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Conserved domains on  [gi|258597825|ref|XP_001348615|]
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pyruvate dehydrogenase E1 component subunit beta [Plasmodium falciparum 3D7]

Protein Classification

alpha-ketoacid dehydrogenase subunit beta( domain architecture ID 11488188)

alpha-ketoacid dehydrogenase subunit beta similar to pyruvate dehydrogenase E1 component subunit beta, 2-oxoisovalerate dehydrogenase subunit beta, and TPP-dependent acetoin dehydrogenase E1 subunit beta

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 58-411 0e+00

3-methyl-2-oxobutanate dehydrogenase; Provisional


:

Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 548.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  58 LNTINGIETISNVENKNILNDTNYINEMKNIKVRRNISEALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFG 137
Cdd:PTZ00182   1 ASSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 138 FSRVLDTPICENAFMGLGIGSAINDLRPIIEGMNLSFLILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEH 217
Cdd:PTZ00182  81 PDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 218 SQRIESYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNPILFIEHVLLYNYEQEIPLLP-YTLPIDKAEVVKNGKDLTVLS 296
Cdd:PTZ00182 161 SQSFEAYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEAdYTLPLGKAKVVREGKDVTIVG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 297 YGITRHLASEAAKELTKFNIDIEVIDLISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAELYTQVIEMFSSYLITKP 376
Cdd:PTZ00182 241 YGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPI 320

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 258597825 377 IRLCTKDIPIAYSNKYEDACIIKKEDIVYMSTYLH 411
Cdd:PTZ00182 321 KRVCGADTPFPYAKNLEPAYLPDKEKVVEAAKRVL 355
 
Name Accession Description Interval E-value
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 58-411 0e+00

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 548.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  58 LNTINGIETISNVENKNILNDTNYINEMKNIKVRRNISEALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFG 137
Cdd:PTZ00182   1 ASSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 138 FSRVLDTPICENAFMGLGIGSAINDLRPIIEGMNLSFLILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEH 217
Cdd:PTZ00182  81 PDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 218 SQRIESYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNPILFIEHVLLYNYEQEIPLLP-YTLPIDKAEVVKNGKDLTVLS 296
Cdd:PTZ00182 161 SQSFEAYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEAdYTLPLGKAKVVREGKDVTIVG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 297 YGITRHLASEAAKELTKFNIDIEVIDLISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAELYTQVIEMFSSYLITKP 376
Cdd:PTZ00182 241 YGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPI 320

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 258597825 377 IRLCTKDIPIAYSNKYEDACIIKKEDIVYMSTYLH 411
Cdd:PTZ00182 321 KRVCGADTPFPYAKNLEPAYLPDKEKVVEAAKRVL 355
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 85-404 2.52e-148

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: 423.66  E-value: 2.52e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  85 MKNIKVRRNISEALHmaiyEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIGSAINDLR 164
Cdd:COG0022    1 MRELTYREAINEALR----EEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 165 PIIEGMNLSFLILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEHSQRIESYLMSIPGIKIVSCSTPFNARG 244
Cdd:COG0022   77 PVVEIQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 245 LLKSAIRDNNPILFIEHVLLYNYEQEIPLLPYTLPIDKAEVVKNGKDLTVLSYGITRHLASEAAKELTKFNIDIEVIDLI 324
Cdd:COG0022  157 LLKAAIRDDDPVIFLEHKRLYRLKGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLR 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 325 SLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAELYTQVIEMFSSYLITKPIRLCTKDIPIAYSNKYEDACIIKKEDIV 404
Cdd:COG0022  237 TLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIV 316
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 96-262 5.53e-94

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: 279.36  E-value: 5.53e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  96 EALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIGSAINDLRPIIEGMNLSFL 175
Cdd:cd07036    1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 176 ILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEHSQRIESYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNP 255
Cdd:cd07036   81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                 ....*..
gi 258597825 256 ILFIEHV 262
Cdd:cd07036  161 VIFLEHK 167
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 95-266 8.77e-44

Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.


Pssm-ID: 460692 [Multi-domain]  Cd Length: 174  Bit Score: 150.39  E-value: 8.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825   95 SEALHMAIYEEMKKDKGVYVLGEDVGlyGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIG-SAINDLRPIIEGMNLS 173
Cdd:pfam02779   6 RKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGmALHGPLLPPVEATFSD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  174 FLILAFNQISNNACMMRYMCdgqfnIPIVIRGPGGIGKQlGPEH-SQRIESYLMSIPGIKIVSCSTPFNARGLLKSAIR- 251
Cdd:pfam02779  84 FLNRADDAIRHGAALGKLPV-----PFVVTRDPIGVGED-GPTHqSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRr 157

                         170
                  ....*....|....*.
gi 258597825  252 -DNNPILFIEHVLLYN 266
Cdd:pfam02779 158 dGRKPVVLRLPRQLLR 173
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 142-266 5.56e-31

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: 115.28  E-value: 5.56e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825   142 LDTPICENAFMGLGIGSAINDLRPIIEGMnLSFLILAFNQISNNACMMrymcdgqfNIPIVIRGPGGIG-KQLGPEH-SQ 219
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQIRSAGASG--------NVPVVFRHDGGGGvGEDGPTHhSI 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 258597825   220 RIESYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNPI-LFIEHVLLYN 266
Cdd:smart00861  89 EDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVvIRLERKSLYR 136
 
Name Accession Description Interval E-value
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 58-411 0e+00

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 548.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  58 LNTINGIETISNVENKNILNDTNYINEMKNIKVRRNISEALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFG 137
Cdd:PTZ00182   1 ASSFSSTLLGSRLPNSFSSASRSSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 138 FSRVLDTPICENAFMGLGIGSAINDLRPIIEGMNLSFLILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEH 217
Cdd:PTZ00182  81 PDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 218 SQRIESYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNPILFIEHVLLYNYEQEIPLLP-YTLPIDKAEVVKNGKDLTVLS 296
Cdd:PTZ00182 161 SQSFEAYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEAdYTLPLGKAKVVREGKDVTIVG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 297 YGITRHLASEAAKELTKFNIDIEVIDLISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAELYTQVIEMFSSYLITKP 376
Cdd:PTZ00182 241 YGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPI 320

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 258597825 377 IRLCTKDIPIAYSNKYEDACIIKKEDIVYMSTYLH 411
Cdd:PTZ00182 321 KRVCGADTPFPYAKNLEPAYLPDKEKVVEAAKRVL 355
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
 96-404 5.36e-153

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 435.71  E-value: 5.36e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  96 EALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIGSAINDLRPIIEGMNLSFL 175
Cdd:CHL00144   8 EALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 176 ILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEHSQRIESYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNP 255
Cdd:CHL00144  88 LLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKSAIRSNNP 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 256 ILFIEHVLLYNYEQEIPLLPYTLPIDKAEVVKNGKDLTVLSYGITRHLASEAAKELTKFNIDIEVIDLISLKPFDMETIE 335
Cdd:CHL00144 168 VIFFEHVLLYNLKEEIPDNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTIS 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 258597825 336 KSLKKTKKCLILDESAGFGGIGAELYTQVIEMFSSYLITKPIRLCTKDIPIAYSNKYEDACIIKKEDIV 404
Cdd:CHL00144 248 KSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQII 316
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
 85-404 2.52e-148

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: 423.66  E-value: 2.52e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  85 MKNIKVRRNISEALHmaiyEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIGSAINDLR 164
Cdd:COG0022    1 MRELTYREAINEALR----EEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 165 PIIEGMNLSFLILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEHSQRIESYLMSIPGIKIVSCSTPFNARG 244
Cdd:COG0022   77 PVVEIQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 245 LLKSAIRDNNPILFIEHVLLYNYEQEIPLLPYTLPIDKAEVVKNGKDLTVLSYGITRHLASEAAKELTKFNIDIEVIDLI 324
Cdd:COG0022  157 LLKAAIRDDDPVIFLEHKRLYRLKGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLR 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 325 SLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAELYTQVIEMFSSYLITKPIRLCTKDIPIAYSNKYEDACIIKKEDIV 404
Cdd:COG0022  237 TLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIV 316
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
 85-404 2.54e-112

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 332.07  E-value: 2.54e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  85 MKNIKVRrnisEALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIGSAINDLR 164
Cdd:PRK09212   1 MAQLTVR----EALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 165 PIIEGMNLSFLILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEHSQRIESYLMSIPGIKIVSCSTPFNARG 244
Cdd:PRK09212  77 PIVEFMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 245 LLKSAIRDNNPILFIEHVLLYNYEQEIPLLPYTLPIDKAEVVKNGKDLTVLSYGITRHLASEAAKELTKFNIDIEVIDLI 324
Cdd:PRK09212 157 LLKTAIRDPNPVIFLENEILYGHSHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLR 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 325 SLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAELYTQVIEMFSSYLITKPIRLCTKDIPIAYSNKYEDACIIKKEDIV 404
Cdd:PRK09212 237 TLRPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDII 316
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 84-404 1.67e-102

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 311.85  E-value: 1.67e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  84 EMKNIKVRrnisEALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIGSAINDL 163
Cdd:PRK11892 138 EMVTMTVR----EALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGL 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 164 RPIIEGMNLSFLILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEHSQRIESYLMSIPGIKIVSCSTPFNAR 243
Cdd:PRK11892 214 KPIVEFMTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAK 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 244 GLLKSAIRDNNPILFIEHVLLYNYEQEIPLLP-YTLPIDKAEVVKNGKDLTVLSYGITRHLASEAAKELTKFNIDIEVID 322
Cdd:PRK11892 294 GLLKAAIRDPNPVIFLENEILYGQSFDVPKLDdFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVID 373

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 323 LISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAELYTQVIEMFSSYLITKPIRLCTKDIPIAYSNKYEDACIIKKED 402
Cdd:PRK11892 374 LRTIRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAE 453


                 ..
gi 258597825 403 IV 404
Cdd:PRK11892 454 VV 455
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 96-262 5.53e-94

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: 279.36  E-value: 5.53e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  96 EALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIGSAINDLRPIIEGMNLSFL 175
Cdd:cd07036    1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 176 ILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEHSQRIESYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNP 255
Cdd:cd07036   81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160


                 ....*..
gi 258597825 256 ILFIEHV 262
Cdd:cd07036  161 VIFLEHK 167
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
 80-404 1.32e-92

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 282.86  E-value: 1.32e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  80 NYINEMKNIKVRrnisEALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIGSA 159
Cdd:PLN02683  19 GYASAAKEMTVR----DALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 160 INDLRPIIEGMNLSFLILAFNQISNNACMMRYMCDGQFNIPIVIRGPGGIGKQLGPEHSQRIESYLMSIPGIKIVSCSTP 239
Cdd:PLN02683  95 YAGLKPVVEFMTFNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSS 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 240 FNARGLLKSAIRDNNPILFIEHVLLYNyeQEIPLLP------YTLPIDKAEVVKNGKDLTVLSYGITRHLASEAAKELTK 313
Cdd:PLN02683 175 EDARGLLKAAIRDPDPVVFLENELLYG--ESFPVSAevldssFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAK 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 314 FNIDIEVIDLISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAELYTQVIEMFSSYLITKPIRLCTKDIPIAYSNKYE 393
Cdd:PLN02683 253 EGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPYAANLE 332

                        330
                 ....*....|.
gi 258597825 394 DACIIKKEDIV 404
Cdd:PLN02683 333 RLALPQVEDIV 343
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 95-266 8.77e-44

Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.


Pssm-ID: 460692 [Multi-domain]  Cd Length: 174  Bit Score: 150.39  E-value: 8.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825   95 SEALHMAIYEEMKKDKGVYVLGEDVGlyGGSYKVTKNLAHFFGFSRVLDTPICENAFMGLGIG-SAINDLRPIIEGMNLS 173
Cdd:pfam02779   6 RKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGmALHGPLLPPVEATFSD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  174 FLILAFNQISNNACMMRYMCdgqfnIPIVIRGPGGIGKQlGPEH-SQRIESYLMSIPGIKIVSCSTPFNARGLLKSAIR- 251
Cdd:pfam02779  84 FLNRADDAIRHGAALGKLPV-----PFVVTRDPIGVGED-GPTHqSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRr 157

                         170
                  ....*....|....*.
gi 258597825  252 -DNNPILFIEHVLLYN 266
Cdd:pfam02779 158 dGRKPVVLRLPRQLLR 173
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 282-389 2.16e-31

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: 116.16  E-value: 2.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  282 KAEVVKNGKDLTVLSYGITRHLASEAAKELTKFNIDIEVIDLISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAELY 361
Cdd:pfam02780   2 KAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEVA 81

                          90       100
                  ....*....|....*....|....*...
gi 258597825  362 TQVIEMFSSYLITKPIRLCTKDIPIAYS 389
Cdd:pfam02780  82 AALAEEAFDGLDAPVLRVGGPDFPEPGS 109
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 142-266 5.56e-31

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: 115.28  E-value: 5.56e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825   142 LDTPICENAFMGLGIGSAINDLRPIIEGMnLSFLILAFNQISNNACMMrymcdgqfNIPIVIRGPGGIG-KQLGPEH-SQ 219
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQIRSAGASG--------NVPVVFRHDGGGGvGEDGPTHhSI 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 258597825   220 RIESYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNPI-LFIEHVLLYN 266
Cdd:smart00861  89 EDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVvIRLERKSLYR 136
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
101-358 5.34e-24

Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 100.93  E-value: 5.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 101 AIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAHffgfsRVLDTPICENAFMGLGIGSAINDLRPIIEGMNlSFLIL-AF 179
Cdd:COG3958   13 ALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPD-----RFFNVGIAEQNMVGVAAGLALAGKIPFVSTFA-PFLTGrAY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 180 NQISNNACmmrYMcdgqfNIPIVIRGPGG---IGKqLGPEHsQRIESY-LM-SIPGIKIVSCSTPFNARGLLKSAI---- 250
Cdd:COG3958   87 EQIRNDIA---YP-----NLNVKIVGSHAglsYGE-DGATH-QALEDIaLMrALPNMTVIVPADAVETEAAVRAAAehdg 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 251 -------RDNNPILfiehvllynYEQEipllpYTLPIDKAEVVKNGKDLTVLSYGITRHLASEAAKELTKFNIDIEVIDL 323
Cdd:COG3958  157 pvylrlgRGAVPVV---------YDED-----YEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINM 222

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 258597825 324 ISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGA 358
Cdd:COG3958  223 HTIKPLDEEAILKAARKTGAVVTAEEHSIIGGLGS 257
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 223-378 8.73e-19

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: 88.53  E-value: 8.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 223 SYLMSIPGIKIvscSTPFNA---RGLLKSAIRDNNPIlfiehVLLY----NYEQEIPLLPYTLPIDKAEVVKNGKDLTVL 295
Cdd:COG1154  436 SYLRCIPNMVI---MAPKDEnelRHMLYTALAYDGPT-----AIRYprgnGPGVELPAELEPLPIGKGEVLREGKDVAIL 507

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 296 SYGITRHLASEAAKELTKFNIDIEVIDLISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAelytQVIEMFSSYLITK 375
Cdd:COG1154  508 AFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVEEGVLAGGFGS----AVLEFLADAGLDV 583


                 ...
gi 258597825 376 PIR 378
Cdd:COG1154  584 PVL 586
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 223-378 1.31e-14

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 75.50  E-value: 1.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 223 SYLMSIPGIKIvscSTPFNA---RGLLKSAIR-DNNPIlfiehVLLY----NYEQEIPLLpYTLPIDKAEVVKNGKDLTV 294
Cdd:PRK05444 398 SYLRCIPNMVI---MAPSDEnelRQMLYTALAyDDGPI-----AIRYprgnGVGVELPEL-EPLPIGKGEVLREGEDVAI 468

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 295 LSYGITRHLASEAAKELTkfniDIEVIDLISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAElytqVIEMFSSYLIT 374
Cdd:PRK05444 469 LAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMGGFGSA----VLEFLADHGLD 540


                 ....
gi 258597825 375 KPIR 378
Cdd:PRK05444 541 VPVL 544
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
 101-256 2.20e-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: 67.47  E-value: 2.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 101 AIYEEMKKDKGVYVLGEDVGlygGSYKVTKNLAHFFGfsRVLDTPICENAFMGLGIGSAINDLRPIIeGMNLSFLILAFN 180
Cdd:cd07033    6 ALLELAKKDPRIVALSADLG---GSTGLDKFAKKFPD--RFIDVGIAEQNMVGIAAGLALHGLKPFV-STFSFFLQRAYD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 181 QISNNACMMrymcdgqfNIPIVIRG-PGGIG-KQLGPEHsQRIE--SYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNPI 256
Cdd:cd07033   80 QIRHDVALQ--------NLPVKFVGtHAGISvGEDGPTH-QGIEdiALLRAIPNMTVLRPADANETAAALEAALEYDGPV 150
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 140-364 4.98e-09

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 58.20  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 140 RVLDTPICENAFMGLGIGSAINDLRPIIeGMNLSFLILAFNQISNNA----CMMRYMCDgqfnipivirgPGGIGKQLGP 215
Cdd:PRK12571 362 RVFDVGIAEQHAVTFAAGLAAAGLKPFC-AVYSTFLQRGYDQLLHDValqnLPVRFVLD-----------RAGLVGADGA 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 216 EHSQRIE-SYLMSIPGIKIVSCSTPFNARGLLKSAI-RDNNPILFiehvllyNYEQ------EIPLLPYTLPIDKAEVVK 287
Cdd:PRK12571 430 THAGAFDlAFLTNLPNMTVMAPRDEAELRHMLRTAAaHDDGPIAV-------RFPRgegvgvEIPAEGTILGIGKGRVPR 502

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258597825 288 NGKDLTVLSYGITRHLASEAAKELTKFNIDIEVIDLISLKPFDMETIEKsLKKTKKCLILDESAGFGGIGAELYTQV 364
Cdd:PRK12571 503 EGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDL-LVRHHIVVIVEEQGAMGGFGAHVLHHL 578
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 84-360 1.84e-07

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 53.18  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  84 EMKNIKVRRNISEALHMAIYEEMKKDKGVYVLGEDVGlyGGSykvTKNLAHFFGFSRVLDTPICENAFMGLGIGSAINDL 163
Cdd:PLN02234 349 QFKNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMG--GGT---MLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGL 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 164 RPIIEgMNLSFLILAFNQISNNACMMRymcdgqFNIPIVIRGPGGIGKQlGPEHSQRIE-SYLMSIPGIKIVSCSTPFNA 242
Cdd:PLN02234 424 KPFCT-IYSSFMQRAYDQVVHDVDLQK------LPVRFAIDRAGLMGAD-GPTHCGAFDvTFMACLPNMIVMAPSDEAEL 495

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 243 RGLLKSAIR-DNNPILFIEH------VLLYNYEQEIPLlpytlPIDKAEVVKNGKDLTVLSYGITRHLASEAAKELTKFN 315
Cdd:PLN02234 496 FNMVATAAAiDDRPSCFRYHrgngigVSLPPGNKGVPL-----QIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERG 570

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 258597825 316 IDIEVIDLISLKPFDMETIeKSLKKTKKCLILDESAGFGGIGAEL 360
Cdd:PLN02234 571 LKITVADARFCKPLDVALI-RSLAKSHEVLITVEEGSIGGFGSHV 614
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 135-354 1.22e-05

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 47.31  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 135 FFGF--------SRVLDTPICENAFMGLGIGSAINDLRPIIeGMNLSFLILAFNQISNNACMMrymcdgqfNIPIVIRGP 206
Cdd:PRK12315 308 VFGLkefrkkypDQYVDVGIAEQESVAFASGIAANGARPVI-FVNSTFLQRAYDQLSHDLAIN--------NNPAVMIVF 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 207 GGIGKQLGPEH--SQRIeSYLMSIPGIKIVSCSTPFNARGLLKSAIRDNNPILFI---EHVLLynyEQEIPLLPYTLPid 281
Cdd:PRK12315 379 GGSISGNDVTHlgIFDI-PMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAIrvpEHGVE---SGPTVDTDYSTL-- 452

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 258597825 282 KAEVVKNGKDLTVLSYGITRHLASEAAKEL-TKFNIDIEVIDLISLKPFDMETIEKsLKKTKKCLILDE----SAGFG 354
Cdd:PRK12315 453 KYEVTKAGEKVAILALGDFYELGEKVAKKLkEELGIDATLINPKFITGLDEELLEK-LKEDHELVVTLEdgilDGGFG 529
PRK05899 PRK05899
transketolase; Reviewed
 269-330 1.27e-05

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 47.44  E-value: 1.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258597825 269 QEIPLLPYTLPIDKAE----VVKNGKDLTVLSYGITRHLASEAAKELTKFNIDIEVIDLISLKPFD 330
Cdd:PRK05899 448 QNLPVLERTAQEEGVAkggyVLRDDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFD 513
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
 86-360 1.01e-04

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 44.71  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  86 KNIKV--RRNISEALHMAIYEEMKKDKGVYVLGEDVGLYGGSYKVTKNLAhffgfSRVLDTPICENAFMGLGIGSAINDL 163
Cdd:PLN02225 373 KNIMVkdRRTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFP-----DRFFNVGMAEQHAVTFSAGLSSGGL 447

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 164 RP--IIEGmnlSFLILAFNQISNNACMMRYMcdgqfnIPIVIRGPGGIGKQlGPEHSQRIE-SYLMSIPGIKIVSCSTPF 240
Cdd:PLN02225 448 KPfcIIPS---AFLQRAYDQVVHDVDRQRKA------VRFVITSAGLVGSD-GPVQCGAFDiAFMSSLPNMIAMAPADED 517

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825 241 NARGLLKSAIR-DNNPILFI---EHVLLYNYeqeipLLPYTLPID--KAEVVKNGKDLTVLSYGITRHLASEAAKELTKF 314
Cdd:PLN02225 518 ELVNMVATAAYvTDRPVCFRfprGSIVNMNY-----LVPTGLPIEigRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKL 592

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 258597825 315 NIDIEVIDLISLKPFDMETIeKSLKKTKKCLILDESAGFGGIGAEL 360
Cdd:PLN02225 593 GLNVTVADARFCKPLDIKLV-RDLCQNHKFLITVEEGCVGGFGSHV 637
PFOR_II pfam17147
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ...
 283-364 1.42e-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: 38.01  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258597825  283 AEVVkngkdltVLSYGITRHLASEAAKELTKFNIDIEVIDLISLKPFDMETIEKSLKKTKKCLILDESAGFGGIGAeLYT 362
Cdd:pfam17147   1 AEVV-------IVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPEEELKELLAGVKKVVVLDRNISFGSPGQ-LGT 72


                  ..
gi 258597825  363 QV 364
Cdd:pfam17147  73 EV 74
PRK08659 PRK08659
2-oxoacid:acceptor oxidoreductase subunit alpha;
280-346 8.58e-03

2-oxoacid:acceptor oxidoreductase subunit alpha;


Pssm-ID: 181526 [Multi-domain]  Cd Length: 376  Bit Score: 37.92  E-value: 8.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 258597825 280 IDKAEVVkngkdltVLSYGITRHLASEAAKELTKFNIDIEVIDLISLKPFDMETIEKSLKKTKKCLI 346
Cdd:PRK08659 271 LEDAEVV-------VVAYGSVARSARRAVKEAREEGIKVGLFRLITVWPFPEEAIRELAKKVKAIVV 330
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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