|
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
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