|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-326 |
0e+00 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 588.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 1 MVSMTVRDALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIE 80
Cdd:PRK11892 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 81 FMTMNFAMQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKA 160
Cdd:PRK11892 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 161 AIRDPNPVVFLENEIMYGKTFTVPESvtkEDFVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLR 240
Cdd:PRK11892 299 AIRDPNPVIFLENEILYGQSFDVPKL---DDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 241 TIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMIFEsSAFNYIDAPLERVCGLDIPLAYAPNLEAMSLPSVAHI 320
Cdd:PRK11892 376 TIRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVME-QAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEV 454
|
....*.
gi 829172433 321 VNAAKK 326
Cdd:PRK11892 455 VEAVKA 460
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-328 |
2.65e-173 |
|
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: 483.36 E-value: 2.65e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 1 MVSMTVRDALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIE 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 81 FMTMNFAMQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKA 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 161 AIRDPNPVVFLENEIMYGKTFTVPEsvtkEDFVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLR 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYRLKGEVPE----EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 241 TIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMIFEsSAFNYIDAPLERVCGLDIPLAYAPNLEAMSLPSVAHI 320
Cdd:COG0022 237 TLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAE-EAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRI 315
|
....*...
gi 829172433 321 VNAAKKTL 328
Cdd:COG0022 316 VAAVRELL 323
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
8-174 |
3.02e-96 |
|
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: 282.06 E-value: 3.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 8 DALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIEFMTMNFA 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 88 MQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKAAIRDPNP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 829172433 168 VVFLENE 174
Cdd:cd07036 161 VIFLEHK 167
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
197-320 |
8.26e-49 |
|
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: 159.68 E-value: 8.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 197 GKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLRTIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEI 276
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 829172433 277 SAMIFEsSAFNYIDAPLERVCGLDIPLAYAP-NLEAMSLPSVAHI 320
Cdd:pfam02780 81 AAALAE-EAFDGLDAPVLRVGGPDFPEPGSAdELEKLYGLTPEKI 124
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
54-178 |
1.44e-25 |
|
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: 99.48 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 54 VDTPISEIGFAGIGVGAAMYGLKPIIEFMTMNFAMqaidhiinsaAKLRYMSNGDLHTQ-IVFRGLngPAAAV----AAQ 128
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDR----------AKDQIRSAGASGNVpVVFRHD--GGGGVgedgPTH 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 829172433 129 HSQCFAAWYSSCPGLIVIAPYDVEDARGLLKAAIRDPNP-VVFLENEIMYG 178
Cdd:smart00861 86 HSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-326 |
0e+00 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 588.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 1 MVSMTVRDALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIE 80
Cdd:PRK11892 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 81 FMTMNFAMQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKA 160
Cdd:PRK11892 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 161 AIRDPNPVVFLENEIMYGKTFTVPESvtkEDFVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLR 240
Cdd:PRK11892 299 AIRDPNPVIFLENEILYGQSFDVPKL---DDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 241 TIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMIFEsSAFNYIDAPLERVCGLDIPLAYAPNLEAMSLPSVAHI 320
Cdd:PRK11892 376 TIRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVME-QAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEV 454
|
....*.
gi 829172433 321 VNAAKK 326
Cdd:PRK11892 455 VEAVKA 460
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-328 |
0e+00 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 556.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 1 MVSMTVRDALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIE 80
Cdd:PTZ00182 32 TVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 81 FMTMNFAMQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKA 160
Cdd:PTZ00182 112 FMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 161 AIRDPNPVVFLENEIMYGKTFTVPESvtkEDFVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLR 240
Cdd:PTZ00182 192 AIRDPNPVVFFEPKLLYRESVEVVPE---ADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 241 TIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMIFEsSAFNYIDAPLERVCGLDIPLAYAPNLEAMSLPSVAHI 320
Cdd:PTZ00182 269 SLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIME-DCFLYLEAPIKRVCGADTPFPYAKNLEPAYLPDKEKV 347
|
....*...
gi 829172433 321 VNAAKKTL 328
Cdd:PTZ00182 348 VEAAKRVL 355
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
3-327 |
0e+00 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 553.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 3 SMTVRDALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIEFM 82
Cdd:PLN02683 26 EMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 83 TMNFAMQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKAAI 162
Cdd:PLN02683 106 TFNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLKAAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 163 RDPNPVVFLENEIMYGKTFTVPESVTKEDFVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLRTI 242
Cdd:PLN02683 186 RDPDPVVFLENELLYGESFPVSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 243 RPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMIFEsSAFNYIDAPLERVCGLDIPLAYAPNLEAMSLPSVAHIVN 322
Cdd:PLN02683 266 RPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVE-ESFDYLDAPVERIAGADVPMPYAANLERLALPQVEDIVR 344
|
....*
gi 829172433 323 AAKKT 327
Cdd:PLN02683 345 AAKRA 349
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
1-328 |
0e+00 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 530.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 1 MVSMTVRDALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIE 80
Cdd:PRK09212 1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 81 FMTMNFAMQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKA 160
Cdd:PRK09212 81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 161 AIRDPNPVVFLENEIMYGKTFTVPEsvtkEDFVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLR 240
Cdd:PRK09212 161 AIRDPNPVIFLENEILYGHSHEVPE----EEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 241 TIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMIFEsSAFNYIDAPLERVCGLDIPLAYAPNLEAMSLPSVAHI 320
Cdd:PRK09212 237 TLRPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMK-EAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDI 315
|
....*...
gi 829172433 321 VNAAKKTL 328
Cdd:PRK09212 316 IEAVKKVC 323
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-328 |
2.65e-173 |
|
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: 483.36 E-value: 2.65e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 1 MVSMTVRDALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIE 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 81 FMTMNFAMQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKA 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 161 AIRDPNPVVFLENEIMYGKTFTVPEsvtkEDFVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLR 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYRLKGEVPE----EDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 241 TIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMIFEsSAFNYIDAPLERVCGLDIPLAYAPNLEAMSLPSVAHI 320
Cdd:COG0022 237 TLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAE-EAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRI 315
|
....*...
gi 829172433 321 VNAAKKTL 328
Cdd:COG0022 316 VAAVRELL 323
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
1-332 |
2.18e-96 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 288.56 E-value: 2.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 1 MVSMTVRDALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIE 80
Cdd:CHL00144 1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 81 FMTMNFAMQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIA---PYDvedARGL 157
Cdd:CHL00144 81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVAcstPYN---AKGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 158 LKAAIRDPNPVVFLENEIMYGKTFTVPEsvtkEDFVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVI 237
Cdd:CHL00144 158 LKSAIRSNNPVIFFEHVLLYNLKEEIPD----NEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 238 NLRTIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMIFEsSAFNYIDAPLERVCGLDIPLAYAPNLEAMSLPSV 317
Cdd:CHL00144 234 DLISLKPLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINE-HLFDELDAPIVRLSSQDVPTPYNGPLEEATVIQP 312
|
330
....*....|....*
gi 829172433 318 AHIVNAAKKTLVGHK 332
Cdd:CHL00144 313 AQIIEAVEQIITNKK 327
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
8-174 |
3.02e-96 |
|
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: 282.06 E-value: 3.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 8 DALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIEFMTMNFA 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 88 MQAIDHIINSAAKLRYMSNGDLHTQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKAAIRDPNP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 829172433 168 VVFLENE 174
Cdd:cd07036 161 VIFLEHK 167
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
197-320 |
8.26e-49 |
|
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: 159.68 E-value: 8.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 197 GKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLRTIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEI 276
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 829172433 277 SAMIFEsSAFNYIDAPLERVCGLDIPLAYAP-NLEAMSLPSVAHI 320
Cdd:pfam02780 81 AAALAE-EAFDGLDAPVLRVGGPDFPEPGSAdELEKLYGLTPEKI 124
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
3-179 |
2.36e-44 |
|
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: 149.62 E-value: 2.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 3 SMTVRDALQSAMADEIARDPQVFLMGEEVAnyHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYG-LKPIIEF 81
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 82 MTMNFAMqaidhiINSAAKLRYMSNGDLH-TQIVFRGLNGPAAAVAAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKA 160
Cdd:pfam02779 80 TFSDFLN------RADDAIRHGAALGKLPvPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRA 153
|
170 180
....*....|....*....|.
gi 829172433 161 AIR--DPNPVVFLENEIMYGK 179
Cdd:pfam02779 154 AIRrdGRKPVVLRLPRQLLRP 174
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
1-328 |
4.61e-39 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 140.22 E-value: 4.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 1 MVSMTVRDALQSAMADEIARDPQVFLMGEEVANYhgaykvskGLLEKFG---PDRIVDTPISE---IGFAGigvGAAMYG 74
Cdd:COG3958 1 MEKKAMRDAFGEALVELAEEDPDIVVLDADLGGS--------TKLDKFAkafPDRFFNVGIAEqnmVGVAA---GLALAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 75 LKPIIE----FMTMNfamqAIDHIINSAAklrYMsngDLHTQIVF------RGLNGPAaavaaqHsQCFA--AWYSSCPG 142
Cdd:COG3958 70 KIPFVStfapFLTGR----AYEQIRNDIA---YP---NLNVKIVGshaglsYGEDGAT------H-QALEdiALMRALPN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 143 LIVIAPYDVEDARGLLKAAIRDPNPVvfleneimY---GKTfTVPEsVTKEDFVLPIGKAKIMREGTDVTLVSFSKPVGM 219
Cdd:COG3958 133 MTVIVPADAVETEAAVRAAAEHDGPV--------YlrlGRG-AVPV-VYDEDYEFEIGKARVLREGKDVTIIATGIMVAE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 220 CLEAAEELQKQGISAEVINLRTIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMIFESsafnyIDAPLERVCGL 299
Cdd:COG3958 203 ALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVVTAEEHSIIGGLGSAVAEVLAEN-----YPVPLRRIGVP 277
|
330 340 350
....*....|....*....|....*....|..
gi 829172433 300 DIPLAYAPN---LEAMSLpSVAHIVNAAKKTL 328
Cdd:COG3958 278 DRFGESGSPeelLEKYGL-DAEGIVAAAKELL 308
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
141-280 |
2.85e-27 |
|
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: 112.03 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 141 PGLIVIAPYDVEDARGLLKAAIRDPNPVVfleneIMY----GKTFTVPESVTKedfvLPIGKAKIMREGTDVTLVSFSKP 216
Cdd:COG1154 442 PNMVIMAPKDENELRHMLYTALAYDGPTA-----IRYprgnGPGVELPAELEP----LPIGKGEVLREGKDVAILAFGTM 512
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 829172433 217 VGMCLEAAEELQKQGISAEVINLRTIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGAEISAMI 280
Cdd:COG1154 513 VAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVEEGVLAGGFGSAVLEFL 576
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
54-178 |
1.44e-25 |
|
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: 99.48 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 54 VDTPISEIGFAGIGVGAAMYGLKPIIEFMTMNFAMqaidhiinsaAKLRYMSNGDLHTQ-IVFRGLngPAAAV----AAQ 128
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDR----------AKDQIRSAGASGNVpVVFRHD--GGGGVgedgPTH 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 829172433 129 HSQCFAAWYSSCPGLIVIAPYDVEDARGLLKAAIRDPNP-VVFLENEIMYG 178
Cdd:smart00861 86 HSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
43-280 |
3.79e-22 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 97.10 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 43 GLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIEFMTmNFAMQAIDHIINSAAklrymsngdLH----TQIVFR-G 117
Cdd:PRK12571 353 DKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYS-TFLQRGYDQLLHDVA---------LQnlpvRFVLDRaG 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 118 LNGPAAAvaaQHSQCFAAWYSSC-PGLIVIAPYDVEDARGLLKAAI-RDPNPVVFleneiMYGKTFTVPESVTKEDFVLP 195
Cdd:PRK12571 423 LVGADGA---THAGAFDLAFLTNlPNMTVMAPRDEAELRHMLRTAAaHDDGPIAV-----RFPRGEGVGVEIPAEGTILG 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 196 IGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLRTIRPLDrQTIINSIKKTHRIVTVEEGWPQNGIGAE 275
Cdd:PRK12571 495 IGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLD-EALTDLLVRHHIVVIVEEQGAMGGFGAH 573
|
....*
gi 829172433 276 ISAMI 280
Cdd:PRK12571 574 VLHHL 578
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
45-280 |
6.12e-21 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 93.22 E-value: 6.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 45 LEKFG---PDRIVDTPISE---IGFAGigvGAAMYGLKPIiefmtmnFA-----MQ-AIDHIINSAA--KLRymsngdlh 110
Cdd:PRK05444 312 LVKFSkrfPDRYFDVGIAEqhaVTFAA---GLATEGLKPV-------VAiystfLQrAYDQVIHDVAlqNLP-------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 111 tqIVF---R-GLNGPAAAVaaqHSQCFAAWYSSC-PGLIVIAPYDVEDARGLLKAAIR-DPNPVVfleneIMYGKTFTVP 184
Cdd:PRK05444 374 --VTFaidRaGLVGADGPT---HQGAFDLSYLRCiPNMVIMAPSDENELRQMLYTALAyDDGPIA-----IRYPRGNGVG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 185 ESVTKEDfVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQkqgiSAEVINLRTIRPLDRQTIINSIKKTHRIVTVE 264
Cdd:PRK05444 444 VELPELE-PLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVE 518
|
250
....*....|....*.
gi 829172433 265 EGWPQNGIGAEISAMI 280
Cdd:PRK05444 519 EGAIMGGFGSAVLEFL 534
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
31-174 |
8.78e-18 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; 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 group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 78.93 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 31 VANYHGAYKVSKGLLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIEFMTMNFAMQAIDHIINSAAKlrymsngdlH 110
Cdd:cd06586 15 VFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADAAAE---------H 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 829172433 111 TQIVFR-GLNGPAAAV-AAQHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKAAIRD---PNPVVFLENE 174
Cdd:cd06586 86 LPVVFLiGARGISAQAkQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAyasQGPVVVRLPR 154
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
8-170 |
2.69e-16 |
|
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), 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. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. 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. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). 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: 132916 [Multi-domain] Cd Length: 156 Bit Score: 74.79 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 8 DALQSAMADEIARDPQVFLMGEEVANYHGAYKVSKGLlekfgPDRIVDTPISEIGFAGIGVGAAMYGLKPIIEFMTMnFA 87
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKF-----PDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSF-FL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 88 MQAIDHIINSAAklrYMsngdlHTQIVFRGlNGPAAAVAA----QHSQCFAAWYSSCPGLIVIAPYDVEDARGLLKAAIR 163
Cdd:cd07033 75 QRAYDQIRHDVA---LQ-----NLPVKFVG-THAGISVGEdgptHQGIEDIALLRAIPNMTVLRPADANETAAALEAALE 145
|
....*..
gi 829172433 164 DPNPVVF 170
Cdd:cd07033 146 YDGPVYI 152
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
29-266 |
3.23e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 76.48 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 29 EEVANYHGAYKVSKGL---LEKFgPDRIVDTPISEIGFAGIGVGAAMYGLKPIIEFMTmNFAMQAIDHIINSAaklryms 105
Cdd:PLN02582 374 KDVVAIHAAMGGGTGLnlfARRF-PTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYS-SFLQRGYDQVVHDV------- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 106 ngDLHTQIVFRGLN--GPAAAVAAQHSQCFAAWYSSC-PGLIVIAPYDVEDARGLL-KAAIRDPNPVVFlenEIMYGKTF 181
Cdd:PLN02582 445 --DLQKLPVRFAMDraGLVGADGPTHCGAFDVTYMAClPNMVVMAPSDEAELFHMVaTAAAIDDRPSCF---RYPRGNGI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 182 TVPESVTKEDFVLPIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLRTIRPLDRqTIINSIKKTHR-I 260
Cdd:PLN02582 520 GVQLPPNNKGIPIEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDR-ALIRSLAKSHEvL 598
|
....*.
gi 829172433 261 VTVEEG 266
Cdd:PLN02582 599 ITVEEG 604
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
44-266 |
9.00e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 75.13 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 44 LLEKFGPDRIVDTPISEIGFAGIGVGAAMYGLKPIIEFMTmNFAMQAIDHIINSAaklrymsngDLHTQIVFRGLN--GP 121
Cdd:PLN02234 392 LFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHDV---------DLQKLPVRFAIDraGL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 122 AAAVAAQHSQCFAAWYSSC-PGLIVIAPYDVEDARGLL-KAAIRDPNPVVFLENEimyGKTFTVPESVTKEDFVLPIGKA 199
Cdd:PLN02234 462 MGADGPTHCGAFDVTFMAClPNMIVMAPSDEAELFNMVaTAAAIDDRPSCFRYHR---GNGIGVSLPPGNKGVPLQIGRG 538
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 829172433 200 KIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEVINLRTIRPLDrQTIINSIKKTHRI-VTVEEG 266
Cdd:PLN02234 539 RILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLD-VALIRSLAKSHEVlITVEEG 605
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
5-280 |
8.32e-14 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 72.05 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 5 TVRDALQSAMADEIARDPQVFLMgeevanyHGAYKVSKGLL---EKFgPDRIVDTPISEIGFAGIGVGAAMYGLKPIIeF 81
Cdd:PLN02225 382 TYSDCFVEALVMEAEKDRDIVVV-------HAGMEMDASLItfqERF-PDRFFNVGMAEQHAVTFSAGLSSGGLKPFC-I 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 82 MTMNFAMQAIDHIINSAAKLRYMsngdLHTQIVFRGLNGPAAAVaaqhsQCFA---AWYSSCPGLIVIAPYDVEDARGLL 158
Cdd:PLN02225 453 IPSAFLQRAYDQVVHDVDRQRKA----VRFVITSAGLVGSDGPV-----QCGAfdiAFMSSLPNMIAMAPADEDELVNMV 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 159 -KAAIRDPNPVVF-LENEIMYGKTFTVPESVTKEdfvlpIGKAKIMREGTDVTLVSFSKPVGMCLEAAEELQKQGISAEV 236
Cdd:PLN02225 524 aTAAYVTDRPVCFrFPRGSIVNMNYLVPTGLPIE-----IGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTV 598
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 829172433 237 INLRTIRPLDRQtIINSIKKTHRI-VTVEEGWpQNGIGAEISAMI 280
Cdd:PLN02225 599 ADARFCKPLDIK-LVRDLCQNHKFlITVEEGC-VGGFGSHVAQFI 641
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
50-277 |
5.23e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 63.49 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 50 PDRIVDTPISE---IGFAGigvGAAMYGLKPIIeFMTMNFAMQAIDHIINSAAklrymSNGDLHTQIVFrglNGPAAAVA 126
Cdd:PRK12315 319 PDQYVDVGIAEqesVAFAS---GIAANGARPVI-FVNSTFLQRAYDQLSHDLA-----INNNPAVMIVF---GGSISGND 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 127 AQHSQCFA-AWYSSCPGLIVIAPYDVEDARGLLKAAIRDPN-PVVFLENEimyGKTFTVPESVTkeDFVLPigKAKIMRE 204
Cdd:PRK12315 387 VTHLGIFDiPMISNIPNLVYLAPTTKEELIAMLEWALTQHEhPVAIRVPE---HGVESGPTVDT--DYSTL--KYEVTKA 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 829172433 205 GTDVTLVSfskpVGMCLEAAEELQKQ-----GISAEVINLRTIRPLDRQTiINSIKKTHRIV-TVEEGWPQNGIGAEIS 277
Cdd:PRK12315 460 GEKVAILA----LGDFYELGEKVAKKlkeelGIDATLINPKFITGLDEEL-LEKLKEDHELVvTLEDGILDGGFGEKIA 533
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
141-269 |
1.56e-06 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 49.75 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 141 PGLIVIAPYD-VEDARGLLKAAIRDPNPVVFLeneIMYGKTFTVPESVTKEDFvlpIGKAKIMREGTDVTLVSFSKPVGM 219
Cdd:PRK05899 413 PNLTVIRPADaNETAAAWKYALERKDGPSALV---LTRQNLPVLERTAQEEGV---AKGGYVLRDDPDVILIATGSEVHL 486
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 829172433 220 CLEAAEELQKQGISAEVINLRTIRPLDRQ--TIINSI--KKTHRIVTVEEGWPQ 269
Cdd:PRK05899 487 ALEAADELEAEGIKVRVVSMPSTELFDEQdaAYKESVlpAAVTARVAVEAGVAD 540
|
|
| porA |
PRK09622 |
2-oxoacid:ferredoxin oxidoreductase subunit alpha; |
158-289 |
9.70e-05 |
|
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
Pssm-ID: 181999 [Multi-domain] Cd Length: 407 Bit Score: 43.60 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829172433 158 LKAAIRDPNPV---VFLENEIMYGKTFTVPESVTKEDfvlpigkakimregTDVTLVSFSKPVGMCLEAAEELQKQGISA 234
Cdd:PRK09622 231 LHHALMSSSSVieeVFNDFAKLTGRKYNLVETYQLED--------------AEVAIVALGTTYESAIVAAKEMRKEGIKA 296
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 829172433 235 EVINLRTIRPLDRQTIINSIKKTHRIVTVEEGWPQNGIGA---EISAMIFESSAF------NYI 289
Cdd:PRK09622 297 GVATIRVLRPFPYERLGQALKNLKALAILDRSSPAGAMGAlfnEVTSAVYQTQGTkhpvvsNYI 360
|
|
| |
