAMVLTRQFDLKAIAMQRTGKIGTFASALGQEAVGVGVASAMRPEDIL 90
Cdd:COG1071 1 LVQVLDPDGTEAA------LPDLSKEELLELYRDMLLIRRFEERALALQRQGKIGFYHLSIGQEAAQVGAAAALRPGDWI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 91 VPSYRDHAAQFVRGVTMTESLLYWGGDERGSG---------FAAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVC 161
Cdd:COG1071 75 FPTYRDHGHALARGVDPKELMAELFGKATGPSkgrggsmhfFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 162 MLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAI 241
Cdd:COG1071 155 FFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 242 ERARAGEGPSLIEAITYRLGDHTTADDASRYRDESTVKAHWQAEPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVE 321
Cdd:COG1071 235 ERARAGEGPTLIEAKTYRLGGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVE 314
|
330 340 350
....*....|....*....|....*....|....
gi 499620356 322 AYLALPPPDPAAMFDCLYATMPAALQEQLATARR 355
Cdd:COG1071 315 FAEASPEPDPEELFDDVYAEPPPHLAEQRAELAA 348
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
41-323 |
8.22e-126 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 363.35 E-value: 8.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 41 LYRAMVLTRQFDLKAIAMQRTGKIGTF-ASALGQEAVGVGVASAMRPEDILVPSYRDHAAQFVRGVTMTESLLYWGGDER 119
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFyHLSIGQEAVAVGVAAALRPGDWVFPTYRDHGHALARGVDLKEMLAELFGKET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 120 GSG---------FAAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIV 190
Cdd:cd02000 81 GPCkgrggsmhiGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 191 VNNNQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERARAGEGPSLIEAITYRLGDHTTADDAS 270
Cdd:cd02000 161 CENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSDDPS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 499620356 271 RYRDESTVKAHWQAEPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAY 323
Cdd:cd02000 241 RYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
42-331 |
3.71e-87 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 265.34 E-value: 3.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 42 YRAMVLTRQFDLKAIAMQRTGKIGTFASALGQEAVGVGVASAMRPEDILVPSYRDHAAQFVRGVTMTESLLYWGGDE-RG 120
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALEPGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVaKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 121 SGFAAAPHD-------FGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNN 193
Cdd:pfam00676 81 KGGSMHGYYgakgnrfYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCEN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 194 NQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERARAGEGPSLIEAITYRLGDHTTADDASRYR 273
Cdd:pfam00676 161 NQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDPSTYR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 499620356 274 DESTVKAHW-QAEPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAYLALPPPDP 331
Cdd:pfam00676 241 TRDEYEEVRkKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHP 299
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
38-340 |
9.33e-61 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 198.94 E-value: 9.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 38 LLPLYRAMVLTRQFDLKAIAMQRTGKIGTFASAL-GQEAVGVGVASAMRPEDILVPSYRDHAAQFVRGV----TMTESLL 112
Cdd:CHL00149 22 LLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGVIKLLAETDYVCSTYRDHVHALSKGVppknVMAELFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 113 YWGGDERGSGFA----AAPHDF-GNNVPIGTQVCHAAGVA----YAVQLRGEP---RVAVCMLGDGGTSKGDFYEGMNMA 180
Cdd:CHL00149 102 KETGCSRGRGGSmhifSAPHNFlGGFAFIGEGIPIALGAAfqsiYRQQVLKEVqplRVTACFFGDGTTNNGQFFECLNMA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 181 GAWHAPLVIVVNNNQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERARAGEGPSLIEAITYRL 260
Cdd:CHL00149 182 VLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTLIEALTYRF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 261 GDHTTAD-DASRYRDEstvKAHWQA-EPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAYLALPPPDPAAMFDCL 338
Cdd:CHL00149 262 RGHSLADpDELRSKQE---KEAWVArDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAISSPEPNISDLKKYL 338
|
..
gi 499620356 339 YA 340
Cdd:CHL00149 339 FA 340
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
35-340 |
2.32e-48 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 168.97 E-value: 2.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 35 PDALLPLYRAMVLTRQFDLKAIAMQRTGKIGTFASAL-GQEAVGVGVASAMRPEDILVPSYRDHAAQFVRGV----TMTE 109
Cdd:PLN02374 85 REEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYnGQEAVSTGFIKLLKKDDSVVSTYRDHVHALSKGVparaVMSE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 110 SLLYWGGDERGSG-----FAAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGE-------PRVAVCMLGDGGTSKGDFYEGM 177
Cdd:PLN02374 165 LFGKATGCCRGQGgsmhmFSKEHNLLGGFAFIGEGIPVATGAAFSSKYRREvlkeescDDVTLAFFGDGTCNNGQFFECL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 178 NMAGAWHAPLVIVVNNNQWAISMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERARAGEGPSLIEAIT 257
Cdd:PLN02374 245 NMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECET 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 258 YRLGDHTTAD-DASRYRDEstvKAHWQA-EPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAYLALPPPDPAAMF 335
Cdd:PLN02374 325 YRFRGHSLADpDELRDPAE---KAHYAArDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFADASPLPPRSQLL 401
|
....*
gi 499620356 336 DCLYA 340
Cdd:PLN02374 402 ENVFA 406
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
15-342 |
9.93e-42 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 149.48 E-value: 9.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 15 LDPPGATPVSSsplppfandPDALLPLYRAMVLTRQFDLKAIAMQRTGKIGTFASAL-GQEAVGVGVASAMRPEDILVPS 93
Cdd:PLN02269 18 CDPPSRTVETS---------KQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYdGQEAVAVGMEAAITKEDAIITA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 94 YRDHAAQFVRGVT----MTESLLYWGGDERGSG-----FAAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVCMLG 164
Cdd:PLN02269 89 YRDHCTHLGRGGTvlevFAELMGRKDGCSRGKGgsmhfYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 165 DGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQWAisMPRSRQTAAHTLAQKAIAAGIPGEQIDGNDVVAVRHRVGEAIERA 244
Cdd:PLN02269 169 DGAANQGQLFEALNIAALWDLPVIFVCENNHYG--MGTAEWRAAKSPAYYKRGDYVPGLKVDGMDVLAVKQACKFAKEHA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 245 RAgEGPSLIEAITYRLGDHTTADDASRYRDESTVKAHWQA-EPLLRLREHLVKLGAWDAGREEALVRECSQQVAQAVEAY 323
Cdd:PLN02269 247 LS-NGPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQErDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKA 325
|
330
....*....|....*....
gi 499620356 324 LALPPPDPAAMFDCLYATM 342
Cdd:PLN02269 326 KESPMPDPSELFTNVYVKG 344
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
121-257 |
8.17e-12 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 63.72 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 121 SGF---AAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQWA 197
Cdd:cd02007 59 SGFtkrSESEYDAFGTGHSSTSISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMS 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499620356 198 ISMPrsrqtaahtlaqkaiaAGIPG---EQ--------IDGNDVvavrHRVGEAIERARAGEGPSLIEAIT 257
Cdd:cd02007 139 ISPN----------------VGTPGnlfEElgfryigpVDGHNI----EALIKVLKEVKDLKGPVLLHVVT 189
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
121-257 |
2.66e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).
Pssm-ID: 463832 [Multi-domain] Cd Length: 274 Bit Score: 60.50 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 121 SGF---AAAPHD-FGnnvpigtqVCH-------AAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVI 189
Cdd:pfam13292 95 SGFpkrSESEYDaFG--------TGHsstsisaALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHLKKDLIV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 190 VVNNNQWAISMP-----------RSRQT--AAHTLAQKAIAAGI--------------------PG---EQ--------I 225
Cdd:pfam13292 167 ILNDNEMSISPNvgalsnylsrlRTSPTynRLKEEVKKLLKPKIgpplyelarrakeslkglvvPGtlfEElgfkyigpI 246
|
170 180 190
....*....|....*....|....*....|..
gi 499620356 226 DGNDVVAVRhrvgEAIERARAGEGPSLIEAIT 257
Cdd:pfam13292 247 DGHDLDALV----KVLENAKDLKGPVLLHVVT 274
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
143-257 |
4.45e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 60.87 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 143 AAGVAYAVQLRG-EPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQWAIS-----MprsrqtaAHTLAQkaI 216
Cdd:PRK05444 126 ALGMAKARDLKGgEDRKVVAVIGDGALTGGMAFEALNNAGDLKSDLIVILNDNEMSISpnvgaL-------SNYLAR--L 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 499620356 217 AAGIPGEQ--------IDGNDVVAVRhrvgEAIERARAGEGPSLIEAIT 257
Cdd:PRK05444 197 RSSTLFEElgfnyigpIDGHDLDALI----ETLKNAKDLKGPVLLHVVT 241
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
143-257 |
4.82e-09 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 56.36 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 143 AAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWH-APLVIVVNNNQWAISMPRSRQTAAHTLAQKAIAAGIP 221
Cdd:cd02012 114 AVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKlDNLIAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWN 193
|
90 100 110
....*....|....*....|....*....|....*..
gi 499620356 222 GEQIDGNDVVAVRhrvgEAIERARAGEG-PSLIEAIT 257
Cdd:cd02012 194 VIEVDGHDVEEIL----AALEEAKKSKGkPTLIIAKT 226
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
143-257 |
3.38e-08 |
|
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440768 [Multi-domain] Cd Length: 623 Bit Score: 55.02 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 143 AAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQWAISMP-----------RSRQT----- 206
Cdd:COG1154 124 ALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHLKKDLIVILNDNEMSISPNvgalsnylarlRTSPTynklr 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 207 ---------------AAHTLAQKA-------IAAGIPGEQ--------IDGNDVVAVRhrvgEAIERARAGEGPSLIEAI 256
Cdd:COG1154 204 eevkkllkklpgigpPLYELARRAkeglkglVVPGTLFEElgfkyigpIDGHDLDALV----ETLRNAKDLKGPVLLHVV 279
|
.
gi 499620356 257 T 257
Cdd:COG1154 280 T 280
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
137-255 |
4.64e-08 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 51.82 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 137 GTQVCHAAGVAYA--VQLRGEPRVAVCMLGDGGTskgdfyeGMNMAGAWHA------PLVIVVNNNQWAI----SMPRSR 204
Cdd:pfam02775 25 GGLGTMGYGLPAAigAKLARPDRPVVAIAGDGGF-------QMNLQELATAvrynlpITVVVLNNGGYGMtrgqQTPFGG 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 205 QTAAHT---------LAQKAIAAGIPGEqidgndVVAVRHRVGEAIERARAGEGPSLIEA 255
Cdd:pfam02775 98 GRYSGPsgkilppvdFAKLAEAYGAKGA------RVESPEELEEALKEALEHDGPALIDV 151
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
127-198 |
2.06e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 52.70 E-value: 2.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499620356 127 PHDFGNnvpIG---TQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQWAI 198
Cdd:PRK12315 106 EHDFFT---VGhtsTSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELKSNLIIIVNDNQMSI 177
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
121-201 |
7.32e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 50.88 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 121 SGF---AAAPHDFGNNVPIGTQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQWA 197
Cdd:PRK12571 103 SGFtkrSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYEALNNAGAADRRLIVILNDNEMS 182
|
....
gi 499620356 198 ISMP 201
Cdd:PRK12571 183 IAPP 186
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
138-201 |
1.29e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 43.93 E-value: 1.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499620356 138 TQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQwAISMP 201
Cdd:PLN02234 181 TTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNK-QVSLP 243
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
142-257 |
1.40e-04 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 41.86 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 142 HAAGVAYAVQLRGEPRVAVCMLGDGGTskgdfyeGMNMAGAWHA-----PLVIVVNNNQwAISMPRSRQTAAHT------ 210
Cdd:cd00568 50 YGLPAAIGAALAAPDRPVVCIAGDGGF-------MMTGQELATAvryglPVIVVVFNNG-GYGTIRMHQEAFYGgrvsgt 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 499620356 211 ------LAQKAIAAGIPGEQIDGNDVVAvrhrvgEAIERARAGEGPSLIEAIT 257
Cdd:cd00568 122 dlsnpdFAALAEAYGAKGVRVEDPEDLE------AALAEALAAGGPALIEVKT 168
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
157-257 |
4.58e-04 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 42.07 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 157 RVAVCMLGDGGtskgdFyeGMNM-----AGAWHAPLVIVVNNNQwAISMPRSRQTAAH---------------TLAQkai 216
Cdd:COG0028 431 RPVVAITGDGG-----F--QMNLqelatAVRYGLPVKVVVLNNG-GLGMVRQWQELFYggrysgtdlpnpdfaKLAE--- 499
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 499620356 217 AAGIPGEQIDGNDvvavrhRVGEAIERARAGEGPSLIEAIT 257
Cdd:COG0028 500 AFGAKGERVETPE------ELEAALEEALASDGPALIDVRV 534
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
138-201 |
8.51e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 41.42 E-value: 8.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499620356 138 TQVCHAAGVAYAVQLRGEPRVAVCMLGDGGTSKGDFYEGMNMAGAWHAPLVIVVNNNQwAISMP 201
Cdd:PLN02582 148 TTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNK-QVSLP 210
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
161-257 |
8.66e-03 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 38.19 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499620356 161 CMLGDGGTSKGDFYEGMNMAGAWH-APLVIVVNNNQwaISMpRSRQTAAHTLAQKA--IAAG---IPgeqIDGNDVVAVR 234
Cdd:PRK05899 155 VLCGDGDLMEGISHEACSLAGHLKlGNLIVIYDDNR--ISI-DGPTEGWFTEDVKKrfEAYGwhvIE---VDGHDVEAID 228
|
90 100
....*....|....*....|...
gi 499620356 235 hrvgEAIERARAGEGPSLIEAIT 257
Cdd:PRK05899 229 ----AAIEEAKASTKPTLIIAKT 247
|
|
| |
