|
Name |
Accession |
Description |
Interval |
E-value |
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
1-322 |
0e+00 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 616.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 1 MAETLLFNALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVE 80
Cdd:CHL00144 1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 81 GMNMGFLLLAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKA 160
Cdd:CHL00144 81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 161 AIRDNNPVLFFEHVLLYNLSEDIPEGDYICALDQAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKP 240
Cdd:CHL00144 161 AIRSNNPVIFFEHVLLYNLKEEIPDNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 241 FDLDTITRSIRKTHKVLVVEECMKTGGIGAELLALITENCFDDLDARPVRLSSQDIPTPYNGNLENLTIIQPHQIVEAAR 320
Cdd:CHL00144 241 LDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAVE 320
|
..
gi 1673828940 321 QI 322
Cdd:CHL00144 321 QI 322
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-324 |
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: 509.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 1 MAETLLFNALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVE 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 81 GMNMGFLLLAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKA 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 161 AIRDNNPVLFFEHVLLYNLSEDIPEGDYICALDQAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKP 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYRLKGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 241 FDLDTITRSIRKTHKVLVVEECMKTGGIGAELLALITENCFDDLDARPVRLSSQDIPTPYNGNLENLTIIQPHQIVEAAR 320
Cdd:COG0022 241 LDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAVR 320
|
....
gi 1673828940 321 QITA 324
Cdd:COG0022 321 ELLA 324
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
9-174 |
2.53e-102 |
|
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: 297.47 E-value: 2.53e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 9 ALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVEGMNMGFLL 88
Cdd:cd07036 2 AINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 89 LAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKAAIRDNNPV 168
Cdd:cd07036 82 PAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDPV 161
|
....*.
gi 1673828940 169 LFFEHV 174
Cdd:cd07036 162 IFLEHK 167
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
8-178 |
1.00e-48 |
|
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: 160.79 E-value: 1.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 8 NALREAIDEEMARDPHVCVMGEDVGeyGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTG-LRPIVEGMNMGF 86
Cdd:pfam02779 7 KASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEATFSDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 87 LLLAFNQISNNMgmlrytSGGNFTIPTVV-RGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKAAIR-- 163
Cdd:pfam02779 85 LNRADDAIRHGA------ALGKLPVPFVVtRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRrd 158
|
170
....*....|....*
gi 1673828940 164 DNNPVLFFEHVLLYN 178
Cdd:pfam02779 159 GRKPVVLRLPRQLLR 173
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
54-178 |
9.99e-30 |
|
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: 110.27 E-value: 9.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 54 LDTPIAENSFTGMAVGAAMTGLRPIVEGMNMgFLLLAFNQISNNMGMLRytsggnftIPTVVR-GPGGVGRQLGAEH-SQ 131
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFT-FFDRAKDQIRSAGASGN--------VPVVFRhDGGGGVGEDGPTHhSI 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1673828940 132 RLEAYFHAVPGIKIVAVSTPTNAKGLMKAAIRDNNP-VLFFEHVLLYN 178
Cdd:smart00861 89 EDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
1-322 |
0e+00 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 616.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 1 MAETLLFNALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVE 80
Cdd:CHL00144 1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 81 GMNMGFLLLAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKA 160
Cdd:CHL00144 81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 161 AIRDNNPVLFFEHVLLYNLSEDIPEGDYICALDQAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKP 240
Cdd:CHL00144 161 AIRSNNPVIFFEHVLLYNLKEEIPDNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 241 FDLDTITRSIRKTHKVLVVEECMKTGGIGAELLALITENCFDDLDARPVRLSSQDIPTPYNGNLENLTIIQPHQIVEAAR 320
Cdd:CHL00144 241 LDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAVE 320
|
..
gi 1673828940 321 QI 322
Cdd:CHL00144 321 QI 322
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-324 |
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: 509.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 1 MAETLLFNALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVE 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 81 GMNMGFLLLAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKA 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 161 AIRDNNPVLFFEHVLLYNLSEDIPEGDYICALDQAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKP 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYRLKGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 241 FDLDTITRSIRKTHKVLVVEECMKTGGIGAELLALITENCFDDLDARPVRLSSQDIPTPYNGNLENLTIIQPHQIVEAAR 320
Cdd:COG0022 241 LDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAAVR 320
|
....
gi 1673828940 321 QITA 324
Cdd:COG0022 321 ELLA 324
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
6-323 |
3.55e-174 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 486.80 E-value: 3.55e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 6 LFNALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVEGMNMG 85
Cdd:PTZ00182 37 VREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFAD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 86 FLLLAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKAAIRDN 165
Cdd:PTZ00182 117 FIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKAAIRDP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 166 NPVLFFEHVLLYNLSEDI-PEGDYICALDQAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKPFDLD 244
Cdd:PTZ00182 197 NPVVFFEPKLLYRESVEVvPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRE 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1673828940 245 TITRSIRKTHKVLVVEECMKTGGIGAELLALITENCFDDLDARPVRLSSQDIPTPYNGNLENLTIIQPHQIVEAARQIT 323
Cdd:PTZ00182 277 TIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNLEPAYLPDKEKVVEAAKRVL 355
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
1-322 |
3.19e-136 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 389.47 E-value: 3.19e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 1 MAETLLFNALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVE 80
Cdd:PRK09212 1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 81 GMNMGFLLLAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKA 160
Cdd:PRK09212 81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 161 AIRDNNPVLFFEHVLLYNLSEDIPEGDYICALDQAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKP 240
Cdd:PRK09212 161 AIRDPNPVIFLENEILYGHSHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 241 FDLDTITRSIRKTHKVLVVEECMKTGGIGAELLALITENCFDDLDARPVRLSSQDIPTPYNGNLENLTIIQPHQIVEAAR 320
Cdd:PRK09212 241 LDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIEAVK 320
|
..
gi 1673828940 321 QI 322
Cdd:PRK09212 321 KV 322
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-323 |
2.13e-125 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 366.94 E-value: 2.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 1 MAETLLFNALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVE 80
Cdd:PRK11892 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 81 GMNMGFLLLAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKA 160
Cdd:PRK11892 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 161 AIRDNNPVLFFEHVLLYNLSEDIPEG-DYICALDQAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLK 239
Cdd:PRK11892 299 AIRDPNPVIFLENEILYGQSFDVPKLdDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIR 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 240 PFDLDTITRSIRKTHKVLVVEECMKTGGIGAELLALITENCFDDLDARPVRLSSQDIPTPYNGNLENLTIIQPHQIVEAA 319
Cdd:PRK11892 379 PMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAV 458
|
....
gi 1673828940 320 RQIT 323
Cdd:PRK11892 459 KAVC 462
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
8-323 |
1.57e-116 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 340.64 E-value: 1.57e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 8 NALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVEGMNMGFL 87
Cdd:PLN02683 31 DALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTFNFS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 88 LLAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKAAIRDNNP 167
Cdd:PLN02683 111 MQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLKAAIRDPDP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 168 VLFFEHVLLYN----LSEDIPEGDYICALDQAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKPFDL 243
Cdd:PLN02683 191 VVFLENELLYGesfpVSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 244 DTITRSIRKTHKVLVVEECMKTGGIGAELLALITENCFDDLDARPVRLSSQDIPTPYNGNLENLTIIQPHQIVEAARQIT 323
Cdd:PLN02683 271 DTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPYAANLERLALPQVEDIVRAAKRAC 350
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
9-174 |
2.53e-102 |
|
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: 297.47 E-value: 2.53e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 9 ALREAIDEEMARDPHVCVMGEDVGEYGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVEGMNMGFLL 88
Cdd:cd07036 2 AINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 89 LAFNQISNNMGMLRYTSGGNFTIPTVVRGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKAAIRDNNPV 168
Cdd:cd07036 82 PAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDPV 161
|
....*.
gi 1673828940 169 LFFEHV 174
Cdd:cd07036 162 IFLEHK 167
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
8-178 |
1.00e-48 |
|
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: 160.79 E-value: 1.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 8 NALREAIDEEMARDPHVCVMGEDVGeyGGSYKVTKDLHAKYGELRVLDTPIAENSFTGMAVGAAMTG-LRPIVEGMNMGF 86
Cdd:pfam02779 7 KASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEATFSDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 87 LLLAFNQISNNMgmlrytSGGNFTIPTVV-RGPGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKAAIR-- 163
Cdd:pfam02779 85 LNRADDAIRHGA------ALGKLPVPFVVtRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRrd 158
|
170
....*....|....*
gi 1673828940 164 DNNPVLFFEHVLLYN 178
Cdd:pfam02779 159 GRKPVVLRLPRQLLR 173
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
194-315 |
1.90e-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: 155.83 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 194 QAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKPFDLDTITRSIRKTHKVLVVEECMKTGGIGAELL 273
Cdd:pfam02780 2 KAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEVA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1673828940 274 ALITENCFDDLDARPVRLSSQDIPTPYN-GNLENLTIIQPHQI 315
Cdd:pfam02780 82 AALAEEAFDGLDAPVLRVGGPDFPEPGSaDELEKLYGLTPEKI 124
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
8-291 |
3.90e-36 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 132.13 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 8 NALREAIDEEMARDPHVCVMGEDVGEYGGsykvTKDLHAKYGElRVLDTPIAENSFTGMAVGAAMTGLRPIVEGMNMgFL 87
Cdd:COG3958 8 DAFGEALVELAEEDPDIVVLDADLGGSTK----LDKFAKAFPD-RFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAP-FL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 88 -LLAFNQISNNMGmlrYtSGGNFTIptVVRGPG-GVGrQLGAEHsQRLE--AYFHAVPGIKIVAVSTPTNAKGLMKAAIR 163
Cdd:COG3958 82 tGRAYEQIRNDIA---Y-PNLNVKI--VGSHAGlSYG-EDGATH-QALEdiALMRALPNMTVIVPADAVETEAAVRAAAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 164 DNNPVLFFehvLLYNLSEDIPEGDYICALDQAELVREGKDITILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKPFDL 243
Cdd:COG3958 154 HDGPVYLR---LGRGAVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1673828940 244 DTITRSIRKTHKVLVVEECMKTGGIG---AELLAlitENCfddldarPVRL 291
Cdd:COG3958 231 EAILKAARKTGAVVTAEEHSIIGGLGsavAEVLA---ENY-------PVPL 271
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
54-178 |
9.99e-30 |
|
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: 110.27 E-value: 9.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 54 LDTPIAENSFTGMAVGAAMTGLRPIVEGMNMgFLLLAFNQISNNMGMLRytsggnftIPTVVR-GPGGVGRQLGAEH-SQ 131
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFT-FFDRAKDQIRSAGASGN--------VPVVFRhDGGGGVGEDGPTHhSI 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1673828940 132 RLEAYFHAVPGIKIVAVSTPTNAKGLMKAAIRDNNP-VLFFEHVLLYN 178
Cdd:smart00861 89 EDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPvVIRLERKSLYR 136
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
8-168 |
1.89e-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: 75.17 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 8 NALREAIDEEMARDPHVCVMGEDVGEYGGsykvTKDLHAKYGElRVLDTPIAENSFTGMAVGAAMTGLRPIVEGMNMgFL 87
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTG----LDKFAKKFPD-RFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSF-FL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 88 LLAFNQISNNMGMlrytSGGNFTIptVVRGPGGVGRQLGAEHsQRLE--AYFHAVPGIKIVAVSTPTNAKGLMKAAIRDN 165
Cdd:cd07033 75 QRAYDQIRHDVAL----QNLPVKF--VGTHAGISVGEDGPTH-QGIEdiALLRAIPNMTVLRPADANETAAALEAALEYD 147
|
...
gi 1673828940 166 NPV 168
Cdd:cd07033 148 GPV 150
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
52-273 |
4.39e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 79.00 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 52 RVLDTPIAENSFTGMAVGAAMTGLRPIVeGMNMGFLLLAFNQISNNMGMLRytsggnftIP-TVVRGPGGVGRQLGAEHS 130
Cdd:PRK12571 362 RVFDVGIAEQHAVTFAAGLAAAGLKPFC-AVYSTFLQRGYDQLLHDVALQN--------LPvRFVLDRAGLVGADGATHA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 131 QRLE-AYFHAVPGIKIVAVS-TPTNAKGLMKAAIRDNNPVlffehVLLYNLSE----DIPEGDYICALDQAELVREGKDI 204
Cdd:PRK12571 433 GAFDlAFLTNLPNMTVMAPRdEAELRHMLRTAAAHDDGPI-----AVRFPRGEgvgvEIPAEGTILGIGKGRVPREGPDV 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1673828940 205 TILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKPFDlDTITRSIRKTHKVLVVEECMKTGGIGAELL 273
Cdd:PRK12571 508 AILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLD-EALTDLLVRHHIVVIVEEQGAMGGFGAHVL 575
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
135-279 |
6.07e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 75.50 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 135 AYFHAVPGIKIVAvstPTNA---KGLMKAAIR-DNNPVlffehVLLY----NLSEDIPEGDYIcALDQAELVREGKDITI 206
Cdd:PRK05444 398 SYLRCIPNMVIMA---PSDEnelRQMLYTALAyDDGPI-----AIRYprgnGVGVELPELEPL-PIGKGEVLREGEDVAI 468
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1673828940 207 LTYSRMRHHCLKAVKQLEadgiDVELIDLISLKPFDLDTItRSIRKTHKVLV-VEECMKTGGIGAELLALITEN 279
Cdd:PRK05444 469 LAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELL-LELAAKHDLVVtVEEGAIMGGFGSAVLEFLADH 537
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
52-276 |
2.72e-09 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 58.19 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 52 RVLDTPIAENSFTGMAVGAAMTGLRPIVEgMNMGFLLLAFNQISNNMGMLRytsggnFTIPTVVRGPGGVGRQlGAEHSQ 131
Cdd:PLN02234 400 RCFDVGIAEQHAVTFAAGLACEGLKPFCT-IYSSFMQRAYDQVVHDVDLQK------LPVRFAIDRAGLMGAD-GPTHCG 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 132 RLEAYFHA-VPGIKIVAVSTPTNAKGLM-KAAIRDNNPVLFFEHvLLYNLSEDIPEGDYICALD--QAELVREGKDITIL 207
Cdd:PLN02234 472 AFDVTFMAcLPNMIVMAPSDEAELFNMVaTAAAIDDRPSCFRYH-RGNGIGVSLPPGNKGVPLQigRGRILRDGERVALL 550
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1673828940 208 TYSRMRHHCLKAVKQLEADGIDVELIDLISLKPFDLDTItRSIRKTHKVLVVEECMKTGGIGAELLALI 276
Cdd:PLN02234 551 GYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALI-RSLAKSHEVLITVEEGSIGGFGSHVVQFL 618
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
31-166 |
1.15e-08 |
|
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: 53.50 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 31 VGEYGGSYKVTKDLhAKYGELRVLDTPIAENSFTGMAVGAAMTGLRPIVEGMNMGFLLLAFNQIsnnmgmlrYTSGGNFt 110
Cdd:cd06586 16 FGYPGDEISSLLDA-LREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGL--------ADAAAEH- 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1673828940 111 IPTVVRG--PGGVGRQLGAEHSQRLEAYFHAVPGIKIVAVSTPTNAKGLMKAAIRDNN 166
Cdd:cd06586 86 LPVVFLIgaRGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYA 143
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
52-276 |
7.60e-08 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 53.95 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 52 RVLDTPIAENSFTGMAVGAAMTGLRPIVEgMNMGFLLLAFNQISNNMGMLRYTsggnftIPTVVRGPGGVGRQLGAEHSQ 131
Cdd:PLN02225 424 RFFNVGMAEQHAVTFSAGLSSGGLKPFCI-IPSAFLQRAYDQVVHDVDRQRKA------VRFVITSAGLVGSDGPVQCGA 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 132 RLEAYFHAVPGIKIVAvstPTNAKGLMK----AAIRDNNPVLF-FEHVLLYNLSEDIPEGDYIcALDQAELVREGKDITI 206
Cdd:PLN02225 497 FDIAFMSSLPNMIAMA---PADEDELVNmvatAAYVTDRPVCFrFPRGSIVNMNYLVPTGLPI-EIGRGRVLVEGQDVAL 572
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 207 LTYSRMRHHCLKAVKQLEADGIDVELIDLISLKPFDLdTITRSIRKTHKVLVVEECMKTGGIGAELLALI 276
Cdd:PLN02225 573 LGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDI-KLVRDLCQNHKFLITVEEGCVGGFGSHVAQFI 641
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
52-275 |
1.92e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 52.60 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 52 RVLDTPIAENSFTGMAVGAAMTGLRPIVeGMNMGFLLLAFNQISNNMGMLRytsggnFTIPTVVRGPGGVGRQlGAEHSQ 131
Cdd:PLN02582 399 RCFDVGIAEQHAVTFAAGLACEGLKPFC-AIYSSFLQRGYDQVVHDVDLQK------LPVRFAMDRAGLVGAD-GPTHCG 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 132 RLEAYFHA-VPGIKIVAvstPTNAKGLMK----AAIRDNNPVLFfEHVLLYNLSEDIPEGDYICALD--QAELVREGKDI 204
Cdd:PLN02582 471 AFDVTYMAcLPNMVVMA---PSDEAELFHmvatAAAIDDRPSCF-RYPRGNGIGVQLPPNNKGIPIEvgKGRILLEGERV 546
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1673828940 205 TILTYSRMRHHCLKAVKQLEADGIDVELIDLISLKPFDLDTItRSIRKTHKVLVVEECMKTGGIG---AELLAL 275
Cdd:PLN02582 547 ALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALI-RSLAKSHEVLITVEEGSIGGFGshvAQFMAL 619
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
8-269 |
8.07e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 50.39 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 8 NALREAIDEEMARDPHVCVMGEDV-GEYGgsykvTKDLHAKYGElRVLDTPIAENSFTGMAVGAAMTGLRPIVeGMNMGF 86
Cdd:PRK12315 282 SVTLDYLLKKIKEGKPVVAINAAIpGVFG-----LKEFRKKYPD-QYVDVGIAEQESVAFASGIAANGARPVI-FVNSTF 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 87 LLLAFNQISNNMGMlrytsgGNFTIPTVVRGPGGVGRQLGAEHSQRLeAYFHAVPGIKIVAVSTPTNAKGLMKAAIRDNN 166
Cdd:PRK12315 355 LQRAYDQLSHDLAI------NNNPAVMIVFGGSISGNDVTHLGIFDI-PMISNIPNLVYLAPTTKEELIAMLEWALTQHE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 167 -PVLFfehvllynlseDIPEGDYI-CALDQA-------ELVREGKDITILTYSRMRHHCLKAVKQLEAD-GIDVELIDLI 236
Cdd:PRK12315 428 hPVAI-----------RVPEHGVEsGPTVDTdystlkyEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPK 496
|
250 260 270
....*....|....*....|....*....|....
gi 1673828940 237 SLKPFDLDTITrSIRKTHKVLV-VEECMKTGGIG 269
Cdd:PRK12315 497 FITGLDEELLE-KLKEDHELVVtLEDGILDGGFG 529
|
|
| PRK08659 |
PRK08659 |
2-oxoacid:acceptor oxidoreductase subunit alpha; |
200-322 |
1.63e-03 |
|
2-oxoacid:acceptor oxidoreductase subunit alpha;
Pssm-ID: 181526 [Multi-domain] Cd Length: 376 Bit Score: 39.84 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1673828940 200 EGKDITILTY---SRMrhhCLKAVKQLEADGIDVELIDLISLKPFDLDTITRSIRKTHKVLVVEecMKTGGIGAELLALI 276
Cdd:PRK08659 272 EDAEVVVVAYgsvARS---ARRAVKEAREEGIKVGLFRLITVWPFPEEAIRELAKKVKAIVVPE--MNLGQMSLEVERVV 346
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1673828940 277 TencfddlDARPVRLSSQdiptpYNGnlenlTIIQPHQIVEAARQI 322
Cdd:PRK08659 347 N-------GRAKVEGINK-----IGG-----ELITPEEILEKIKEV 375
|
|
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