|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
3-326 |
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: 503.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 3 TKTMSFRDTIILAMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVD 82
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 83 MTFMDFSVIAMDNIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLKS 162
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 163 SIRDNNPVIILEYKSEFNQKGEVPvDPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTLV 242
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYRLKGEVP-EEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 243 PLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEISAIISEsEAFDYLDAPIRRCAGEDVPMPYAQNLENAMIPTVESIKDA 322
Cdd:COG0022 240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAE-EAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAA 318
|
....
gi 446370869 323 IRKT 326
Cdd:COG0022 319 VREL 322
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
2-326 |
4.27e-136 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 390.50 E-value: 4.27e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 2 ETKTMSFRDTIILAMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIV 81
Cdd:PTZ00182 31 ATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 82 DMTFMDFSVIAMDNIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLK 161
Cdd:PTZ00182 111 EFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 162 SSIRDNNPVIILEYKSEFNQKGEVPVDPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTL 241
Cdd:PTZ00182 191 AAIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 242 VPLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEISAIISEsEAFDYLDAPIRRCAGEDVPMPYAQNLENAMIPTVESIKD 321
Cdd:PTZ00182 271 RPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIME-DCFLYLEAPIKRVCGADTPFPYAKNLEPAYLPDKEKVVE 349
|
....*
gi 446370869 322 AIRKT 326
Cdd:PTZ00182 350 AAKRV 354
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
10-176 |
5.82e-83 |
|
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: 248.16 E-value: 5.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 10 DTIILAMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVDMTFMDFS 89
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 90 VIAMDNIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLKSSIRDNNP 169
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 446370869 170 VIILEYK 176
Cdd:cd07036 161 VIFLEHK 167
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
196-319 |
2.09e-45 |
|
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: 150.82 E-value: 2.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 196 GVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTLVPLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEI 275
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446370869 276 SAIISEsEAFDYLDAPIRRCAGEDVPMPYAQ-NLENAMIPTVESI 319
Cdd:pfam02780 81 AAALAE-EAFDGLDAPVLRVGGPDFPEPGSAdELEKLYGLTPEKI 124
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
74-177 |
1.36e-25 |
|
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: 99.48 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 74 MTGLRPIVDMTFMDFsviamdnivnQAAKTRYMFGGK-GQVPMTVRCAAGNGVGS--AAQHSQSLESWFTHIPGLKVVAP 150
Cdd:smart00861 36 LHGLRPVVEIFFTFF----------DRAKDQIRSAGAsGNVPVVFRHDGGGGVGEdgPTHHSIEDEALLRAIPGLKVVAP 105
|
90 100
....*....|....*....|....*...
gi 446370869 151 GTPADMKGLLKSSIRDNNP-VIILEYKS 177
Cdd:smart00861 106 SDPAEAKGLLRAAIRDDGPvVIRLERKS 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
3-326 |
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: 503.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 3 TKTMSFRDTIILAMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVD 82
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 83 MTFMDFSVIAMDNIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLKS 162
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 163 SIRDNNPVIILEYKSEFNQKGEVPvDPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTLV 242
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYRLKGEVP-EEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 243 PLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEISAIISEsEAFDYLDAPIRRCAGEDVPMPYAQNLENAMIPTVESIKDA 322
Cdd:COG0022 240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAE-EAFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVAA 318
|
....
gi 446370869 323 IRKT 326
Cdd:COG0022 319 VREL 322
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
2-326 |
4.27e-136 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 390.50 E-value: 4.27e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 2 ETKTMSFRDTIILAMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIV 81
Cdd:PTZ00182 31 ATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 82 DMTFMDFSVIAMDNIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLK 161
Cdd:PTZ00182 111 EFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 162 SSIRDNNPVIILEYKSEFNQKGEVPVDPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTL 241
Cdd:PTZ00182 191 AAIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 242 VPLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEISAIISEsEAFDYLDAPIRRCAGEDVPMPYAQNLENAMIPTVESIKD 321
Cdd:PTZ00182 271 RPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIME-DCFLYLEAPIKRVCGADTPFPYAKNLEPAYLPDKEKVVE 349
|
....*
gi 446370869 322 AIRKT 326
Cdd:PTZ00182 350 AAKRV 354
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
4-325 |
1.49e-132 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 380.22 E-value: 1.49e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 4 KTMSFRDTIILAMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVD- 82
Cdd:PRK09212 2 AQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 83 MTFmDFSVIAMDNIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLKS 162
Cdd:PRK09212 82 MTF-NFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 163 SIRDNNPVIILEYKSEFNQKGEVPvDPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTLV 242
Cdd:PRK09212 161 AIRDPNPVIFLENEILYGHSHEVP-EEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 243 PLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEISAIISEsEAFDYLDAPIRRCAGEDVPMPYAQNLENAMIPTVESIKDA 322
Cdd:PRK09212 240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMK-EAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIEA 318
|
...
gi 446370869 323 IRK 325
Cdd:PRK09212 319 VKK 321
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
2-325 |
1.78e-129 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 377.34 E-value: 1.78e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 2 ETKTMSFRDTIILAMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIV 81
Cdd:PRK11892 138 EMVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 82 D-MTFmDFSVIAMDNIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLL 160
Cdd:PRK11892 218 EfMTF-NFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 161 KSSIRDNNPVIILEYKSEFNQKGEVPVDPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRT 240
Cdd:PRK11892 297 KAAIRDPNPVIFLENEILYGQSFDVPKLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 241 LVPLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEISAIISEsEAFDYLDAPIRRCAGEDVPMPYAQNLENAMIPTVESIK 320
Cdd:PRK11892 377 IRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVME-QAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVV 455
|
....*
gi 446370869 321 DAIRK 325
Cdd:PRK11892 456 EAVKA 460
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
1-326 |
3.34e-113 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 332.17 E-value: 3.34e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 1 METKTMSFRDTIILAMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPI 80
Cdd:PLN02683 22 SAAKEMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 81 VD-MTFmDFSVIAMDNIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGL 159
Cdd:PLN02683 102 VEfMTF-NFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 160 LKSSIRDNNPVIILE----YKSEFNQKGEVpVDPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEI 235
Cdd:PLN02683 181 LKAAIRDPDPVVFLEnellYGESFPVSAEV-LDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 236 VDPRTLVPLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEISAIISEsEAFDYLDAPIRRCAGEDVPMPYAQNLENAMIPT 315
Cdd:PLN02683 260 INLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVE-ESFDYLDAPVERIAGADVPMPYAANLERLALPQ 338
|
330
....*....|.
gi 446370869 316 VESIKDAIRKT 326
Cdd:PLN02683 339 VEDIVRAAKRA 349
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
15-325 |
1.19e-91 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 276.23 E-value: 1.19e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 15 AMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVDMTFMDFSVIAMD 94
Cdd:CHL00144 13 AIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFLLLAFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 95 NIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLKSSIRDNNPVIILE 174
Cdd:CHL00144 93 QISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKSAIRSNNPVIFFE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 175 YKSEFNQKGEVPvDPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTLVPLDKDIIINSVK 254
Cdd:CHL00144 173 HVLLYNLKEEIP-DNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVK 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446370869 255 KTGKVVLVNDAHKTSGYIGEISAIISESeAFDYLDAPIRRCAGEDVPMPYAQNLENAMIPTVESIKDAIRK 325
Cdd:CHL00144 252 KTHKVLIVEECMKTGGIGAELIAQINEH-LFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAVEQ 321
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
10-176 |
5.82e-83 |
|
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: 248.16 E-value: 5.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 10 DTIILAMSEEMRRDENVFLMGEDVGVFGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVDMTFMDFS 89
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 90 VIAMDNIVNQAAKTRYMFGGKGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLKSSIRDNNP 169
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 446370869 170 VIILEYK 176
Cdd:cd07036 161 VIFLEHK 167
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
196-319 |
2.09e-45 |
|
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: 150.82 E-value: 2.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 196 GVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTLVPLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEI 275
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446370869 276 SAIISEsEAFDYLDAPIRRCAGEDVPMPYAQ-NLENAMIPTVESI 319
Cdd:pfam02780 81 AAALAE-EAFDGLDAPVLRVGGPDFPEPGSAdELEKLYGLTPEKI 124
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
4-181 |
1.29e-38 |
|
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: 134.99 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 4 KTMSFRDTIILAMSEEMRRDENVFLMGEDVGvfGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTG-LRPIVD 82
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 83 MTFMDFSVIAmdnivnQAAKTRYMFGGKGQVP-MTVRcaAGNGVGS--AAQHSQSLESWFTHIPGLKVVAPGTPADMKGL 159
Cdd:pfam02779 79 ATFSDFLNRA------DDAIRHGAALGKLPVPfVVTR--DPIGVGEdgPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGL 150
|
170 180
....*....|....*....|....
gi 446370869 160 LKSSIR--DNNPVIILEYKSEFNQ 181
Cdd:pfam02779 151 LRAAIRrdGRKPVVLRLPRQLLRP 174
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
1-260 |
6.05e-30 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 115.57 E-value: 6.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 1 METKTMsfRDTIILAMSEEMRRDENVFLMGEDVGVFGGdfgtsvgmLEEFG---PERVRDCPISEAAisgaaagaaM--- 74
Cdd:COG3958 1 MEKKAM--RDAFGEALVELAEEDPDIVVLDADLGGSTK--------LDKFAkafPDRFFNVGIAEQN---------Mvgv 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 75 ------TGLRPIVdMTFMDFSVI-AMDNIVNQAAktrYMfggkgQVPMTVrCAAGNGVGSAAQ---HsQSLE--SWFTHI 142
Cdd:COG3958 62 aaglalAGKIPFV-STFAPFLTGrAYEQIRNDIA---YP-----NLNVKI-VGSHAGLSYGEDgatH-QALEdiALMRAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 143 PGLKVVAPGTPADMKGLLKSSIRDNNPVII-LEyksefnqKGEVPV--DPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRV 219
Cdd:COG3958 131 PNMTVIVPADAVETEAAVRAAAEHDGPVYLrLG-------RGAVPVvyDEDYEFEIGKARVLREGKDVTIIATGIMVAEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446370869 220 VQAAEELAEEGISVEIVDPRTLVPLDKDIIINSVKKTGKVV 260
Cdd:COG3958 204 LEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVV 244
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
74-177 |
1.36e-25 |
|
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: 99.48 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 74 MTGLRPIVDMTFMDFsviamdnivnQAAKTRYMFGGK-GQVPMTVRCAAGNGVGS--AAQHSQSLESWFTHIPGLKVVAP 150
Cdd:smart00861 36 LHGLRPVVEIFFTFF----------DRAKDQIRSAGAsGNVPVVFRHDGGGGVGEdgPTHHSIEDEALLRAIPGLKVVAP 105
|
90 100
....*....|....*....|....*...
gi 446370869 151 GTPADMKGLLKSSIRDNNP-VIILEYKS 177
Cdd:smart00861 106 SDPAEAKGLLRAAIRDDGPvVIRLERKS 133
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
137-264 |
8.42e-23 |
|
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: 98.93 E-value: 8.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 137 SWFTHIPGLKVVAPGTPADMKGLLKSSIRDNNPVIIlEYKsefnqKGEVP-VDPDY---TIPLGVGEIKRQGTDVTVVTY 212
Cdd:COG1154 436 SYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAI-RYP-----RGNGPgVELPAelePLPIGKGEVLREGKDVAILAF 509
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446370869 213 GKMLRRVVQAAEELAEEGISVEIVDPRTLVPLDKDIIINSVKKTGKVVLVND 264
Cdd:COG1154 510 GTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVEE 561
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
137-325 |
6.55e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 87.44 E-value: 6.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 137 SWFTHIPGLKVVAPGTPADMKGLLKSSIR-DNNPVIIlEYKsefnqKGE---VPVDPDYTIPLGVGEIKRQGTDVTVVTY 212
Cdd:PRK05444 398 SYLRCIPNMVIMAPSDENELRQMLYTALAyDDGPIAI-RYP-----RGNgvgVELPELEPLPIGKGEVLREGEDVAILAF 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 213 GKMLRRVVQAAEELAeegiSVEIVDPRTLVPLDKDIIINSVKKTGKVVLVNDAHKTSGYIGEISAIISESEafdyLDAPI 292
Cdd:PRK05444 472 GTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMGGFGSAVLEFLADHG----LDVPV 543
|
170 180 190
....*....|....*....|....*....|....*.
gi 446370869 293 RRCAGEDVPMPY---AQNLENAMIpTVESIKDAIRK 325
Cdd:PRK05444 544 LNLGLPDEFIDHgsrEELLAELGL-DAEGIARRILE 578
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
41-293 |
9.14e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 77.84 E-value: 9.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 41 GTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVDM--TFMD--FSVIAMDnIVNQAAKTRYMFGGKGQVpmt 116
Cdd:PRK12571 349 GTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVysTFLQrgYDQLLHD-VALQNLPVRFVLDRAGLV--- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 117 vrcaagnGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLKSSIRDNNPVIILEYKsefnqKGE---VPVDPDYTI 193
Cdd:PRK12571 425 -------GADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFP-----RGEgvgVEIPAEGTI 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 194 -PLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTLVPLDKDIIINSVKKTgKVVLVNDAHKTSGYI 272
Cdd:PRK12571 493 lGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHH-IVVIVEEQGAMGGFG 571
|
250 260
....*....|....*....|.
gi 446370869 273 GEISAIISESEAFDyLDAPIR 293
Cdd:PRK12571 572 AHVLHHLADTGLLD-GGLKLR 591
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
15-172 |
4.39e-10 |
|
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: 57.45 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 15 AMSEEMRRDENVFLMGEDVGVfggdfGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVDmTFMDFSVIAMD 94
Cdd:cd07033 6 ALLELAKKDPRIVALSADLGG-----STGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVS-TFSFFLQRAYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 95 NIVNQAAktrYMfggkgQVPMTVrCAAGNGVGSA---AQHsQSLE--SWFTHIPGLKVVAPGTPADMKGLLKSSIRDNNP 169
Cdd:cd07033 80 QIRHDVA---LQ-----NLPVKF-VGTHAGISVGedgPTH-QGIEdiALLRAIPNMTVLRPADANETAAALEAALEYDGP 149
|
...
gi 446370869 170 VII 172
Cdd:cd07033 150 VYI 152
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
3-271 |
4.56e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 60.50 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 3 TKTMSFRDTIILAMSEEMRRDENVFLMGedvGVFGGdfGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVD 82
Cdd:PLN02234 354 SKTQSYTSCFVEALIAEAEADKDIVAIH---AAMGG--GTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCT 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 83 MtFMDFSVIAMDNIVNQAAKTRymfggkgqvpMTVRCA---AGNGVGSAAQHSQSLESWFTH-IPGLKVVAPGTPADMKG 158
Cdd:PLN02234 429 I-YSSFMQRAYDQVVHDVDLQK----------LPVRFAidrAGLMGADGPTHCGAFDVTFMAcLPNMIVMAPSDEAELFN 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 159 LLKSSIR-DNNPVIILEYKSEFNQKGEVPVDPDYTIPLGVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVD 237
Cdd:PLN02234 498 MVATAAAiDDRPSCFRYHRGNGIGVSLPPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVAD 577
|
250 260 270
....*....|....*....|....*....|....
gi 446370869 238 PRTLVPLDKdIIINSVKKTGKVVLVNDAHKTSGY 271
Cdd:PLN02234 578 ARFCKPLDV-ALIRSLAKSHEVLITVEEGSIGGF 610
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
7-274 |
1.26e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 53.09 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 7 SFRDTIILAMSEEMRRDENVFLMGEDV-GVFGgdfgtsvgmLEEFG---PERVRDCPISEAAISGAAAGAAMTGLRPI-- 80
Cdd:PRK12315 279 SYSSVTLDYLLKKIKEGKPVVAINAAIpGVFG---------LKEFRkkyPDQYVDVGIAEQESVAFASGIAANGARPVif 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 81 VDMTFMD--FSVIAMDNIVNQAaktrymfggkgqvPMTVRCAAGNGVGSAAQHSQSLE-SWFTHIPGLKVVAPGTPADMK 157
Cdd:PRK12315 350 VNSTFLQraYDQLSHDLAINNN-------------PAVMIVFGGSISGNDVTHLGIFDiPMISNIPNLVYLAPTTKEELI 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 158 GLLKSSIRDNN-PVIILEYKSEFNQKGEVPVD---PDYtiplgvgEIKRQGTDVTVVTYGKMLRRVVQAAEELAEE-GIS 232
Cdd:PRK12315 417 AMLEWALTQHEhPVAIRVPEHGVESGPTVDTDystLKY-------EVTKAGEKVAILALGDFYELGEKVAKKLKEElGID 489
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446370869 233 VEIVDPRTLVPLDKDIIINSVKKTGKVVLVNDAHKTSGYiGE 274
Cdd:PRK12315 490 ATLINPKFITGLDEELLEKLKEDHELVVTLEDGILDGGF-GE 530
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
3-288 |
1.29e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 49.90 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 3 TKTMSFRDTIILAMSEEMRRDENVFLMGedvGVFGGdfGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVD 82
Cdd:PLN02582 353 AKTQSYTTYFAEALIAEAEVDKDVVAIH---AAMGG--GTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 83 MtFMDFSVIAMDNIVNQAAKTRymfggkgqvpMTVRCA---AGNGVGSAAQHSQSLE-SWFTHIPGLKVVAPGTPADMKG 158
Cdd:PLN02582 428 I-YSSFLQRGYDQVVHDVDLQK----------LPVRFAmdrAGLVGADGPTHCGAFDvTYMACLPNMVVMAPSDEAELFH 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 159 LLKSSIRDNNPVIILEYKSEfNQKGeVPVDPDYT-IPL--GVGEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEI 235
Cdd:PLN02582 497 MVATAAAIDDRPSCFRYPRG-NGIG-VQLPPNNKgIPIevGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATV 574
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446370869 236 VDPRTLVPLDKDiIINSVKKTGKVVLVNDahktSGYIGEISAIISESEAFDYL 288
Cdd:PLN02582 575 ADARFCKPLDRA-LIRSLAKSHEVLITVE----EGSIGGFGSHVAQFMALDGL 622
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
7-293 |
2.61e-05 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 45.86 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 7 SFRDTIILAMSEEMRRDENVFLMGEdvgvfGGDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRP--IVDMT 84
Cdd:PLN02225 382 TYSDCFVEALVMEAEKDRDIVVVHA-----GMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPfcIIPSA 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 85 FMDFsviAMDNIVNQAAKTRymfggkGQVPMTVRCAAGNGVGSAAQHSQSLESWFTHIPGLKVVAPGTPADMKGLLKSSI 164
Cdd:PLN02225 457 FLQR---AYDQVVHDVDRQR------KAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAA 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 165 RDNNPVIILEYKsefnqKGEVpVDPDYTIPLGV------GEIKRQGTDVTVVTYGKMLRRVVQAAEELAEEGISVEIVDP 238
Cdd:PLN02225 528 YVTDRPVCFRFP-----RGSI-VNMNYLVPTGLpieigrGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADA 601
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446370869 239 RTLVPLDKDIIINSVKKTGKVVLVNDahktsGYIGEISAIISESEAFD-YLDAPIR 293
Cdd:PLN02225 602 RFCKPLDIKLVRDLCQNHKFLITVEE-----GCVGGFGSHVAQFIALDgQLDGNIK 652
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
35-174 |
9.23e-05 |
|
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: 41.95 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 35 VFG--GDFGTSVGMLEEFGPERVRDCPISEAAISGAAAGAAMTGLRPIVDMTFMDFSVIAMDNIVNQAAKtrymfggkgQ 112
Cdd:cd06586 15 VFGypGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADAAAE---------H 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446370869 113 VPMTVRCAAGNGVGSAAQHSQSLE--SWFTHIPGLKVVAPGTPADMKGLLKSSIRDNN---PVIILE 174
Cdd:cd06586 86 LPVVFLIGARGISAQAKQTFQSMFdlGMYRSIPEANISSPSPAELPAGIDHAIRTAYAsqgPVVVRL 152
|
|
| PFOR_II |
pfam17147 |
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ... |
206-300 |
2.17e-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: 36.85 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446370869 206 DVTVVTYGKMLRRVVQAAEELAEEGISVEIVDPRTLVPLDKDIIINSVKKTgKVVLVNDAHKTSGYIG----EISAIISE 281
Cdd:pfam17147 2 EVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPEEELKELLAGV-KKVVVLDRNISFGSPGqlgtEVKAALYD 80
|
90
....*....|....*....
gi 446370869 282 SEAFDYldAPIRRCAGEDV 300
Cdd:pfam17147 81 SDPPVV--NFIAGLGGRDI 97
|
|
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