|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
32-337 |
0e+00 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 517.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:PRK11892 141 TMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFM 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:PRK11892 221 TFNFAMQAIDQIINSAAKTLYMSGgqmgcpivfrgpngaaarVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVPFEFPpeaQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTI 253
Cdd:PRK11892 301 RDPNPVIFLENEILYGQSFDVP---KLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTI 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 254 RPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 333
Cdd:PRK11892 378 RPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVME-QAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVE 456
|
....
gi 291084858 334 AIKK 337
Cdd:PRK11892 457 AVKA 460
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
32-340 |
6.70e-166 |
|
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: 465.26 E-value: 6.70e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:COG0022 3 ELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVEIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:COG0022 83 FADFIYPAFDQIVNQAAKLRYMSGgqfkvpmvirtpygggigAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVPFEFPPEaqskDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTI 253
Cdd:COG0022 163 RDDDPVIFLEHKRLYRLKGEVPEE----DYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 254 RPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 333
Cdd:COG0022 239 SPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEE-AFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVA 317
|
....*..
gi 291084858 334 AIKKTLN 340
Cdd:COG0022 318 AVRELLA 324
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
37-185 |
3.50e-95 |
|
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: 279.75 E-value: 3.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNP 178
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGgqfkvpivirgpngggigGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 291084858 179 VVVLENE 185
Cdd:cd07036 161 VIFLEHK 167
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
208-331 |
1.18e-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: 151.59 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 208 GKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEI 287
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 291084858 288 CARIMEgPAFNFLDAPAVRVTGADVPMPY-AKILEDNSIPQVKDI 331
Cdd:pfam02780 81 AAALAE-EAFDGLDAPVLRVGGPDFPEPGsADELEKLYGLTPEKI 124
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
83-189 |
3.29e-27 |
|
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: 104.11 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 83 IDTPISEMGFAGIAVGAAMAGLRPICEFMtFNFSMQAIDQVINSAAKT------------YYMSGVAAQHSQCFAAWYGH 150
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQIRSAGASGnvpvvfrhdgggGVGEDGPTHHSIEDEALLRA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 291084858 151 CPGLKVVSPWNSEDAKGLIKSAIRDNNPVVV-LENELMYG 189
Cdd:smart00861 97 IPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIrLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
32-337 |
0e+00 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 517.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:PRK11892 141 TMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFM 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:PRK11892 221 TFNFAMQAIDQIINSAAKTLYMSGgqmgcpivfrgpngaaarVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVPFEFPpeaQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTI 253
Cdd:PRK11892 301 RDPNPVIFLENEILYGQSFDVP---KLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTI 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 254 RPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 333
Cdd:PRK11892 378 RPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVME-QAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVE 456
|
....
gi 291084858 334 AIKK 337
Cdd:PRK11892 457 AVKA 460
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
6-338 |
0e+00 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 513.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 6 GLVRRPLREVSGLLKRRFhwtAPAALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDT 85
Cdd:PLN02683 3 GQLLRRTRPAAAAAARGY---ASAAKEMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 86 PISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMS------------------GVAAQHSQCFAAW 147
Cdd:PLN02683 80 PITEAGFTGIGVGAAYAGLKPVVEFMTFNFSMQAIDHIINSAAKTNYMSagqisvpivfrgpngaaaGVGAQHSQCFAAW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 148 YGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRP 227
Cdd:PLN02683 160 YSSVPGLKVLAPYSSEDARGLLKAAIRDPDPVVFLENELLYGESFPVSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 228 VGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRV 307
Cdd:PLN02683 240 VGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVE-ESFDYLDAPVERI 318
|
330 340 350
....*....|....*....|....*....|.
gi 291084858 308 TGADVPMPYAKILEDNSIPQVKDIIFAIKKT 338
Cdd:PLN02683 319 AGADVPMPYAANLERLALPQVEDIVRAAKRA 349
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
19-339 |
4.87e-177 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 494.50 E-value: 4.87e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 19 LKRRFHWTAP--AALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIA 96
Cdd:PTZ00182 19 SASRSSSTESkgATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 97 VGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVS 158
Cdd:PTZ00182 99 IGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGgqfdcpivirgpngavghGGAYHSQSFEAYFAHVPGLKVVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 159 PWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAqskDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVL 238
Cdd:PTZ00182 179 PSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEA---DYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEEL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 239 SKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAK 318
Cdd:PTZ00182 256 AKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMED-CFLYLEAPIKRVCGADTPFPYAK 334
|
330 340
....*....|....*....|.
gi 291084858 319 ILEDNSIPQVKDIIFAIKKTL 339
Cdd:PTZ00182 335 NLEPAYLPDKEKVVEAAKRVL 355
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
32-340 |
1.82e-170 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 476.91 E-value: 1.82e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:PRK09212 3 QLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:PRK09212 83 TFNFSMQAIDQIVNSAAKTNYMSGgqlkcpivfrgpngaaarVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKTAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVPFEFPPEAQSkdflIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTI 253
Cdd:PRK09212 163 RDPNPVIFLENEILYGHSHEVPEEEES----IPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 254 RPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 333
Cdd:PRK09212 239 RPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMK-EAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIE 317
|
....*..
gi 291084858 334 AIKKTLN 340
Cdd:PRK09212 318 AVKKVCY 324
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
32-340 |
6.70e-166 |
|
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: 465.26 E-value: 6.70e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:COG0022 3 ELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVEIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:COG0022 83 FADFIYPAFDQIVNQAAKLRYMSGgqfkvpmvirtpygggigAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVPFEFPPEaqskDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTI 253
Cdd:COG0022 163 RDDDPVIFLEHKRLYRLKGEVPEE----DYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 254 RPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 333
Cdd:COG0022 239 SPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEE-AFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVA 317
|
....*..
gi 291084858 334 AIKKTLN 340
Cdd:COG0022 318 AVRELLA 324
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
37-340 |
2.44e-95 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 286.25 E-value: 2.44e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:CHL00144 8 EALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVV---SPWNsedAKGLIKSAIRD 175
Cdd:CHL00144 88 LLAFNQISNNAGMLHYTSGgnftipivirgpggvgrqLGAEHSQRLESYFQSVPGLQIVacsTPYN---AKGLLKSAIRS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 176 NNPVVVLENELMYGVPFEFPPEaqskDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRP 255
Cdd:CHL00144 165 NNPVIFFEHVLLYNLKEEIPDN----EYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 256 MDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAI 335
Cdd:CHL00144 241 LDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEH-LFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAV 319
|
....*
gi 291084858 336 KKTLN 340
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 ... |
37-185 |
3.50e-95 |
|
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: 279.75 E-value: 3.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNP 178
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGgqfkvpivirgpngggigGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 291084858 179 VVVLENE 185
Cdd:cd07036 161 VIFLEHK 167
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
208-331 |
1.18e-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: 151.59 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 208 GKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEI 287
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 291084858 288 CARIMEgPAFNFLDAPAVRVTGADVPMPY-AKILEDNSIPQVKDI 331
Cdd:pfam02780 81 AAALAE-EAFDGLDAPVLRVGGPDFPEPGsADELEKLYGLTPEKI 124
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
32-190 |
8.27e-40 |
|
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: 138.07 E-value: 8.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQydGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAG-LRPICEF 110
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLAG--GTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 111 MTFNFSMQAIDQVINSAAKTYYMSG-------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIR--D 175
Cdd:pfam02779 80 TFSDFLNRADDAIRHGAALGKLPVPfvvtrdpigvgedGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRrdG 159
|
170
....*....|....*
gi 291084858 176 NNPVVVLENELMYGV 190
Cdd:pfam02779 160 RKPVVLRLPRQLLRP 174
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
37-185 |
7.11e-30 |
|
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: 111.67 E-value: 7.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 37 DAINQGMDEELerdeKVFLLGEEVAQYdgayKVSRGLWKKyGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:cd06586 1 AAFAEVLTAWG----VRHVFGYPGDEI----SSLLDALRE-GDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVInSAAKTY----YMSGV--------AAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNN---PVVV 181
Cdd:cd06586 72 LNAINGLA-DAAAEHlpvvFLIGArgisaqakQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAsqgPVVV 150
|
....
gi 291084858 182 LENE 185
Cdd:cd06586 151 RLPR 154
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
34-275 |
1.59e-28 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 112.10 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 34 TVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSrglwKKYGDkRIIDTPISEMGFAGIAVGAAMAGLRPICefMTF 113
Cdd:COG3958 5 AMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFA----KAFPD-RFFNVGIAEQNMVGVAAGLALAGKIPFV--STF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 114 -NF-SMQAIDQVINSAAktyYM----------SGVAAQHS----QCFA--AWYGHCPGLKVVSPWNSEDAKGLIKSAI-- 173
Cdd:COG3958 78 aPFlTGRAYEQIRNDIA---YPnlnvkivgshAGLSYGEDgathQALEdiALMRALPNMTVIVPADAVETEAAVRAAAeh 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 ---------RDNNPVVVLENElmygvPFEfppeaqskdflipIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVE 244
Cdd:COG3958 155 dgpvylrlgRGAVPVVYDEDY-----EFE-------------IGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGIS 216
|
250 260 270
....*....|....*....|....*....|.
gi 291084858 245 CEVINMRTIRPMDMETIEASVMKTNHLVTVE 275
Cdd:COG3958 217 ARVINMHTIKPLDEEAILKAARKTGAVVTAE 247
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
83-189 |
3.29e-27 |
|
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: 104.11 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 83 IDTPISEMGFAGIAVGAAMAGLRPICEFMtFNFSMQAIDQVINSAAKT------------YYMSGVAAQHSQCFAAWYGH 150
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQIRSAGASGnvpvvfrhdgggGVGEDGPTHHSIEDEALLRA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 291084858 151 CPGLKVVSPWNSEDAKGLIKSAIRDNNPVVV-LENELMYG 189
Cdd:smart00861 97 IPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIrLERKSLYR 136
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
37-181 |
4.22e-20 |
|
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: 85.57 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKvsrgLWKKYGDkRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFnFS 116
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDK----FAKKFPD-RFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSF-FL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAktyYM----------SGVAA------QHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVV 180
Cdd:cd07033 75 QRAYDQIRHDVA---LQnlpvkfvgthAGISVgedgptHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVY 151
|
.
gi 291084858 181 V 181
Cdd:cd07033 152 I 152
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
75-293 |
1.28e-17 |
|
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: 83.52 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 75 KKYGDkRIIDTPISE---MGFAGiavGAAMAGLRPICE-FMTFnfsMQ-AIDQVInsaaktyymsgvaaqHSQC------ 143
Cdd:COG1154 355 ERFPD-RFFDVGIAEqhaVTFAA---GLATEGLKPVVAiYSTF---LQrAYDQVI---------------HDVAlqnlpv 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 144 -FA--------------------AWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVlenelMY------GVPFEFPP 196
Cdd:COG1154 413 tFAidraglvgadgpthhgvfdlSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAI-----RYprgngpGVELPAEL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 197 EAqskdflIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEG 276
Cdd:COG1154 488 EP------LPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVEE 561
|
250
....*....|....*..
gi 291084858 277 GWPQFGVGAEICARIME 293
Cdd:COG1154 562 GVLAGGFGSAVLEFLAD 578
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
73-293 |
3.34e-14 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 73.19 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 73 LWKKYGDkRIIDTPISE---MGFAGiavGAAMAGLRPICE-FMTFnfsMQ-AIDQVINSaaktyymsgVAAQ-------- 139
Cdd:PRK05444 315 FSKRFPD-RYFDVGIAEqhaVTFAA---GLATEGLKPVVAiYSTF---LQrAYDQVIHD---------VALQnlpvtfai 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 140 ------------HSQCF-AAWYGHCPGLKVVSPWNSEDAKGLIKSAIR-DNNPVVVlenelMY----GVPFEFPPEAQsk 201
Cdd:PRK05444 379 draglvgadgptHQGAFdLSYLRCIPNMVIMAPSDENELRQMLYTALAyDDGPIAI-----RYprgnGVGVELPELEP-- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 202 dflIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSkegvECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQF 281
Cdd:PRK05444 452 ---LPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMG 524
|
250
....*....|..
gi 291084858 282 GVGAEICARIME 293
Cdd:PRK05444 525 GFGSAVLEFLAD 536
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
81-277 |
8.41e-14 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 72.44 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 81 RIIDTPISEMGFAGIAVGAAMAGLRPICEFMTfNFSMQAIDQVIN-----------SAAKTYYMSGVAAQHSQCFAAWYG 149
Cdd:PLN02234 400 RCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHdvdlqklpvrfAIDRAGLMGADGPTHCGAFDVTFM 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 150 HC-PGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPeaQSKDFLIPIGKAKIERQGTHITVVSHSRPV 228
Cdd:PLN02234 479 AClPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPP--GNKGVPLQIGRGRILRDGERVALLGYGSAV 556
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 291084858 229 GHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGG 277
Cdd:PLN02234 557 QRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEG 605
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
80-287 |
3.56e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 61.28 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 80 KRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTfNFSMQAIDQVINSAA-----KTYYM--SGV----AAQHSQCF-AAW 147
Cdd:PRK12571 361 NRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYS-TFLQRGYDQLLHDVAlqnlpVRFVLdrAGLvgadGATHAGAFdLAF 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 148 YGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQskdfLIPIGKAKIERQGTHITVVS---H 224
Cdd:PRK12571 440 LTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVGVEIPAEGT----ILGIGKGRVPREGPDVAILSvgaH 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084858 225 SRPvghCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGwPQFGVGAEI 287
Cdd:PRK12571 516 LHE---CLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHIVVIVEEQG-AMGGFGAHV 574
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
81-277 |
6.25e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 60.30 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 81 RIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFnFSMQAIDQVIN-----------SAAKTYYMSGVAAQHSQCFAAWYG 149
Cdd:PLN02582 399 RCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSS-FLQRGYDQVVHdvdlqklpvrfAMDRAGLVGADGPTHCGAFDVTYM 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 150 HC-PGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEaqSKDFLIPIGKAKIERQGTHITVVSHSRPV 228
Cdd:PLN02582 478 AClPNMVVMAPSDEAELFHMVATAAAIDDRPSCFRYPRGNGIGVQLPPN--NKGIPIEVGKGRILLEGERVALLGYGTAV 555
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 291084858 229 GHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGG 277
Cdd:PLN02582 556 QSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEG 604
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
20-287 |
3.21e-08 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 55.01 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 20 KRRFHWTAPAALQV----------TVRDAINQGMDEELERDEKVFLLGeevAQYDGAYKVSRgLWKKYGDkRIIDTPISE 89
Cdd:PRK12315 255 KEAFHWHMPFDLETgqskvpasgeSYSSVTLDYLLKKIKEGKPVVAIN---AAIPGVFGLKE-FRKKYPD-QYVDVGIAE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 90 MGFAGIAVGAAMAGLRPICeFMTFNFSMQAIDQVI-------NSAAKTYYMSGVAAQ---HSQCFA-AWYGHCPGLKVVS 158
Cdd:PRK12315 330 QESVAFASGIAANGARPVI-FVNSTFLQRAYDQLShdlainnNPAVMIVFGGSISGNdvtHLGIFDiPMISNIPNLVYLA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 159 PWNSEDAKGLIKSAIRDNN-PVVVleneLMYGVPFEFPPEAQSkDFLIPigKAKIERQGTHITVVSHSRPVGHCLEAAAV 237
Cdd:PRK12315 409 PTTKEELIAMLEWALTQHEhPVAI----RVPEHGVESGPTVDT-DYSTL--KYEVTKAGEKVAILALGDFYELGEKVAKK 481
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 291084858 238 LSKE-GVECEVINMRTIRPMDMETIEAsvMKTNH--LVTVEGGWPQFGVGAEI 287
Cdd:PRK12315 482 LKEElGIDATLINPKFITGLDEELLEK--LKEDHelVVTLEDGILDGGFGEKI 532
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
81-277 |
1.24e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 53.18 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 81 RIIDTPISEMGFAGIAVGAAMAGLRPICeFMTFNFSMQAIDQVINSA-----AKTYYMSGVAAQHS----QCFA---AWY 148
Cdd:PLN02225 424 RFFNVGMAEQHAVTFSAGLSSGGLKPFC-IIPSAFLQRAYDQVVHDVdrqrkAVRFVITSAGLVGSdgpvQCGAfdiAFM 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 149 GHCPGLKVVSPWNSEDAKGLIKSAIR-DNNPVVvlenelmygvpFEFPPEA-QSKDFLIP------IGKAKIERQGTHIT 220
Cdd:PLN02225 503 SSLPNMIAMAPADEDELVNMVATAAYvTDRPVC-----------FRFPRGSiVNMNYLVPtglpieIGRGRVLVEGQDVA 571
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 291084858 221 VVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGG 277
Cdd:PLN02225 572 LLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITVEEG 628
|
|
| |
