|
Name |
Accession |
Description |
Interval |
E-value |
| PDH_E1_alph_y |
TIGR03182 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
19-333 |
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: 274473 [Multi-domain] Cd Length: 315 Bit Score: 553.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 19 DELLKFYEQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDGDkDSVITGYRDHGHMLAYGIDPKVIMAE 98
Cdd:TIGR03182 2 EELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPD-DYVITSYRDHGHALARGVPPKEVMAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 99 LTGRQAGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWN 178
Cdd:TIGR03182 81 LTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 179 LPIVFVVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRKGGGPVLMELNTYRYRGHS 258
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2176097075 259 MSDPAKYRSREEVQDVREKsDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFAENSPEPEMAELYTDVLV 333
Cdd:TIGR03182 241 MSDPAKYRSKEEVEEWRKR-DPIEKLKARLIEQGIaSEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
1-333 |
1.56e-160 |
|
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: 452.29 E-value: 1.56e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 1 MRNLQQALEANRHYKANDDELLKFYEQMLLIRRFEERAGQLYGLGLIGgFCHLYIGQEAVAVGLQSALDGDkDSVITGYR 80
Cdd:COG1071 2 VQVLDPDGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIG-FYHLSIGQEAAQVGAAAALRPG-DWIFPTYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 81 DHGHMLAYGIDPKVIMAELTGRQAGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDG 160
Cdd:COG1071 80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 161 AANQGQVYETFNMAALWNLPIVFVVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRK 240
Cdd:COG1071 160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 241 GGGPVLMELNTYRYRGHSMSD-PAKYRSREEVQDVREKsDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFAEN 318
Cdd:COG1071 240 GEGPTLIEAKTYRLGGHSTSDdPTRYRTKEEVEEWRER-DPIERLRAYLLEEGLlTEEELEAIEAEAKAEVEEAVEFAEA 318
|
330
....*....|....*
gi 2176097075 319 SPEPEMAELYTDVLV 333
Cdd:COG1071 319 SPEPDPEELFDDVYA 333
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
24-316 |
3.47e-143 |
|
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: 406.11 E-value: 3.47e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 24 FYEQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDgDKDSVITGYRDHGHMLAYGIDPKVIMAELTGRQ 103
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALR-PGDWVFPTYRDHGHALARGVDLKEMLAELFGKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 104 AGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWNLPIVF 183
Cdd:cd02000 80 TGPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 184 VVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRKGGGPVLMELNTYRYRGHSMS-DP 262
Cdd:cd02000 160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2176097075 263 AKYRSREEVQDvREKSDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFA 316
Cdd:cd02000 240 SRYRTKEEVEE-WKKRDPILRLRKYLIEAGIlTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
11-333 |
1.18e-137 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 394.85 E-value: 1.18e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 11 NRHYKANDDELLKFYEQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDgDKDSVITGYRDHGHMLAYGI 90
Cdd:PLN02269 22 SRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAIT-KEDAIITAYRDHCTHLGRGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 91 DPKVIMAELTGRQAGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYET 170
Cdd:PLN02269 101 TVLEVFAELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 171 FNMAALWNLPIVFVVENNGYAMGTAVKRSSAETEFYRRGTAfrIPGMDVNGMDVLEVRAAAEIAMDYVRKgGGPVLMELN 250
Cdd:PLN02269 181 LNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDY--VPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 251 TYRYRGHSMSDP-AKYRSREEVQDVREKSDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFAENSPEPEMAELY 328
Cdd:PLN02269 258 TYRYHGHSMSDPgSTYRTRDEISGVRQERDPIERVRKLLLAHELaTEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELF 337
|
....*
gi 2176097075 329 TDVLV 333
Cdd:PLN02269 338 TNVYV 342
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
26-323 |
9.74e-122 |
|
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: 352.01 E-value: 9.74e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 26 EQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDgDKDSVITGYRDHGHMLAYGIDPKVIMAELTGRQAg 105
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALE-PGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 106 isKGKGGSMHMF--STEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWNLPIVF 183
Cdd:pfam00676 79 --KGKGGSMHGYygAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 184 VVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRKGGGPVLMELNTYRYRGHSMSDPA 263
Cdd:pfam00676 157 VCENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2176097075 264 -KYRSREEVQDVREKSDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFAENSPEPE 323
Cdd:pfam00676 237 sTYRTRDEYEEVRKKKDPIQRFKEHLVSKGVwSEEELKAIEKEVRKEVEEAFKKAESAPEPH 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PDH_E1_alph_y |
TIGR03182 |
pyruvate dehydrogenase E1 component, alpha subunit; Members of this protein family are the ... |
19-333 |
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: 274473 [Multi-domain] Cd Length: 315 Bit Score: 553.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 19 DELLKFYEQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDGDkDSVITGYRDHGHMLAYGIDPKVIMAE 98
Cdd:TIGR03182 2 EELLELYRDMLLIRRFEEKAGQLYGMGKIGGFCHLYIGQEAVAVGLIAALKPD-DYVITSYRDHGHALARGVPPKEVMAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 99 LTGRQAGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWN 178
Cdd:TIGR03182 81 LTGRETGCSKGKGGSMHMFDREKNFYGGHGIVGAQVPLATGLAFANKYRGNDNVTACFFGDGAANQGQFYESFNMAALWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 179 LPIVFVVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRKGGGPVLMELNTYRYRGHS 258
Cdd:TIGR03182 161 LPVIFVIENNLYAMGTAVERSSSVTDLYKRGESFGIPGERVDGMDVLAVREAAKEAVERARSGKGPILLEMKTYRFRGHS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2176097075 259 MSDPAKYRSREEVQDVREKsDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFAENSPEPEMAELYTDVLV 333
Cdd:TIGR03182 241 MSDPAKYRSKEEVEEWRKR-DPIEKLKARLIEQGIaSEEELKEIDKEVRAEVEEAVEFAENSPEPPVEELYTDVYA 315
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
1-333 |
1.56e-160 |
|
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: 452.29 E-value: 1.56e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 1 MRNLQQALEANRHYKANDDELLKFYEQMLLIRRFEERAGQLYGLGLIGgFCHLYIGQEAVAVGLQSALDGDkDSVITGYR 80
Cdd:COG1071 2 VQVLDPDGTEAALPDLSKEELLELYRDMLLIRRFEERALALQRQGKIG-FYHLSIGQEAAQVGAAAALRPG-DWIFPTYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 81 DHGHMLAYGIDPKVIMAELTGRQAGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDG 160
Cdd:COG1071 80 DHGHALARGVDPKELMAELFGKATGPSKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 161 AANQGQVYETFNMAALWNLPIVFVVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRK 240
Cdd:COG1071 160 ATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVRVDGNDVLAVYAAVKEAVERARA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 241 GGGPVLMELNTYRYRGHSMSD-PAKYRSREEVQDVREKsDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFAEN 318
Cdd:COG1071 240 GEGPTLIEAKTYRLGGHSTSDdPTRYRTKEEVEEWRER-DPIERLRAYLLEEGLlTEEELEAIEAEAKAEVEEAVEFAEA 318
|
330
....*....|....*
gi 2176097075 319 SPEPEMAELYTDVLV 333
Cdd:COG1071 319 SPEPDPEELFDDVYA 333
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
24-316 |
3.47e-143 |
|
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: 406.11 E-value: 3.47e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 24 FYEQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDgDKDSVITGYRDHGHMLAYGIDPKVIMAELTGRQ 103
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALR-PGDWVFPTYRDHGHALARGVDLKEMLAELFGKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 104 AGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWNLPIVF 183
Cdd:cd02000 80 TGPCKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 184 VVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRKGGGPVLMELNTYRYRGHSMS-DP 262
Cdd:cd02000 160 VCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSdDP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2176097075 263 AKYRSREEVQDvREKSDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFA 316
Cdd:cd02000 240 SRYRTKEEVEE-WKKRDPILRLRKYLIEAGIlTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
11-333 |
1.18e-137 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 394.85 E-value: 1.18e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 11 NRHYKANDDELLKFYEQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDgDKDSVITGYRDHGHMLAYGI 90
Cdd:PLN02269 22 SRTVETSKQELVDFFRDMYLMRRMEIAADSLYKAKLIRGFCHLYDGQEAVAVGMEAAIT-KEDAIITAYRDHCTHLGRGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 91 DPKVIMAELTGRQAGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYET 170
Cdd:PLN02269 101 TVLEVFAELMGRKDGCSRGKGGSMHFYKKDANFYGGHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 171 FNMAALWNLPIVFVVENNGYAMGTAVKRSSAETEFYRRGTAfrIPGMDVNGMDVLEVRAAAEIAMDYVRKgGGPVLMELN 250
Cdd:PLN02269 181 LNIAALWDLPVIFVCENNHYGMGTAEWRAAKSPAYYKRGDY--VPGLKVDGMDVLAVKQACKFAKEHALS-NGPIVLEMD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 251 TYRYRGHSMSDP-AKYRSREEVQDVREKSDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFAENSPEPEMAELY 328
Cdd:PLN02269 258 TYRYHGHSMSDPgSTYRTRDEISGVRQERDPIERVRKLLLAHELaTEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELF 337
|
....*
gi 2176097075 329 TDVLV 333
Cdd:PLN02269 338 TNVYV 342
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
26-323 |
9.74e-122 |
|
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: 352.01 E-value: 9.74e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 26 EQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDgDKDSVITGYRDHGHMLAYGIDPKVIMAELTGRQAg 105
Cdd:pfam00676 1 RRMMTLRRMEDARDALYKRQGIRGFYHLYAGQEAAQVGIAAALE-PGDYIIPGYRDHGNLLARGLSLEEIFAELYGRVA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 106 isKGKGGSMHMF--STEHKFYGGHGIVGAQVALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWNLPIVF 183
Cdd:pfam00676 79 --KGKGGSMHGYygAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 184 VVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRKGGGPVLMELNTYRYRGHSMSDPA 263
Cdd:pfam00676 157 VCENNQYGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2176097075 264 -KYRSREEVQDVREKSDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFAENSPEPE 323
Cdd:pfam00676 237 sTYRTRDEYEEVRKKKDPIQRFKEHLVSKGVwSEEELKAIEKEVRKEVEEAFKKAESAPEPH 298
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
14-328 |
4.73e-101 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 301.01 E-value: 4.73e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 14 YKANDDELLKFYEQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDgDKDSVITGYRDHGHMLAYGIDPK 93
Cdd:CHL00149 15 NNINSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLA-ETDYVCSTYRDHVHALSKGVPPK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 94 VIMAELTGRQAGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQYN-------DDGGLCLAYFGDGAANQGQ 166
Cdd:CHL00149 94 NVMAELFGKETGCSRGRGGSMHIFSAPHNFLGGFAFIGEGIPIALGAAFQSIYRqqvlkevQPLRVTACFFGDGTTNNGQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 167 VYETFNMAALWNLPIVFVVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRKGGGPVL 246
Cdd:CHL00149 174 FFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAFGLPGIEVDGMDVLAVREVAKEAVERARQGDGPTL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 247 MELNTYRYRGHSMSDPAKYRSREEvQDVREKSDPIEGAKKALIERG-VSEEKLKEIDKAIKARVSDAADFAENSPEPEMA 325
Cdd:CHL00149 254 IEALTYRFRGHSLADPDELRSKQE-KEAWVARDPIKKLKSYIIDNElASQKELNKIQREVKIEIEQAVQFAISSPEPNIS 332
|
...
gi 2176097075 326 ELY 328
Cdd:CHL00149 333 DLK 335
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
19-331 |
1.22e-97 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 295.70 E-value: 1.22e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 19 DELLKFYEQMLLIRRFEERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDGDkDSVITGYRDHGHMLAYGIDPKVIMAE 98
Cdd:PLN02374 86 EEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKD-DSVVSTYRDHVHALSKGVPARAVMSE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 99 LTGRQAGISKGKGGSMHMFSTEHKFYGGHGIVGAQVALGGGLALAHQY-------NDDGGLCLAYFGDGAANQGQVYETF 171
Cdd:PLN02374 165 LFGKATGCCRGQGGSMHMFSKEHNLLGGFAFIGEGIPVATGAAFSSKYrrevlkeESCDDVTLAFFGDGTCNNGQFFECL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 172 NMAALWNLPIVFVVENNGYAMGTAVKRSSAETEFYRRGTAFRIPGMDVNGMDVLEVRAAAEIAMDYVRKGGGPVLMELNT 251
Cdd:PLN02374 245 NMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAFGMPGVHVDGMDVLKVREVAKEAIERARRGEGPTLVECET 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 252 YRYRGHSMSDPAKYRSREEVQDVREKsDPIEGAKKALIERGV-SEEKLKEIDKAIKARVSDAADFAENSPEPEMAELYTD 330
Cdd:PLN02374 325 YRFRGHSLADPDELRDPAEKAHYAAR-DPIAALKKYLIENGLaTEAELKAIEKKIDEVVEDAVEFADASPLPPRSQLLEN 403
|
.
gi 2176097075 331 V 331
Cdd:PLN02374 404 V 404
|
|
| TPP_E1_OGDC_like |
cd02016 |
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed ... |
134-261 |
9.17e-11 |
|
Thiamine pyrophosphate (TPP) family, E1 of OGDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the 2-oxoglutarate dehydrogenase multienzyme complex (OGDC). OGDC catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA and carbon dioxide, a key reaction of the tricarboxylic acid cycle.
Pssm-ID: 238974 [Multi-domain] Cd Length: 265 Bit Score: 61.39 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 134 VALGGGLALAHQYNDDGG---LCLAYFGDGA-ANQGQVYETFNMaalWNLP------IVFVVENN--GYAMGTAVKRSSA 201
Cdd:cd02016 121 VVMGKTRAKQDYRGDGERdkvLPILIHGDAAfAGQGVVYETLNL---SNLPgyttggTIHIVVNNqiGFTTDPRDSRSSP 197
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2176097075 202 E-TEFYRrgtAFRIPGMDVNGMDVLEVRAAAEIAMDYVRKGGGPVLMELNTYRYRGHSMSD 261
Cdd:cd02016 198 YcTDVAK---MIGAPIFHVNGDDPEAVVRATRLALEYRQKFKKDVVIDLVCYRRHGHNELD 255
|
|
| kgd |
PRK12270 |
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
158-317 |
8.77e-08 |
|
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;
Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 53.74 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 158 GDGA-ANQGQVYETFNMAALWNLPI---VFVVENN--GYAMGTAVKRSSaeteFYRRGTA--FRIPGMDVNGMDVLEVRA 229
Cdd:PRK12270 655 GDAAfAGQGVVAETLNLSQLRGYRTggtIHIVVNNqvGFTTAPESSRSS----EYATDVAkmIQAPIFHVNGDDPEAVVR 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 230 AAEIAMDYVRKGGGPVLMELNTYRYRGH------SMSDPAKYRSREEVQDVReksdpiEGAKKALIERG-VSEEKLKEID 302
Cdd:PRK12270 731 VARLAFEYRQRFHKDVVIDLVCYRRRGHnegddpSMTQPLMYDLIDAKRSVR------KLYTEALIGRGdITVEEAEQAL 804
|
170
....*....|....*
gi 2176097075 303 KAIKARVSDAadFAE 317
Cdd:PRK12270 805 RDYQGQLERV--FNE 817
|
|
| sucA |
PRK09404 |
2-oxoglutarate dehydrogenase E1 component; Reviewed |
158-323 |
7.32e-07 |
|
2-oxoglutarate dehydrogenase E1 component; Reviewed
Pssm-ID: 236499 [Multi-domain] Cd Length: 924 Bit Score: 50.89 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 158 GDGA-ANQGQVYETFNMAalwNLP------IVFVVENN--GYamgTAVKRSSaetefyrRGT--------AFRIPGMDVN 220
Cdd:PRK09404 350 GDAAfAGQGVVAETLNLS---QLRgyrtggTIHIVINNqiGF---TTSPPDD-------RSTpyctdvakMVQAPIFHVN 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 221 GMDVLEVRAAAEIAMDYVRKGGGPVLMELNTYRYRGHSMSD------PAKYRSreevqdVREKSDPIEGAKKALIERGV- 293
Cdd:PRK09404 417 GDDPEAVVFATRLALEYRQKFKKDVVIDLVCYRRHGHNEGDepsftqPLMYKK------IKKHPTTRELYADKLVAEGVi 490
|
170 180 190
....*....|....*....|....*....|
gi 2176097075 294 SEEKLKEIDKAIKARVsDAADFAENSPEPE 323
Cdd:PRK09404 491 TEEEADEMVNEYRDAL-DAGFEVVKEWRPA 519
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
125-251 |
1.54e-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: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 125 GGHGIVGAQVALGGGLALAHQynDDGGLCLAyfGDGAAN-QGQVYETfnmAALWNLPIVFVVENNG-YAMGtavkRSSAE 202
Cdd:cd00568 43 TGFGAMGYGLPAAIGAALAAP--DRPVVCIA--GDGGFMmTGQELAT---AVRYGLPVIVVVFNNGgYGTI----RMHQE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2176097075 203 TEFYRRGTAFRIPGMDVN------GMDVLEVRAAAEI--AMDYVRKGGGPVLMELNT 251
Cdd:cd00568 112 AFYGGRVSGTDLSNPDFAalaeayGAKGVRVEDPEDLeaALAEALAAGGPALIEVKT 168
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
123-248 |
1.55e-03 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 38.34 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 123 FYGGHGIVGAQVALGGGLALAHqyndDGGLCLAYFGDGAANqgqvyetFNMAALW-----NLPIVFVVENNG-YAMgtaV 196
Cdd:pfam02775 23 TSGGLGTMGYGLPAAIGAKLAR----PDRPVVAIAGDGGFQ-------MNLQELAtavryNLPITVVVLNNGgYGM---T 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2176097075 197 KRSSAETEFYRRGTAFRIPGMDVN--------GMDVLEVRAAAEI--AMDYVRKGGGPVLME 248
Cdd:pfam02775 89 RGQQTPFGGGRYSGPSGKILPPVDfaklaeayGAKGARVESPEELeeALKEALEHDGPALID 150
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
62-256 |
1.63e-03 |
|
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: 39.07 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 62 VGLQSALDGDKDSVI--TGYRDHGHMLaygidpkvimaeLTGRQAGIS-----KGKGGSMHMFSTEHKFYG-GHGivGAQ 133
Cdd:cd02007 15 LALHYVFDSPKDKIIwdVGHQAYPHKI------------LTGRRDQFHtlrqyGGLSGFTKRSESEYDAFGtGHS--STS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 134 VALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWNLPIVFVVENNgyamgtavKRSSAETeFYRRGTAFR 213
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDN--------EMSISPN-VGTPGNLFE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2176097075 214 IPGMD----VNGMDVLEVRAAAEiamdYVRKGGGPVLMELNTYRYRG 256
Cdd:cd02007 152 ELGFRyigpVDGHNIEALIKVLK----EVKDLKGPVLLHVVTKKGKG 194
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
139-251 |
1.93e-03 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 38.73 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 139 GLALAHqyndDGGLCLAYFGDGAANqgqvyetFNMAALW-----NLPIVFVVENN-GYAmgtAVKRSSAETEFYRRGTAF 212
Cdd:cd02002 60 GAALAN----PDRKVVAIIGDGSFM-------YTIQALWtaaryGLPVTVVILNNrGYG---ALRSFLKRVGPEGPGENA 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2176097075 213 RIPGMDVN------------GMDVLEVRAAAEIAMDYVR--KGGGPVLMELNT 251
Cdd:cd02002 126 PDGLDLLDpgidfaaiakafGVEAERVETPEELDEALREalAEGGPALIEVVV 178
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
62-261 |
2.38e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 39.71 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 62 VGLQSALDGDKDSVI--TGYRDHGHMLaygidpkvimaeLTGRQAGISKGK-GGSMHMFSTEHK-----FYGGHGIVGAQ 133
Cdd:PRK12571 59 VALHAVFNTPKDKLVwdVGHQCYPHKI------------LTGRRDRFRTLRqKGGLSGFTKRSEseydpFGAAHSSTSIS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 134 VALGggLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWNLPIVFVVENNGYAMGTAVKRSSAETEFYRRGT--- 210
Cdd:PRK12571 127 AALG--FAKARALGQPDGDVVAVIGDGSLTAGMAYEALNNAGAADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDpfa 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2176097075 211 AFRIPGMDVNGMDVLEVRAAAEIAMDYVRK-GGGPVLMELNTYRY----RGHSMSD 261
Cdd:PRK12571 205 RLRAIAKGVEERLPGPLRDGARRARELVTGmIGGGTLFEELGFTYvgpiDGHDMEA 260
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
126-268 |
3.70e-03 |
|
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: 38.25 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 126 GHGIvgaqvALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWNL-PIVFVVENNGYAMGTAVKRSSAETE 204
Cdd:cd02012 108 GQGL-----SVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLdNLIAIVDSNRIQIDGPTDDILFTED 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2176097075 205 FYRRGTAFripGMDV---NGMDVLEVRAaaeiAMDYVRKGGG-PVLMELNTYRYRG-HSMSDPAKYRSR 268
Cdd:cd02012 183 LAKKFEAF---GWNVievDGHDVEEILA----ALEEAKKSKGkPTLIIAKTIKGKGvPFMENTAKWHGK 244
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
35-188 |
9.83e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 37.77 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 35 EERAGQLYGLGLIGGFCHLYIGQEAVAVGLQSALDGDKDSVI--TGYRDHGHMLaygidpkvimaeLTGRQAGI-----S 107
Cdd:PLN02234 90 ELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILwdVGHQSYPHKI------------LTGRRGKMktirqT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2176097075 108 KGKGGSMHMFSTEHKFYG-GHGivGAQVALGGGLALAHQYNDDGGLCLAYFGDGAANQGQVYETFNMAALWNLPIVFVVE 186
Cdd:PLN02234 158 NGLSGYTKRRESEHDSFGtGHS--STTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILN 235
|
..
gi 2176097075 187 NN 188
Cdd:PLN02234 236 DN 237
|
|
| |
