|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-325 |
0e+00 |
|
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 439793 [Multi-domain] Cd Length: 325 Bit Score: 510.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 1 MAQMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGigglalglglngF----- 75
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAG------------Ivgaai 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 76 -------RPVMEIQFFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIP 148
Cdd:COG0022 69 gaalaglRPVVEIQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 149 STPYDAKGLLISAIRDNDPVVFLEHMKLYRSfRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDG 228
Cdd:COG0022 149 STPYDAKGLLKAAIRDDDPVIFLEHKRLYRL-KGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 229 ISAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFSQA-ESV 307
Cdd:COG0022 228 ISAEVIDLRTLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPAlEKA 307
|
330
....*....|....*...
gi 503879666 308 WLPNHKDVLETARKVLEF 325
Cdd:COG0022 308 YLPSADRIVAAVRELLAY 325
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-323 |
4.73e-132 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 379.71 E-value: 4.73e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 1 MAQMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVME 80
Cdd:PTZ00182 32 TVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 81 IQFFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLIS 160
Cdd:PTZ00182 112 FMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 161 AIRDNDPVVFLEHMKLYRSFRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVS 240
Cdd:PTZ00182 192 AIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 241 PLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFSQA-ESVWLPNHKDVLETA 319
Cdd:PTZ00182 272 PWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNlEPAYLPDKEKVVEAA 351
|
....
gi 503879666 320 RKVL 323
Cdd:PTZ00182 352 KRVL 355
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
8-173 |
1.72e-77 |
|
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132919 [Multi-domain] Cd Length: 167 Bit Score: 234.29 E-value: 1.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 8 QAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVMEIQFFGFV 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 88 YEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLISAIRDNDP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*.
gi 503879666 168 VVFLEH 173
Cdd:cd07036 161 VIFLEH 166
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
194-315 |
1.00e-45 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 151.21 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 194 GKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQEAQKQAGIAANV 273
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 503879666 274 VAEINDRAILSLEAPVLRVAAPDTVFPFSQA--ESVWLPNHKDV 315
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPDFPEPGSADelEKLYGLTPEKI 124
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
2-178 |
1.29e-24 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 96.79 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 2 AQMTMIQAITDALRTELkndenvlvfgedvgvnggvfrateglqkefgedrvFDTPLAESGIGGLALGLGLNGFRPVMEI 81
Cdd:smart00861 1 KKIATRKAFGEALAELA-----------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 82 QFFGFVYevmdsvsgqmARMRYRSGGRWTS-PVTIRSPFGGGVHT--PELHADSLEGLVAQQPGIKVVIPSTPYDAKGLL 158
Cdd:smart00861 46 FFTFFDR----------AKDQIRSAGASGNvPVVFRHDGGGGVGEdgPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLL 115
|
170 180
....*....|....*....|.
gi 503879666 159 ISAIRDNDP-VVFLEHMKLYR 178
Cdd:smart00861 116 RAAIRDDGPvVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-325 |
0e+00 |
|
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 439793 [Multi-domain] Cd Length: 325 Bit Score: 510.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 1 MAQMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGigglalglglngF----- 75
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAG------------Ivgaai 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 76 -------RPVMEIQFFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIP 148
Cdd:COG0022 69 gaalaglRPVVEIQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 149 STPYDAKGLLISAIRDNDPVVFLEHMKLYRSfRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDG 228
Cdd:COG0022 149 STPYDAKGLLKAAIRDDDPVIFLEHKRLYRL-KGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 229 ISAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFSQA-ESV 307
Cdd:COG0022 228 ISAEVIDLRTLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPAlEKA 307
|
330
....*....|....*...
gi 503879666 308 WLPNHKDVLETARKVLEF 325
Cdd:COG0022 308 YLPSADRIVAAVRELLAY 325
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-323 |
4.73e-132 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 379.71 E-value: 4.73e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 1 MAQMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVME 80
Cdd:PTZ00182 32 TVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 81 IQFFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLIS 160
Cdd:PTZ00182 112 FMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 161 AIRDNDPVVFLEHMKLYRSFRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVS 240
Cdd:PTZ00182 192 AIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 241 PLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFSQA-ESVWLPNHKDVLETA 319
Cdd:PTZ00182 272 PWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNlEPAYLPDKEKVVEAA 351
|
....
gi 503879666 320 RKVL 323
Cdd:PTZ00182 352 KRVL 355
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
1-324 |
1.26e-101 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 301.64 E-value: 1.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 1 MAQMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVME 80
Cdd:PRK09212 1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 81 IQFFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLIS 160
Cdd:PRK09212 81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 161 AIRDNDPVVFLEHMKLYrSFRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVS 240
Cdd:PRK09212 161 AIRDPNPVIFLENEILY-GHSHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 241 PLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFSQA-ESVWLPNHKDVLETA 319
Cdd:PRK09212 240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYAANlEKLALPSEEDIIEAV 319
|
....*
gi 503879666 320 RKVLE 324
Cdd:PRK09212 320 KKVCY 324
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-322 |
1.35e-85 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 265.24 E-value: 1.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 1 MAQMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVME 80
Cdd:PRK11892 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 81 IQFFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLIS 160
Cdd:PRK11892 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 161 AIRDNDPVVFLEHMKLY-RSFrqEVPE-EEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRT 238
Cdd:PRK11892 299 AIRDPNPVIFLENEILYgQSF--DVPKlDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 239 VSPLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFS-QAESVWLPNHKDVLE 317
Cdd:PRK11892 377 IRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAaNLEKLALPSVAEVVE 456
|
....*
gi 503879666 318 TARKV 322
Cdd:PRK11892 457 AVKAV 461
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
1-302 |
1.77e-84 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 257.75 E-value: 1.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 1 MAQMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVME 80
Cdd:CHL00144 1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 81 IQFFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLIS 160
Cdd:CHL00144 81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 161 AIRDNDPVVFLEHMKLYrSFRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVS 240
Cdd:CHL00144 161 AIRSNNPVIFFEHVLLY-NLKEEIPDNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503879666 241 PLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFS 302
Cdd:CHL00144 240 PLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYN 301
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
3-322 |
1.59e-80 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 248.58 E-value: 1.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 3 QMTMIQAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVMEIQ 82
Cdd:PLN02683 26 EMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 83 FFGFVYEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLISAI 162
Cdd:PLN02683 106 TFNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLKAAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 163 RDNDPVVFLEHMKLY-RSF--RQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTV 239
Cdd:PLN02683 186 RDPDPVVFLENELLYgESFpvSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 240 SPLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFPFS-QAESVWLPNHKDVLET 318
Cdd:PLN02683 266 RPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPYAaNLERLALPQVEDIVRA 345
|
....
gi 503879666 319 ARKV 322
Cdd:PLN02683 346 AKRA 349
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
8-173 |
1.72e-77 |
|
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132919 [Multi-domain] Cd Length: 167 Bit Score: 234.29 E-value: 1.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 8 QAITDALRTELKNDENVLVFGEDVGVNGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLALGLGLNGFRPVMEIQFFGFV 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 88 YEVMDSVSGQMARMRYRSGGRWTSPVTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLISAIRDNDP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*.
gi 503879666 168 VVFLEH 173
Cdd:cd07036 161 VIFLEH 166
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
194-315 |
1.00e-45 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 151.21 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 194 GKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQEAQKQAGIAANV 273
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 503879666 274 VAEINDRAILSLEAPVLRVAAPDTVFPFSQA--ESVWLPNHKDV 315
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPDFPEPGSADelEKLYGLTPEKI 124
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
141-297 |
1.01e-36 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 133.67 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 141 PGIKVVIPSTPYDAKGLLISAIRDNDPVvfleHMKLYRSFRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKA 220
Cdd:COG3958 131 PNMTVIVPADAVETEAAVRAAAEHDGPV----YLRLGRGAVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 221 AEELEKDGISAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQEAQKQAGIA---ANVVAEindrailSLEAPVLRVAAPDT 297
Cdd:COG3958 207 AELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVVTAEEHSIIGGLGsavAEVLAE-------NYPVPLRRIGVPDR 279
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
2-178 |
3.05e-31 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 115.34 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 2 AQMTMIQAITDALRTELKNDENVLVFGEDVGvnGGVFRATEGLQKEFGEDRVFDTPLAESGIGGLAL-GLGLNGFRPVME 80
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANgMALHGPLLPPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 81 IQFFGFvyevmdSVSGQMARMRYRSGGRWTSP-VTIRSPFGGGVHTPELHADSLEGLVAQQPGIKVVIPSTPYDAKGLLI 159
Cdd:pfam02779 79 ATFSDF------LNRADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLR 152
|
170 180
....*....|....*....|.
gi 503879666 160 SAIR--DNDPVVFLEHMKLYR 178
Cdd:pfam02779 153 AAIRrdGRKPVVLRLPRQLLR 173
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
183-296 |
5.14e-25 |
|
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: 105.48 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 183 EVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQE 262
Cdd:COG1154 482 ELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVEE 561
|
90 100 110
....*....|....*....|....*....|....
gi 503879666 263 AQKQAGIAANVVAEINDRAILsleAPVLRVAAPD 296
Cdd:COG1154 562 GVLAGGFGSAVLEFLADAGLD---VPVLRLGLPD 592
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
2-178 |
1.29e-24 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 96.79 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 2 AQMTMIQAITDALRTELkndenvlvfgedvgvnggvfrateglqkefgedrvFDTPLAESGIGGLALGLGLNGFRPVMEI 81
Cdd:smart00861 1 KKIATRKAFGEALAELA-----------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 82 QFFGFVYevmdsvsgqmARMRYRSGGRWTS-PVTIRSPFGGGVHT--PELHADSLEGLVAQQPGIKVVIPSTPYDAKGLL 158
Cdd:smart00861 46 FFTFFDR----------AKDQIRSAGASGNvPVVFRHDGGGGVGEdgPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLL 115
|
170 180
....*....|....*....|.
gi 503879666 159 ISAIRDNDP-VVFLEHMKLYR 178
Cdd:smart00861 116 RAAIRDDGPvVIRLERKSLYR 136
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
141-305 |
1.41e-20 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 92.07 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 141 PGIKVVIPSTPYDAKGLLISAIRDND-PVVFlehmklyR----SFRQEVPEEEYTIELGKADVKREGTDLSIITYGAMVH 215
Cdd:PRK05444 404 PNMVIMAPSDENELRQMLYTALAYDDgPIAI-------RyprgNGVGVELPELEPLPIGKGEVLREGEDVAILAFGTMLA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 216 ESLKAAEELEkdgiSAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQEAQKQAGIAANVVAEINDRAILsleAPVLRVAAP 295
Cdd:PRK05444 477 EALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMGGFGSAVLEFLADHGLD---VPVLNLGLP 549
|
170
....*....|.
gi 503879666 296 DTVFPF-SQAE 305
Cdd:PRK05444 550 DEFIDHgSREE 560
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
183-300 |
1.26e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 77.46 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 183 EVPEEEYTIELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVSPLDiDTIIASVEKTGRAIVVQE 262
Cdd:PRK12571 485 EIPAEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLD-EALTDLLVRHHIVVIVEE 563
|
90 100 110
....*....|....*....|....*....|....*...
gi 503879666 263 AQKQAGIAANVVAEINDRAILSLEAPVLRVAAPDTVFP 300
Cdd:PRK12571 564 QGAMGGFGAHVLHHLADTGLLDGGLKLRTLGLPDRFID 601
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
181-263 |
9.01e-09 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 56.30 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 181 RQEVP-----EEEYTIELGKADVKREGtDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVSPLDI--DTIIASVEK 253
Cdd:PRK05899 447 RQNLPvlertAQEEGVAKGGYVLRDDP-DVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEqdAAYKESVLP 525
|
90
....*....|.
gi 503879666 254 TG-RAIVVQEA 263
Cdd:PRK05899 526 AAvTARVAVEA 536
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
191-274 |
1.42e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 52.98 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 191 IELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVSPLDiDTIIASVEKTGRAIVVQEAQKQAGIA 270
Cdd:PLN02582 532 IEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLD-RALIRSLAKSHEVLITVEEGSIGGFG 610
|
....
gi 503879666 271 ANVV 274
Cdd:PLN02582 611 SHVA 614
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
191-274 |
4.85e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 48.17 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503879666 191 IELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVSPLDIdTIIASVEKTGRAIVVQEAQKQAGIA 270
Cdd:PLN02234 533 LQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDV-ALIRSLAKSHEVLITVEEGSIGGFG 611
|
....
gi 503879666 271 ANVV 274
Cdd:PLN02234 612 SHVV 615
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
191-263 |
6.91e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 47.79 E-value: 6.91e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503879666 191 IELGKADVKREGTDLSIITYGAMVHESLKAAEELEKDGISAEVVDLRTVSPLDIDTIIASVEKTGRAIVVQEA 263
Cdd:PLN02225 556 IEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITVEEG 628
|
|
| |
