|
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: 544.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 1 MTKLSYLEAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAE 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 81 IQFADFILPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLS 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 161 SIESNDPVLYFEHKKAYRfLKEEVPEAYYTVPLGKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVY 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYR-LKGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 241 PLDKETIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFDLDAPIMRLAAPDVPsMPFSPVLENEIMMSPEKIQDK 320
Cdd:COG0022 240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTP-IPYAPALEKAYLPSADRIVAA 318
|
....*..
gi 488373650 321 MRELAEF 327
Cdd:COG0022 319 VRELLAY 325
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-324 |
2.17e-146 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 416.30 E-value: 2.17e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 1 MTKLSYLEAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAE 80
Cdd:PTZ00182 32 TVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 81 IQFADFILPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLS 160
Cdd:PTZ00182 112 FMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 161 SIESNDPVLYFEHKKAYRFLKEEVPEAYYTVPLGKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVY 240
Cdd:PTZ00182 192 AIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 241 PLDKETIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFDLDAPIMRLAAPDVPsMPFSPVLENEIMMSPEKIQDK 320
Cdd:PTZ00182 272 PWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTP-FPYAKNLEPAYLPDKEKVVEA 350
|
....
gi 488373650 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 |
2.39e-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: 287.07 E-value: 2.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 8 EAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAEIQFADFI 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 88 LPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLSSIESNDP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 488373650 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 |
1.57e-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: 156.22 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 194 GKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVYPLDKETIIERASKTGKVLLVTEDNLEGSVMSEV 273
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488373650 274 SAIIAEHCLFDLDAPIMRLAAPDVPsMPFSP-VLENEIMMSPEKI 317
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPDFP-EPGSAdELEKLYGLTPEKI 124
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
54-178 |
1.37e-38 |
|
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: 133.38 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 54 IDTPLAESNIIGTAIGAAMIGKRPIAEIQFADFILpatnqiiseaAKMRYRSNNDWG-CPITIRAPFGGGVH--GGLYHS 130
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDR----------AKDQIRSAGASGnVPVVFRHDGGGGVGedGPTHHS 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488373650 131 QSIESIFASTPGLTIVIPSSPYDAKGLLLSSIESNDP-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: 544.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 1 MTKLSYLEAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAE 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 81 IQFADFILPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLS 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 161 SIESNDPVLYFEHKKAYRfLKEEVPEAYYTVPLGKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVY 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYR-LKGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 241 PLDKETIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFDLDAPIMRLAAPDVPsMPFSPVLENEIMMSPEKIQDK 320
Cdd:COG0022 240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTP-IPYAPALEKAYLPSADRIVAA 318
|
....*..
gi 488373650 321 MRELAEF 327
Cdd:COG0022 319 VRELLAY 325
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-324 |
2.17e-146 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 416.30 E-value: 2.17e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 1 MTKLSYLEAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAE 80
Cdd:PTZ00182 32 TVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 81 IQFADFILPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLS 160
Cdd:PTZ00182 112 FMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 161 SIESNDPVLYFEHKKAYRFLKEEVPEAYYTVPLGKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVY 240
Cdd:PTZ00182 192 AIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 241 PLDKETIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFDLDAPIMRLAAPDVPsMPFSPVLENEIMMSPEKIQDK 320
Cdd:PTZ00182 272 PWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTP-FPYAKNLEPAYLPDKEKVVEA 350
|
....
gi 488373650 321 MREL 324
Cdd:PTZ00182 351 AKRV 354
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
1-326 |
1.37e-107 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 316.66 E-value: 1.37e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 1 MTKLSYLEAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAE 80
Cdd:PRK09212 1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 81 IQFADFILPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLS 160
Cdd:PRK09212 81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 161 SIESNDPVLYFEHKKAYRfLKEEVPEAYYTVPLGKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVY 240
Cdd:PRK09212 161 AIRDPNPVIFLENEILYG-HSHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 241 PLDKETIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFDLDAPIMRLAAPDVPsMPFSPVLENEIMMSPEKIQDK 320
Cdd:PRK09212 240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVP-LPYAANLEKLALPSEEDIIEA 318
|
....*.
gi 488373650 321 MRELAE 326
Cdd:PRK09212 319 VKKVCY 324
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
1-324 |
2.91e-100 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 298.19 E-value: 2.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 1 MTKLSYLEAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAE 80
Cdd:CHL00144 1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 81 IQFADFILPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLS 160
Cdd:CHL00144 81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 161 SIESNDPVLYFEHKKAYRfLKEEVPEAYYTVPLGKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVY 240
Cdd:CHL00144 161 AIRSNNPVIFFEHVLLYN-LKEEIPDNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 241 PLDKETIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFDLDAPIMRLAAPDVPSmPFSPVLENEIMMSPEKIQDK 320
Cdd:CHL00144 240 PLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPT-PYNGPLEEATVIQPAQIIEA 318
|
....
gi 488373650 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 |
2.39e-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: 287.07 E-value: 2.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 8 EAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAEIQFADFI 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 88 LPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLSSIESNDP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 488373650 168 VLYFEHK 174
Cdd:cd07036 161 VIFLEHK 167
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
8-322 |
7.38e-87 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 265.14 E-value: 7.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 8 EAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAEIQFADFI 87
Cdd:PLN02683 31 DALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTFNFS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 88 LPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLSSIESNDP 167
Cdd:PLN02683 111 MQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLKAAIRDPDP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 168 VLYFEHKKAY--RF-LKEEVPEAYYTVPLGKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVYPLDK 244
Cdd:PLN02683 191 VVFLENELLYgeSFpVSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDR 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488373650 245 ETIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFDLDAPIMRLAAPDVPsMPFSPVLENeimMSPEKIQDKMR 322
Cdd:PLN02683 271 DTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVP-MPYAANLER---LALPQVEDIVR 344
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-317 |
8.69e-87 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 268.32 E-value: 8.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 1 MTKLSYLEAIRQAHDLALEKDKNTFILGEDVGKKGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAE 80
Cdd:PRK11892 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 81 IQFADFILPATNQIISEAAKMRYRSNNDWGCPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLS 160
Cdd:PRK11892 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 161 SIESNDPVLYFEHKKAY--RFlkeEVPEAY-YTVPLGKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLR 237
Cdd:PRK11892 299 AIRDPNPVIFLENEILYgqSF---DVPKLDdFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 238 TVYPLDKETIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFDLDAPIMRLAAPDVPsMPFSPVLENEIMMSPEKI 317
Cdd:PRK11892 376 TIRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVP-MPYAANLEKLALPSVAEV 454
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
194-317 |
1.57e-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: 156.22 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 194 GKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVYPLDKETIIERASKTGKVLLVTEDNLEGSVMSEV 273
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488373650 274 SAIIAEHCLFDLDAPIMRLAAPDVPsMPFSP-VLENEIMMSPEKI 317
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPDFP-EPGSAdELEKLYGLTPEKI 124
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
3-178 |
1.27e-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: 147.70 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 3 KLSYLEAIRQAHDLALEKDKNTFILGEDVGkkGGVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIG-KRPIAEI 81
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 82 QFADFILPATNQIISEAAKMRYRSNndwgcPITIRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLLLSS 161
Cdd:pfam02779 80 TFSDFLNRADDAIRHGAALGKLPVP-----FVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAA 154
|
170
....*....|....*....
gi 488373650 162 IESND--PVLYFEHKKAYR 178
Cdd:pfam02779 155 IRRDGrkPVVLRLPRQLLR 173
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
54-178 |
1.37e-38 |
|
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: 133.38 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 54 IDTPLAESNIIGTAIGAAMIGKRPIAEIQFADFILpatnqiiseaAKMRYRSNNDWG-CPITIRAPFGGGVH--GGLYHS 130
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDR----------AKDQIRSAGASGnVPVVFRHDGGGGVGedGPTHHS 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488373650 131 QSIESIFASTPGLTIVIPSSPYDAKGLLLSSIESNDP-VLYFEHKKAYR 178
Cdd:smart00861 88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
141-296 |
1.84e-26 |
|
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: 109.72 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 141 PGLTIVIPSSPYDAKGLLLSSIESNDPVlyfehkkAYRF-----LKEEVPEAYYTVPLGKADVKRQGDDITVFCYGLMVN 215
Cdd:COG1154 442 PNMVIMAPKDENELRHMLYTALAYDGPT-------AIRYprgngPGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVA 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 216 YCLQAADILAEDGINVEVVDLRTVYPLDKETIIERASKTGKVLLVtEDN-LEGSVMSEVSAIIAEHclfDLDAPIMRLAA 294
Cdd:COG1154 515 EALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTV-EEGvLAGGFGSAVLEFLADA---GLDVPVLRLGL 590
|
..
gi 488373650 295 PD 296
Cdd:COG1154 591 PD 592
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
51-324 |
1.78e-24 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 103.62 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 51 ERVIDTPLAESNIIGTAIGAAMIGKRPIAEIqFADFILPATNQIISEAAKMRyrsnndwgCPITI---RApfgGGV---- 123
Cdd:PRK05444 321 DRYFDVGIAEQHAVTFAAGLATEGLKPVVAI-YSTFLQRAYDQVIHDVALQN--------LPVTFaidRA---GLVgadg 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 124 --HGGLYhsqSIeSIFASTPGLTIVIPSSPYDAKGLLLSSIESND-PVlyfehkkAYRFLKEEVP----EAYYTVPLGKA 196
Cdd:PRK05444 389 ptHQGAF---DL-SYLRCIPNMVIMAPSDENELRQMLYTALAYDDgPI-------AIRYPRGNGVgvelPELEPLPIGKG 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 197 DVKRQGDDITVFCYGLMVNYCLQAADILAEdginVEVVDLRTVYPLDKETIIERASKTGKVLLVtEDN-LEGSVMSEVSA 275
Cdd:PRK05444 458 EVLREGEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAKHDLVVTV-EEGaIMGGFGSAVLE 532
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488373650 276 IIAEHclfDLDAPIMRLAAPDVpsmpFSP-----VLENEIMMSPEKIQDKMREL 324
Cdd:PRK05444 533 FLADH---GLDVPVLNLGLPDE----FIDhgsreELLAELGLDAEGIARRILEL 579
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
46-296 |
9.96e-20 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 89.78 E-value: 9.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 46 SKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAEIqFADFILPATNQIISEAAKMRyrsnndwgCPITI---RAPF--- 119
Cdd:PRK12571 356 QKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAV-YSTFLQRGYDQLLHDVALQN--------LPVRFvldRAGLvga 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 120 GGGVHGGLYHSqsieSIFASTPGLTIVIPSSPYDAKGLLLSSIESND-PVlyfehkkAYRFLK-----EEVPEAYYTVPL 193
Cdd:PRK12571 427 DGATHAGAFDL----AFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDgPI-------AVRFPRgegvgVEIPAEGTILGI 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 194 GKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVYPLDkETIIERASKTGKVLLVTEDNLEGSVMSEV 273
Cdd:PRK12571 496 GKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLD-EALTDLLVRHHIVVIVEEQGAMGGFGAHV 574
|
250 260
....*....|....*....|...
gi 488373650 274 SAIIAEHCLFDLDAPIMRLAAPD 296
Cdd:PRK12571 575 LHHLADTGLLDGGLKLRTLGLPD 597
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
51-296 |
3.31e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 70.31 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 51 ERVIDTPLAESNIIGTAIGAAMIGKRPIAEIqFADFILPATNQIISEA--AKMRYRSNNDwgcpitiRAPFGGGvhGGLY 128
Cdd:PLN02582 398 TRCFDVGIAEQHAVTFAAGLACEGLKPFCAI-YSSFLQRGYDQVVHDVdlQKLPVRFAMD-------RAGLVGA--DGPT 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 129 HSQSIESIF-ASTPGLTIVIPSSPYDAKGLLLSSIESNDPVLYFEHKKAyRFLKEEVPEAYYTVPL--GKADVKRQGDDI 205
Cdd:PLN02582 468 HCGAFDVTYmACLPNMVVMAPSDEAELFHMVATAAAIDDRPSCFRYPRG-NGIGVQLPPNNKGIPIevGKGRILLEGERV 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 206 TVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVYPLDKeTIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFDL 285
Cdd:PLN02582 547 ALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDR-ALIRSLAKSHEVLITVEEGSIGGFGSHVAQFMALDGLLDG 625
|
250
....*....|.
gi 488373650 286 DAPIMRLAAPD 296
Cdd:PLN02582 626 KLKWRPLVLPD 636
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
8-168 |
6.15e-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: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 8 EAIRQAHDLALEKDKNTFILGEDVGKKGGvfgvTQGLQSKYGiERVIDTPLAESNIIGTAIGAAMIGKRPIAEIqFADFI 87
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTG----LDKFAKKFP-DRFIDVGIAEQNMVGIAAGLALHGLKPFVST-FSFFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 88 LPATNQIISEAAKMRYrsnndwgcPITIRapfggGVHGGLY-------HsQSIE--SIFASTPGLTIVIPSSPYDAKGLL 158
Cdd:cd07033 75 QRAYDQIRHDVALQNL--------PVKFV-----GTHAGISvgedgptH-QGIEdiALLRAIPNMTVLRPADANETAAAL 140
|
170
....*....|
gi 488373650 159 LSSIESNDPV 168
Cdd:cd07033 141 EAALEYDGPV 150
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
5-284 |
1.66e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 65.12 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 5 SYLEAIRQAHDLALEKDKNTFILGEDVGkkGGVfgVTQGLQSKYGIeRVIDTPLAESNIIGTAIGAAMIGKRPIAEIqFA 84
Cdd:PLN02234 358 SYTSCFVEALIAEAEADKDIVAIHAAMG--GGT--MLNLFESRFPT-RCFDVGIAEQHAVTFAAGLACEGLKPFCTI-YS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 85 DFILPATNQIISEA--AKMRYRSNNDwgcpitiRAPFGGGvhGGLYHSQSIESIF-ASTPGLTIVIPSSPYDAKGLLLSS 161
Cdd:PLN02234 432 SFMQRAYDQVVHDVdlQKLPVRFAID-------RAGLMGA--DGPTHCGAFDVTFmACLPNMIVMAPSDEAELFNMVATA 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 162 IESNDPVLYFEHKKAyRFLKEEVPEAYYTVPL--GKADVKRQGDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTV 239
Cdd:PLN02234 503 AAIDDRPSCFRYHRG-NGIGVSLPPGNKGVPLqiGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFC 581
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 488373650 240 YPLDKeTIIERASKTGKVLLVTEDNLEGSVMSEVSAIIAEHCLFD 284
Cdd:PLN02234 582 KPLDV-ALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLD 625
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
51-278 |
3.34e-09 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 57.80 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 51 ERVIDTPLAESNIIGTAIGAAMIGKRPIAEIQFAdFILPATNQIISEAAKMRYRSNndwgCPITIRAPFG--GGVHGGLY 128
Cdd:PLN02225 423 DRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSA-FLQRAYDQVVHDVDRQRKAVR----FVITSAGLVGsdGPVQCGAF 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 129 HSqsieSIFASTPGLTIVIPSSPYDAKGLLLSSIESND-PVlyfehkkAYRFLKEEVPEAYYTVP------LGKADVKRQ 201
Cdd:PLN02225 498 DI----AFMSSLPNMIAMAPADEDELVNMVATAAYVTDrPV-------CFRFPRGSIVNMNYLVPtglpieIGRGRVLVE 566
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488373650 202 GDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVYPLDKEtIIERASKTGKVLLVTEDNLEGSVMSEVSAIIA 278
Cdd:PLN02225 567 GQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIK-LVRDLCQNHKFLITVEEGCVGGFGSHVAQFIA 642
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
36-172 |
2.60e-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: 49.65 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 36 GVFGVTQGLQSKYGIERVIDTPLAESNIIGTAIGAAMIGKRPIAEIQFADFILPATNQIISEAAKmryrsnndwGCPIT- 114
Cdd:cd06586 20 GDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADAAAE---------HLPVVf 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488373650 115 -IRAPFGGGVHGGLYHSQSIESIFASTPGLTIVIPSSPYDAKGLL---LSSIESNDPVLYFE 172
Cdd:cd06586 91 lIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDhaiRTAYASQGPVVVRL 152
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
131-245 |
3.67e-07 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 51.67 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 131 QSIESIFA--STPGLTIVIPSSPYDAKGLLLSSIESND------------PVLYFEHKKAyrflkeevpeayyTVPLGKA 196
Cdd:PRK05899 401 QPVEQLASlrAIPNLTVIRPADANETAAAWKYALERKDgpsalvltrqnlPVLERTAQEE-------------GVAKGGY 467
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488373650 197 DVKRQgDDITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVYPLDKE 245
Cdd:PRK05899 468 VLRDD-PDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ 515
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
36-267 |
9.09e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 47.31 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 36 GVFGVTQgLQSKYGiERVIDTPLAESNIIGTAIGAAMIGKRPIAeIQFADFILPATNQIISEAAkmryrSNNDwgcPITI 115
Cdd:PRK12315 307 GVFGLKE-FRKKYP-DQYVDVGIAEQESVAFASGIAANGARPVI-FVNSTFLQRAYDQLSHDLA-----INNN---PAVM 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 116 rAPFGGGV------HGGLYHSQSIESIfastPGLTIVIPSSPYDAKGLLLSSIESND-------PVLYFEHkkayrflKE 182
Cdd:PRK12315 376 -IVFGGSIsgndvtHLGIFDIPMISNI----PNLVYLAPTTKEELIAMLEWALTQHEhpvairvPEHGVES-------GP 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 183 EVPEAYYTVplgKADVKRQGDDITVFCYGLMVNYCLQAADILAED-GINVEVVDLRTVYPLDKETiIERASKTGKVLLVT 261
Cdd:PRK12315 444 TVDTDYSTL---KYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVVTL 519
|
....*..
gi 488373650 262 EDN-LEG 267
Cdd:PRK12315 520 EDGiLDG 526
|
|
| PRK08659 |
PRK08659 |
2-oxoacid:acceptor oxidoreductase subunit alpha; |
204-273 |
2.85e-04 |
|
2-oxoacid:acceptor oxidoreductase subunit alpha;
Pssm-ID: 181526 [Multi-domain] Cd Length: 376 Bit Score: 42.15 E-value: 2.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 204 DITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVYPLDkETIIERASKTGKVLLVTEDNLeGSVMSEV 273
Cdd:PRK08659 275 EVVVVAYGSVARSARRAVKEAREEGIKVGLFRLITVWPFP-EEAIRELAKKVKAIVVPEMNL-GQMSLEV 342
|
|
| PFOR_II |
pfam17147 |
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ... |
204-294 |
1.74e-03 |
|
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic enzyme pyruvate:ferredoxin oxidoreductase and is necessary for inter subunit contacts in conjunction with domains I and IV.
Pssm-ID: 407280 [Multi-domain] Cd Length: 102 Bit Score: 37.24 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488373650 204 DITVFCYGLMVNYCLQAADILAEDGINVEVVDLRTVYPLDKETIIERASKTgKVLLVTEDN----LEGSVMSEVSAiiae 279
Cdd:pfam17147 2 EVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPEEELKELLAGV-KKVVVLDRNisfgSPGQLGTEVKA---- 76
|
90
....*....|....*
gi 488373650 280 hCLFDLDAPIMRLAA 294
Cdd:pfam17147 77 -ALYDSDPPVVNFIA 90
|
|
| |
