|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-327 |
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: 544.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 1 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAE 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 81 IQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLS 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 161 SIESNDPVLYFEHKKAYRfLKEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYR-LKGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 241 PLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDTPIMRLAAPDVPsMPFSPVLENEIMMNPEKILNK 320
Cdd:COG0022 240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTP-IPYAPALEKAYLPSADRIVAA 318
|
....*..
gi 593418481 321 MRELAEF 327
Cdd:COG0022 319 VRELLAY 325
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-324 |
8.78e-146 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 414.76 E-value: 8.78e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 1 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAE 80
Cdd:PTZ00182 32 TVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 81 IQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLS 160
Cdd:PTZ00182 112 FMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 161 SIESNDPVLYFEHKKAYRFLKEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY 240
Cdd:PTZ00182 192 AIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 241 PLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDTPIMRLAAPDVPsMPFSPVLENEIMMNPEKILNK 320
Cdd:PTZ00182 272 PWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTP-FPYAKNLEPAYLPDKEKVVEA 350
|
....
gi 593418481 321 MREL 324
Cdd:PTZ00182 351 AKRV 354
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
8-174 |
5.48e-98 |
|
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: 286.30 E-value: 5.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 8 EAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAEIQFADFI 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 88 LPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 593418481 168 VLYFEHK 174
Cdd:cd07036 161 VIFLEHK 167
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
194-317 |
2.47e-47 |
|
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: 155.45 E-value: 2.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 194 GKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVYPLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEV 273
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 593418481 274 SAIIAEHCLFDLDTPIMRLAAPDVPsMPFSP-VLENEIMMNPEKI 317
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPDFP-EPGSAdELEKLYGLTPEKI 124
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
54-178 |
3.68e-39 |
|
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: 134.92 E-value: 3.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 54 IDTPLAESNIVGTAIGAAMVGKRPIAEIQFADFILpatnqiiseaAKMRYRSNNDWQ-CPLTIRAPFGGGVH--GGLYHS 130
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDR----------AKDQIRSAGASGnVPVVFRHDGGGGVGedGPTHHS 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 593418481 131 QSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDP-VLYFEHKKAYR 178
Cdd:smart00861 88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-327 |
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: 544.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 1 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAE 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 81 IQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLS 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 161 SIESNDPVLYFEHKKAYRfLKEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYR-LKGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 241 PLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDTPIMRLAAPDVPsMPFSPVLENEIMMNPEKILNK 320
Cdd:COG0022 240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTP-IPYAPALEKAYLPSADRIVAA 318
|
....*..
gi 593418481 321 MRELAEF 327
Cdd:COG0022 319 VRELLAY 325
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-324 |
8.78e-146 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 414.76 E-value: 8.78e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 1 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAE 80
Cdd:PTZ00182 32 TVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 81 IQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLS 160
Cdd:PTZ00182 112 FMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 161 SIESNDPVLYFEHKKAYRFLKEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY 240
Cdd:PTZ00182 192 AIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 241 PLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDTPIMRLAAPDVPsMPFSPVLENEIMMNPEKILNK 320
Cdd:PTZ00182 272 PWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTP-FPYAKNLEPAYLPDKEKVVEA 350
|
....
gi 593418481 321 MREL 324
Cdd:PTZ00182 351 AKRV 354
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
1-326 |
1.38e-106 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 314.35 E-value: 1.38e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 1 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAE 80
Cdd:PRK09212 1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 81 IQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLS 160
Cdd:PRK09212 81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 161 SIESNDPVLYFEHKKAYRfLKEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY 240
Cdd:PRK09212 161 AIRDPNPVIFLENEILYG-HSHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 241 PLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDTPIMRLAAPDVPsMPFSPVLENEIMMNPEKILNK 320
Cdd:PRK09212 240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVP-LPYAANLEKLALPSEEDIIEA 318
|
....*.
gi 593418481 321 MRELAE 326
Cdd:PRK09212 319 VKKVCY 324
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
1-324 |
5.61e-99 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 294.72 E-value: 5.61e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 1 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAE 80
Cdd:CHL00144 1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 81 IQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLS 160
Cdd:CHL00144 81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 161 SIESNDPVLYFEHKKAYRfLKEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY 240
Cdd:CHL00144 161 AIRSNNPVIFFEHVLLYN-LKEEIPDNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 241 PLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDTPIMRLAAPDVPSmPFSPVLENEIMMNPEKILNK 320
Cdd:CHL00144 240 PLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPT-PYNGPLEEATVIQPAQIIEA 318
|
....
gi 593418481 321 MREL 324
Cdd:CHL00144 319 VEQI 322
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
8-174 |
5.48e-98 |
|
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: 286.30 E-value: 5.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 8 EAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAEIQFADFI 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 88 LPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 593418481 168 VLYFEHK 174
Cdd:cd07036 161 VIFLEHK 167
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-317 |
1.37e-85 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 265.24 E-value: 1.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 1 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAE 80
Cdd:PRK11892 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 81 IQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLS 160
Cdd:PRK11892 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 161 SIESNDPVLYFEHKKAY--RFlkeEVPE-EYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLR 237
Cdd:PRK11892 299 AIRDPNPVIFLENEILYgqSF---DVPKlDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 238 TVYPLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDTPIMRLAAPDVPsMPFSPVLENEIMMNPEKI 317
Cdd:PRK11892 376 TIRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVP-MPYAANLEKLALPSVAEV 454
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
8-308 |
5.85e-84 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 257.44 E-value: 5.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 8 EAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAEIQFADFI 87
Cdd:PLN02683 31 DALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTFNFS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 88 LPATNQIISEAAKMRYRSNNDWQCPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDP 167
Cdd:PLN02683 111 MQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLKAAIRDPDP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 168 VLYFEHKKAY--RF-LKEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVYPLDK 244
Cdd:PLN02683 191 VVFLENELLYgeSFpVSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDR 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 593418481 245 ETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDTPIMRLAAPDVPsMPFSPVLEN 308
Cdd:PLN02683 271 DTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVP-MPYAANLER 333
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
194-317 |
2.47e-47 |
|
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: 155.45 E-value: 2.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 194 GKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVYPLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEV 273
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 593418481 274 SAIIAEHCLFDLDTPIMRLAAPDVPsMPFSP-VLENEIMMNPEKI 317
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPDFP-EPGSAdELEKLYGLTPEKI 124
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
1-324 |
2.49e-45 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 156.40 E-value: 2.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 1 MAKLSYLEAIRQA-QDLAlQQNKDVFILGEDVGKkggvFGTTQGLQQQYGeDRVIDTPLAESNIVGTAIGAAMVGKRPIA 79
Cdd:COG3958 1 MEKKAMRDAFGEAlVELA-EEDPDIVVLDADLGG----STKLDKFAKAFP-DRFFNVGIAEQNMVGVAAGLALAGKIPFV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 80 EiQFADFI-LPATNQIISEAAkmryRSNNdwqcPLTIrapfgGGVHGGL-Y------HsQSIE--SIFASSPGLTIVIPS 149
Cdd:COG3958 75 S-TFAPFLtGRAYEQIRNDIA----YPNL----NVKI-----VGSHAGLsYgedgatH-QALEdiALMRALPNMTVIVPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 150 TPYDAKGLLLSSIESNDPVlYFehkkayRFLKEEVP---EEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAA 226
Cdd:COG3958 140 DAVETEAAVRAAAEHDGPV-YL------RLGRGAVPvvyDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 227 DGINVEVVDLRTVYPLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHClfdlDTPIMRLAAPDVpsmpFSPV- 305
Cdd:COG3958 213 EGISARVINMHTIKPLDEEAILKAARKTGAVVTAEEHSIIGGLGSAVAEVLAENY----PVPLRRIGVPDR----FGESg 284
|
330 340
....*....|....*....|...
gi 593418481 306 ----LENEIMMNPEKILNKMREL 324
Cdd:COG3958 285 speeLLEKYGLDAEGIVAAAKEL 307
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
2-178 |
1.81e-43 |
|
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: 147.31 E-value: 1.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 2 AKLSYLEAIRQAQDLALQQNKDVFILGEDVGkkGGVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVG-KRPIAE 80
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 81 IQFADFILPATNQIISEAAKMRYRSNndwqcPLTIRAPFGGGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLS 160
Cdd:pfam02779 79 ATFSDFLNRADDAIRHGAALGKLPVP-----FVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRA 153
|
170 180
....*....|....*....|
gi 593418481 161 SIESND--PVLYFEHKKAYR 178
Cdd:pfam02779 154 AIRRDGrkPVVLRLPRQLLR 173
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
54-178 |
3.68e-39 |
|
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: 134.92 E-value: 3.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 54 IDTPLAESNIVGTAIGAAMVGKRPIAEIQFADFILpatnqiiseaAKMRYRSNNDWQ-CPLTIRAPFGGGVH--GGLYHS 130
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDR----------AKDQIRSAGASGnVPVVFRHDGGGGVGedGPTHHS 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 593418481 131 QSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDP-VLYFEHKKAYR 178
Cdd:smart00861 88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
141-326 |
8.11e-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: 110.49 E-value: 8.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 141 PGLTIVIPSTPYDAKGLLLSSIESNDPVlyfehkkAYRF-----LKEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVN 215
Cdd:COG1154 442 PNMVIMAPKDENELRHMLYTALAYDGPT-------AIRYprgngPGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVA 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 216 YCLQAADILAADGINVEVVDLRTVYPLDKETIIDRAKNTGKVLLVtEDN-LEGSIMSEVSAIIAEHclfDLDTPIMRLAA 294
Cdd:COG1154 515 EALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTV-EEGvLAGGFGSAVLEFLADA---GLDVPVLRLGL 590
|
170 180 190
....*....|....*....|....*....|....*..
gi 593418481 295 PDVpsmpFSP-----VLENEIMMNPEKILNKMRELAE 326
Cdd:COG1154 591 PDR----FIEhgsraELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
44-324 |
6.72e-24 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 102.08 E-value: 6.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 44 LQQQYGeDRVIDTPLAESNIVGTAIGAAMVGKRPIAEIqFADFILPATNQIISEAAKMRyrsnndwqCPLTI---RApfg 120
Cdd:PRK05444 315 FSKRFP-DRYFDVGIAEQHAVTFAAGLATEGLKPVVAI-YSTFLQRAYDQVIHDVALQN--------LPVTFaidRA--- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 121 GGV------HGGLYhsqSIeSIFASSPGLTIVIPSTPYDAKGLLLSSIESND-PVlyfehkkAYRFLKEEVP----EEYY 189
Cdd:PRK05444 382 GLVgadgptHQGAF---DL-SYLRCIPNMVIMAPSDENELRQMLYTALAYDDgPI-------AIRYPRGNGVgvelPELE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 190 TVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAAdginVEVVDLRTVYPLDKETIIDRAKNTGKVLLVtEDN-LEGS 268
Cdd:PRK05444 451 PLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAKHDLVVTV-EEGaIMGG 525
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 593418481 269 IMSEVSAIIAEHclfDLDTPIMRLAAPDVpsmpFSP-----VLENEIMMNPEKILNKMREL 324
Cdd:PRK05444 526 FGSAVLEFLADH---GLDVPVLNLGLPDE----FIDhgsreELLAELGLDAEGIARRILEL 579
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
39-296 |
1.65e-22 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 98.26 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 39 GTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAEIqFADFILPATNQIISEAAKMRyrsnndwqCPLTI--- 115
Cdd:PRK12571 349 GTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAV-YSTFLQRGYDQLLHDVALQN--------LPVRFvld 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 116 RAPF---GGGVHGGLYHSqsieSIFASSPGLTIVIPSTPYDAKGLLLSSIESND-PVlyfehkkAYRFLK-----EEVPE 186
Cdd:PRK12571 420 RAGLvgaDGATHAGAFDL----AFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDgPI-------AVRFPRgegvgVEIPA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 187 EYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVYPLDkETIIDRAKNTGKVLLVTEDNLE 266
Cdd:PRK12571 489 EGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLD-EALTDLLVRHHIVVIVEEQGAM 567
|
250 260 270
....*....|....*....|....*....|
gi 593418481 267 GSIMSEVSAIIAEHCLFDLDTPIMRLAAPD 296
Cdd:PRK12571 568 GGFGAHVLHHLADTGLLDGGLKLRTLGLPD 597
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
2-296 |
7.23e-14 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 72.24 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 2 AKLSYLEAIRQAQDLALQQNKDVFILGEDVGKkggvfGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAEI 81
Cdd:PLN02582 354 KTQSYTTYFAEALIAEAEVDKDVVAIHAAMGG-----GTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 82 qFADFILPATNQIISEA--AKMRYRSNNDwqcpltiRAPFGGGvhGGLYHSQSIESIF-ASSPGLTIVIPSTPYDAKGLL 158
Cdd:PLN02582 429 -YSSFLQRGYDQVVHDVdlQKLPVRFAMD-------RAGLVGA--DGPTHCGAFDVTYmACLPNMVVMAPSDEAELFHMV 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 159 LSSIESNDPVLYFEHKKAyRFLKEEVPEEYYTVPL--GKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDL 236
Cdd:PLN02582 499 ATAAAIDDRPSCFRYPRG-NGIGVQLPPNNKGIPIevGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADA 577
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 237 RTVYPLDKETIIDRAKNTgKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDTPIMRLAAPD 296
Cdd:PLN02582 578 RFCKPLDRALIRSLAKSH-EVLITVEEGSIGGFGSHVAQFMALDGLLDGKLKWRPLVLPD 636
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
14-168 |
6.21e-13 |
|
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: 65.54 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 14 QDLAlQQNKDVFILGEDVGKKGGvfgtTQGLQQQYGeDRVIDTPLAESNIVGTAIGAAMVGKRPIAEIqFADFILPATNQ 93
Cdd:cd07033 8 LELA-KKDPRIVALSADLGGSTG----LDKFAKKFP-DRFIDVGIAEQNMVGIAAGLALHGLKPFVST-FSFFLQRAYDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 94 IISEAAKMRYrsnndwqcPLTIRapfggGVHGGLY-------HsQSIE--SIFASSPGLTIVIPSTPYDAKGLLLSSIES 164
Cdd:cd07033 81 IRHDVALQNL--------PVKFV-----GTHAGISvgedgptH-QGIEdiALLRAIPNMTVLRPADANETAAALEAALEY 146
|
....
gi 593418481 165 NDPV 168
Cdd:cd07033 147 DGPV 150
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
46-296 |
1.35e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 65.51 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 46 QQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAEIQFAdFILPATNQIISEAAKMRYRSNndwqcpLTIRAPFGGGVHG 125
Cdd:PLN02225 418 QERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSA-FLQRAYDQVVHDVDRQRKAVR------FVITSAGLVGSDG 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 126 GLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESND-PVlyfehkkAYRFLKEEVPEEYYTVP------LGKADV 198
Cdd:PLN02225 491 PVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDrPV-------CFRFPRGSIVNMNYLVPtglpieIGRGRV 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 199 KREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVYPLDKETIIDRAKNTgKVLLVTEDNLEGSIMSEVSAIIA 278
Cdd:PLN02225 564 LVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNH-KFLITVEEGCVGGFGSHVAQFIA 642
|
250
....*....|....*...
gi 593418481 279 EHCLFDLDTPIMRLAAPD 296
Cdd:PLN02225 643 LDGQLDGNIKWRPIVLPD 660
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
5-284 |
3.75e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 63.96 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 5 SYLEAIRQAQDLALQQNKDVFILGEDVGKkggvfGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAEIqFA 84
Cdd:PLN02234 358 SYTSCFVEALIAEAEADKDIVAIHAAMGG-----GTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTI-YS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 85 DFILPATNQIISEA--AKMRYRSNNDwqcpltiRAPFGGGvhGGLYHSQSIESIF-ASSPGLTIVIPSTPYDAKGLLLSS 161
Cdd:PLN02234 432 SFMQRAYDQVVHDVdlQKLPVRFAID-------RAGLMGA--DGPTHCGAFDVTFmACLPNMIVMAPSDEAELFNMVATA 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 162 IESNDPVLYFEHKKAyRFLKEEVPEEYYTVPL--GKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTV 239
Cdd:PLN02234 503 AAIDDRPSCFRYHRG-NGIGVSLPPGNKGVPLqiGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFC 581
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 593418481 240 YPLDKETIIDRAKnTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFD 284
Cdd:PLN02234 582 KPLDVALIRSLAK-SHEVLITVEEGSIGGFGSHVVQFLALDGLLD 625
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
36-172 |
3.40e-07 |
|
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: 49.27 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 36 GVFGTTQGLQQQYGEDRVIDTPLAESNIVGTAIGAAMVGKRPIAEIQFADFILPATNQIISEAAKmryrsnNDWQCPLTI 115
Cdd:cd06586 20 GDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADAAAE------HLPVVFLIG 93
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 116 RAPFGGGVhGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLL---LSSIESNDPVLYFE 172
Cdd:cd06586 94 ARGISAQA-KQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDhaiRTAYASQGPVVVRL 152
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| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
36-267 |
1.60e-06 |
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1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 49.62 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 36 GVFGTTQgLQQQYGeDRVIDTPLAESNIVGTAIGAAMVGKRPIAeIQFADFILPATNQIISEAAkmryrSNNDwqcPLTI 115
Cdd:PRK12315 307 GVFGLKE-FRKKYP-DQYVDVGIAEQESVAFASGIAANGARPVI-FVNSTFLQRAYDQLSHDLA-----INNN---PAVM 375
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 116 rAPFGGGV------HGGLYHSQSIESIfassPGLTIVIPSTPYDAKGLLLSSIESND-------PVLYFEHkkayrflKE 182
Cdd:PRK12315 376 -IVFGGSIsgndvtHLGIFDIPMISNI----PNLVYLAPTTKEELIAMLEWALTQHEhpvairvPEHGVES-------GP 443
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 183 EVPEEYYTVplgKADVKREGEDLTVFCYGLMVNYCLQAADILAAD-GINVEVVDLRTVYPLDKETiIDRAKNTGKVLLVT 261
Cdd:PRK12315 444 TVDTDYSTL---KYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVVTL 519
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....*..
gi 593418481 262 EDN-LEG 267
Cdd:PRK12315 520 EDGiLDG 526
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| PRK05899 |
PRK05899 |
transketolase; Reviewed |
131-245 |
1.65e-06 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 49.36 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 131 QSIESIFA--SSPGLTIVIPSTPYDAKGLLLSSIESND-P-VLYFEhKKAYRFLKEEVPEEyyTVPLGKADVkREGEDLT 206
Cdd:PRK05899 401 QPVEQLASlrAIPNLTVIRPADANETAAAWKYALERKDgPsALVLT-RQNLPVLERTAQEE--GVAKGGYVL-RDDPDVI 476
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90 100 110
....*....|....*....|....*....|....*....
gi 593418481 207 VFCYGLMVNYCLQAADILAADGINVEVVDLRTVYPLDKE 245
Cdd:PRK05899 477 LIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ 515
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| PRK08659 |
PRK08659 |
2-oxoacid:acceptor oxidoreductase subunit alpha; |
186-325 |
1.52e-04 |
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2-oxoacid:acceptor oxidoreductase subunit alpha;
Pssm-ID: 181526 [Multi-domain] Cd Length: 376 Bit Score: 42.93 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 186 EEYYTvplgkadvkrEGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVYPLDKETIIDRAKNTgKVLLVTEDNL 265
Cdd:PRK08659 267 EEYML----------EDAEVVVVAYGSVARSARRAVKEAREEGIKVGLFRLITVWPFPEEAIRELAKKV-KAIVVPEMNL 335
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 593418481 266 eGSIMSEVsaiiaehclfdldtpiMRLAAPDVPSMPFSPVleNEIMMNPEKILNKMRELA 325
Cdd:PRK08659 336 -GQMSLEV----------------ERVVNGRAKVEGINKI--GGELITPEEILEKIKEVA 376
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