|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-325 |
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: 521.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 1 MAQMTMVQAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVME 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 81 IQFLGFVFEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLIS 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 161 SIRSNDPVVYLEHMKLYRSfREEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQ 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYRL-KGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 241 PLDMDTLVASVEKTGRVVVVQEAQRQSGVGANVAAELQERAILSLEAPIARVAAADTVYPFTQA-ENVWLPNKNDIVEQA 319
Cdd:COG0022 240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPAlEKAYLPSADRIVAAV 319
|
....*.
gi 488390039 320 KATLEF 325
Cdd:COG0022 320 RELLAY 325
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-323 |
4.11e-141 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 402.82 E-value: 4.11e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 1 MAQMTMVQAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVME 80
Cdd:PTZ00182 32 TVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 81 IQFLGFVFEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLIS 160
Cdd:PTZ00182 112 FMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 161 SIRSNDPVVYLEHMKLYRSFREEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQ 240
Cdd:PTZ00182 192 AIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 241 PLDMDTLVASVEKTGRVVVVQEAQRQSGVGANVAAELQERAILSLEAPIARVAAADTVYPFTQA-ENVWLPNKNDIVEQA 319
Cdd:PTZ00182 272 PWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNlEPAYLPDKEKVVEAA 351
|
....
gi 488390039 320 KATL 323
Cdd:PTZ00182 352 KRVL 355
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
8-173 |
4.00e-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: 248.55 E-value: 4.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 8 QAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVMEIQFLGFV 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 88 FEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLISSIRSNDP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*.
gi 488390039 168 VVYLEH 173
Cdd:cd07036 161 VIFLEH 166
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
194-315 |
3.06e-44 |
|
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: 147.74 E-value: 3.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 194 GKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQPLDMDTLVASVEKTGRVVVVQEAQRQSGVGANV 273
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488390039 274 AAELQERAILSLEAPIARVAAADTVYPFTQA--ENVWLPNKNDI 315
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPDFPEPGSADelEKLYGLTPEKI 124
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
2-178 |
2.43e-30 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 111.81 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 2 AQMTMVQAINNALKTELqndenvlifgedvgvnggvfrvteglqkefgedrvFDTPLAESGIGGLALGLTTQGYRPVMEI 81
Cdd:smart00861 1 KKIATRKAFGEALAELA-----------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 82 QFLGFVFevfdevagqiARTRFRSGGT-KTAPVTIRTPFGGGVHT--PELHADNLEGILAQSPGIKVVIPSGPYDAKGLL 158
Cdd:smart00861 46 FFTFFDR----------AKDQIRSAGAsGNVPVVFRHDGGGGVGEdgPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLL 115
|
170 180
....*....|....*....|.
gi 488390039 159 ISSIRSNDP-VVYLEHMKLYR 178
Cdd:smart00861 116 RAAIRDDGPvVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
1-325 |
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: 521.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 1 MAQMTMVQAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVME 80
Cdd:COG0022 1 MRELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 81 IQFLGFVFEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLIS 160
Cdd:COG0022 81 IQFADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 161 SIRSNDPVVYLEHMKLYRSfREEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQ 240
Cdd:COG0022 161 AIRDDDPVIFLEHKRLYRL-KGEVPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 241 PLDMDTLVASVEKTGRVVVVQEAQRQSGVGANVAAELQERAILSLEAPIARVAAADTVYPFTQA-ENVWLPNKNDIVEQA 319
Cdd:COG0022 240 PLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPAlEKAYLPSADRIVAAV 319
|
....*.
gi 488390039 320 KATLEF 325
Cdd:COG0022 320 RELLAY 325
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-323 |
4.11e-141 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 402.82 E-value: 4.11e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 1 MAQMTMVQAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVME 80
Cdd:PTZ00182 32 TVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 81 IQFLGFVFEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLIS 160
Cdd:PTZ00182 112 FMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDPEDAKGLLKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 161 SIRSNDPVVYLEHMKLYRSFREEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQ 240
Cdd:PTZ00182 192 AIRDPNPVVFFEPKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 241 PLDMDTLVASVEKTGRVVVVQEAQRQSGVGANVAAELQERAILSLEAPIARVAAADTVYPFTQA-ENVWLPNKNDIVEQA 319
Cdd:PTZ00182 272 PWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNlEPAYLPDKEKVVEAA 351
|
....
gi 488390039 320 KATL 323
Cdd:PTZ00182 352 KRVL 355
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
1-324 |
3.99e-101 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 300.10 E-value: 3.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 1 MAQMTMVQAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVME 80
Cdd:PRK09212 1 MAQLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 81 IQFLGFVFEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLIS 160
Cdd:PRK09212 81 FMTFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 161 SIRSNDPVVYLEHMKLYrSFREEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQ 240
Cdd:PRK09212 161 AIRDPNPVIFLENEILY-GHSHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 241 PLDMDTLVASVEKTGRVVVVQEAQRQSGVGANVAAELQERAILSLEAPIARVAAADTVYPF-TQAENVWLPNKNDIVEQA 319
Cdd:PRK09212 240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYaANLEKLALPSEEDIIEAV 319
|
....*
gi 488390039 320 KATLE 324
Cdd:PRK09212 320 KKVCY 324
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
1-321 |
3.30e-91 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 279.49 E-value: 3.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 1 MAQMTMVQAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVME 80
Cdd:PRK11892 139 MVTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 81 IQFLGFVFEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLIS 160
Cdd:PRK11892 219 FMTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 161 SIRSNDPVVYLEHMKLY-RSFreEVPE-EEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRT 238
Cdd:PRK11892 299 AIRDPNPVIFLENEILYgQSF--DVPKlDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 239 VQPLDMDTLVASVEKTGRVVVVQEAQRQSGVGANVAAELQERAILSLEAPIARVAAADTVYPFT-QAENVWLPNKNDIVE 317
Cdd:PRK11892 377 IRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAaNLEKLALPSVAEVVE 456
|
....
gi 488390039 318 QAKA 321
Cdd:PRK11892 457 AVKA 460
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
3-322 |
5.56e-91 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 275.54 E-value: 5.56e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 3 QMTMVQAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVMEIQ 82
Cdd:PLN02683 26 EMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 83 FLGFVFEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLISSI 162
Cdd:PLN02683 106 TFNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLKAAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 163 RSNDPVVYLEHMKLY-RSF--REEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTV 239
Cdd:PLN02683 186 RDPDPVVFLENELLYgESFpvSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 240 QPLDMDTLVASVEKTGRVVVVQEAQRQSGVGANVAAELQERAILSLEAPIARVAAADTVYPF-TQAENVWLPNKNDIVEQ 318
Cdd:PLN02683 266 RPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPYaANLERLALPQVEDIVRA 345
|
....
gi 488390039 319 AKAT 322
Cdd:PLN02683 346 AKRA 349
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
1-324 |
3.31e-83 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 254.66 E-value: 3.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 1 MAQMTMVQAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVME 80
Cdd:CHL00144 1 MSEVFLFEALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 81 IQFLGFVFEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLIS 160
Cdd:CHL00144 81 GMNMGFLLLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 161 SIRSNDPVVYLEHMKLYrSFREEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQ 240
Cdd:CHL00144 161 AIRSNNPVIFFEHVLLY-NLKEEIPDNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 241 PLDMDTLVASVEKTGRVVVVQEAQRQSGVGANVAAELQERAILSLEAPIARVAAADTVYPFT-QAENVWLPNKNDIVEQA 319
Cdd:CHL00144 240 PLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYNgPLEEATVIQPAQIIEAV 319
|
....*
gi 488390039 320 KATLE 324
Cdd:CHL00144 320 EQIIT 324
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
8-173 |
4.00e-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: 248.55 E-value: 4.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 8 QAINNALKTELQNDENVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQGYRPVMEIQFLGFV 87
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 88 FEVFDEVAGQIARTRFRSGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLISSIRSNDP 167
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*.
gi 488390039 168 VVYLEH 173
Cdd:cd07036 161 VIFLEH 166
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
194-315 |
3.06e-44 |
|
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: 147.74 E-value: 3.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 194 GKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQPLDMDTLVASVEKTGRVVVVQEAQRQSGVGANV 273
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488390039 274 AAELQERAILSLEAPIARVAAADTVYPFTQA--ENVWLPNKNDI 315
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPDFPEPGSADelEKLYGLTPEKI 124
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
1-297 |
2.30e-41 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 146.00 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 1 MAQMTMVQAINNALKTELQNDENVLIFGEDVGVNGGvfrvTEGLQKEFGeDRVFDTPLAESGIGGLALGLTTQGYRPVme 80
Cdd:COG3958 1 MEKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTK----LDKFAKAFP-DRFFNVGIAEQNMVGVAAGLALAGKIPF-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 81 iqFLGF-VF---EVFDEVAGQIARTRfrsggtktAPVTIrTPFGGGVHTPEL----HAdnLE--GILAQSPGIKVVIPSG 150
Cdd:COG3958 74 --VSTFaPFltgRAYEQIRNDIAYPN--------LNVKI-VGSHAGLSYGEDgathQA--LEdiALMRALPNMTVIVPAD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 151 PYDAKGLLISSIRSNDPVvYlehMKLYRSFREEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHS 230
Cdd:COG3958 141 AVETEAAVRAAAEHDGPV-Y---LRLGRGAVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGIS 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488390039 231 VEVIDLRTVQPLDMDTLVASVEKTGRVVVVQEAQRQSGVGANVAAELQERailsLEAPIARVAAADT 297
Cdd:COG3958 217 ARVINMHTIKPLDEEAILKAARKTGAVVTAEEHSIIGGLGSAVAEVLAEN----YPVPLRRIGVPDR 279
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
2-178 |
5.04e-36 |
|
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: 128.05 E-value: 5.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 2 AQMTMVQAINNALKTELQNDENVLIFGEDVGvnGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLALGLTTQG-YRPVME 80
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLA--GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 81 IQFLGFVFEVFDevagQIARTRFRsGGTKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLIS 160
Cdd:pfam02779 79 ATFSDFLNRADD----AIRHGAAL-GKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRA 153
|
170 180
....*....|....*....|
gi 488390039 161 SIRSND--PVVYLEHMKLYR 178
Cdd:pfam02779 154 AIRRDGrkPVVLRLPRQLLR 173
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
2-178 |
2.43e-30 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 111.81 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 2 AQMTMVQAINNALKTELqndenvlifgedvgvnggvfrvteglqkefgedrvFDTPLAESGIGGLALGLTTQGYRPVMEI 81
Cdd:smart00861 1 KKIATRKAFGEALAELA-----------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEI 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 82 QFLGFVFevfdevagqiARTRFRSGGT-KTAPVTIRTPFGGGVHT--PELHADNLEGILAQSPGIKVVIPSGPYDAKGLL 158
Cdd:smart00861 46 FFTFFDR----------AKDQIRSAGAsGNVPVVFRHDGGGGVGEdgPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLL 115
|
170 180
....*....|....*....|.
gi 488390039 159 ISSIRSNDP-VVYLEHMKLYR 178
Cdd:smart00861 116 RAAIRDDGPvVIRLERKSLYR 136
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
183-283 |
2.55e-26 |
|
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440768 [Multi-domain] Cd Length: 623 Bit Score: 108.95 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 183 EVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQPLDMDTLVASVEKTGRVVVVQE 262
Cdd:COG1154 482 ELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVEE 561
|
90 100
....*....|....*....|.
gi 488390039 263 AQRQSGVGANVAAELQERAIL 283
Cdd:COG1154 562 GVLAGGFGSAVLEFLADAGLD 582
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
44-288 |
2.44e-20 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 91.30 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 44 LQKEFGeDRVFDTPLAESGIGGLALGLTTQGYRPVMEI--QFL--GFVfEVFDEVAGQIARTRF---RSGGT----KTap 112
Cdd:PRK05444 315 FSKRFP-DRYFDVGIAEQHAVTFAAGLATEGLKPVVAIysTFLqrAYD-QVIHDVALQNLPVTFaidRAGLVgadgPT-- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 113 vtirtpfgggvhtpelHAdnleGI-----LAQSPGIKVVIPSGPYDAKGLLISSIRSND-PVVYlehmklyR----SFRE 182
Cdd:PRK05444 391 ----------------HQ----GAfdlsyLRCIPNMVIMAPSDENELRQMLYTALAYDDgPIAI-------RyprgNGVG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 183 EVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEkdghSVEVIDLRTVQPLDMDTLVASVEKTGRVVVVQE 262
Cdd:PRK05444 444 VELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEE 519
|
250 260 270
....*....|....*....|....*....|
gi 488390039 263 AQRQSGVGANVAAELQER----AILSLEAP 288
Cdd:PRK05444 520 GAIMGGFGSAVLEFLADHgldvPVLNLGLP 549
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
44-289 |
7.01e-20 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 90.17 E-value: 7.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 44 LQKEFgEDRVFDTPLAESGIGGLALGLTTQGYRPVMEIqFLGFVFEVFDEVAGQIARTRFrsggtktaPVTIRTPFGGGV 123
Cdd:PRK12571 355 LQKRF-PNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAV-YSTFLQRGYDQLLHDVALQNL--------PVRFVLDRAGLV 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 124 HTP-ELHADNLE-GILAQSPGIKVVIPSGPYDAKGLLISSIRSND-PVVylehmklyrsFR--------EEVPEEEYTIE 192
Cdd:PRK12571 425 GADgATHAGAFDlAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDgPIA----------VRfprgegvgVEIPAEGTILG 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 193 IGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQPLDMDtLVASVEKTGRVVVVQEAQRQSGVGAN 272
Cdd:PRK12571 495 IGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEA-LTDLLVRHHIVVIVEEQGAMGGFGAH 573
|
250
....*....|....*..
gi 488390039 273 VAAELQERAILSLEAPI 289
Cdd:PRK12571 574 VLHHLADTGLLDGGLKL 590
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
191-274 |
5.50e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 63.38 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 191 IEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQPLDMDtLVASVEKTGRVVVVQEAQRQSGVG 270
Cdd:PLN02582 532 IEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRA-LIRSLAKSHEVLITVEEGSIGGFG 610
|
....
gi 488390039 271 ANVA 274
Cdd:PLN02582 611 SHVA 614
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
13-274 |
6.37e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 63.20 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 13 ALKTELQNDENVLIFGEDVGVNGGVFRvtegLQKEFgEDRVFDTPLAESGIGGLALGLTTQGYRPVMEIQFlGFVFEVFD 92
Cdd:PLN02225 390 ALVMEAEKDRDIVVVHAGMEMDASLIT----FQERF-PDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPS-AFLQRAYD 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 93 EVAGQIARTRfrsggtKTAPVTIRTPFGGGVHTPELHADNLEGILAQSPGIKVVIPSGPYDAKGLLISSIRSNDPVVYLE 172
Cdd:PLN02225 464 QVVHDVDRQR------KAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDRPVCFR 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 173 HMKLYRSFREEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQPLDMdTLVASVE 252
Cdd:PLN02225 538 FPRGSIVNMNYLVPTGLPIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDI-KLVRDLC 616
|
250 260
....*....|....*....|..
gi 488390039 253 KTGRVVVVQEAQRQSGVGANVA 274
Cdd:PLN02225 617 QNHKFLITVEEGCVGGFGSHVA 638
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
13-273 |
4.34e-09 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 57.42 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 13 ALKTELQNDENVLIFGEDVGvnGGVfrVTEGLQKEFgEDRVFDTPLAESGIGGLALGLTTQGYRPVMEIqFLGFVFEVFD 92
Cdd:PLN02234 366 ALIAEAEADKDIVAIHAAMG--GGT--MLNLFESRF-PTRCFDVGIAEQHAVTFAAGLACEGLKPFCTI-YSSFMQRAYD 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 93 EVAGQIARTRFrsggtktaPVTIRTPFGG--GVHTPElHADNLE-GILAQSPGIKVVIPSGPYDAKGLLISSIRSND-PV 168
Cdd:PLN02234 440 QVVHDVDLQKL--------PVRFAIDRAGlmGADGPT-HCGAFDvTFMACLPNMIVMAPSDEAELFNMVATAAAIDDrPS 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 169 VYLEHMKLYRSFREEVPEEEYTIEIGKAKVVKEGTDITLIAYGAMVQESVKAAEELEKDGHSVEVIDLRTVQPLDMdTLV 248
Cdd:PLN02234 511 CFRYHRGNGIGVSLPPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDV-ALI 589
|
250 260
....*....|....*....|....*
gi 488390039 249 ASVEKTGRVVVVQEAQRQSGVGANV 273
Cdd:PLN02234 590 RSLAKSHEVLITVEEGSIGGFGSHV 614
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
14-274 |
2.69e-05 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 45.77 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 14 LKTELQNDENVlifgedVGVNG---GVFRVTEgLQKEFGeDRVFDTPLAESGIGGLALGLTTQGYRPVMeIQFLGFVFEV 90
Cdd:PRK12315 288 LLKKIKEGKPV------VAINAaipGVFGLKE-FRKKYP-DQYVDVGIAEQESVAFASGIAANGARPVI-FVNSTFLQRA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 91 FDEVAGQIArtrfrsggTKTAPVTIrTPFGGGVH-TPELHadnlEGILAQS-----PGIKVVIPSGPYDAKGLLISSIRS 164
Cdd:PRK12315 359 YDQLSHDLA--------INNNPAVM-IVFGGSISgNDVTH----LGIFDIPmisniPNLVYLAPTTKEELIAMLEWALTQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390039 165 ND-PVVYLEHMKLYRSfREEVPEEEYTIeigKAKVVKEGTDITLIAYGAMVQESVKAAEEL-EKDGHSVEVIDLRTVQPL 242
Cdd:PRK12315 426 HEhPVAIRVPEHGVES-GPTVDTDYSTL---KYEVTKAGEKVAILALGDFYELGEKVAKKLkEELGIDATLINPKFITGL 501
|
250 260 270
....*....|....*....|....*....|..
gi 488390039 243 DMDTLVASVEKTGRVVVVQEAQRQSGVGANVA 274
Cdd:PRK12315 502 DEELLEKLKEDHELVVTLEDGILDGGFGEKIA 533
|
|
| Prefoldin_alpha |
cd00584 |
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ... |
214-286 |
9.08e-03 |
|
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467468 [Multi-domain] Cd Length: 121 Bit Score: 35.67 E-value: 9.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390039 214 VQESVKAAEELEKDGHSVEVidlrtvqPLDMDTLV-ASVEKTGRVVVvqeaqrqsGVGANVAAEL-QERAILSLE 286
Cdd:cd00584 29 IDEAKEALEELKKEGSEVLV-------PLGGNAYVrAEVVDIDKVIV--------HLGLGYYAERdPDGAIEILE 88
|
|
| |
