|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
347-677 |
1.45e-143 |
|
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: 421.35 E-value: 1.45e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 347 EKETLVTAINKTLKAEFRHNPDTFIWGQDVAnkEKGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANGMCrfdpkihv 426
Cdd:COG0022 2 RELTYREAINEALREEMERDPRVFVMGEDVG--KYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAA-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 427 vIEG----AE--FADYFWPAVEQYV-ECTHEYWRSNGQFTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSF 499
Cdd:COG0022 72 -LAGlrpvVEiqFADFIYPAFDQIVnQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 500 ADDAAGLLRTSMRSKGFTLYLEPKALYNAVEAstfVPE-DFEVPFGKARIRRPGKDLTIITYGNTTHLCLNVAELLyKEK 578
Cdd:COG0022 151 PYDAKGLLKAAIRDDDPVIFLEHKRLYRLKGE---VPEeDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEEL-AEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 579 GWELEVIDLRTLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAEIAGIIGSELFQYLDAPIQRVGSLFTPVGFHPVLER 658
Cdd:COG0022 227 GISAEVIDLRTLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEK 306
|
330
....*....|....*....
gi 492489108 659 AILPNEETIYHAAKELLLY 677
Cdd:COG0022 307 AYLPSADRIVAAVRELLAY 325
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
10-334 |
4.55e-99 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 307.84 E-value: 4.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 10 DKETLRKWFYLMTLGRAIDEKAPSYLLQSLGwSYHAPYAGHDGIQLAMGQVFDKDtDFLFPYYRDMLTVLSAGMTAEEII 89
Cdd:COG1071 18 SKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPG-DWIFPTYRDHGHALARGVDPKELM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 90 LNGISKATDLtSGGRHMSNHFSKMEWHIENVSSATATHDLHAAGVARAMVYYGQKGVAITSHGESAASEGYVYEAINGAS 169
Cdd:COG1071 96 AELFGKATGP-SKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 170 NERLPVIFVFQDNGYGISVPKKDQTANRKVADNFSGFkNLRIIHCNGKDVFDSMNAMTEAKEYAIANRTPVIVQANCVRI 249
Cdd:COG1071 175 VWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGY-GIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 250 GSHSNSDKHTLYRDENELTYVKSADPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKAMAAPDPDPSTVKDYVLP 329
Cdd:COG1071 254 GGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYA 333
|
....*
gi 492489108 330 EPYQP 334
Cdd:COG1071 334 EPPPH 338
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
342-675 |
2.37e-96 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 300.74 E-value: 2.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 342 QNEEGEKETLVTAINKTLKAEFRHNPDTFIWGQDVANKekGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANGMCRFD 421
Cdd:PTZ00182 28 SKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQY--GGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 422 pkIHVVIEGaEFADYFWPAVEQYVECTHEY-WRSNGQFTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSFA 500
Cdd:PTZ00182 106 --LRPIAEF-MFADFIFPAFDQIVNEAAKYrYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 501 DDAAGLLRTSMRSKGFTLYLEPKALYN-AVEASTfvPEDFEVPFGKARIRRPGKDLTIITYGNTTHLCLNVAELLYKEkG 579
Cdd:PTZ00182 183 EDAKGLLKAAIRDPNPVVFFEPKLLYReSVEVVP--EADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKE-G 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 580 WELEVIDLRTLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAEIAGIIGSELFQYLDAPIQRVGSLFTPVGFHPVLERA 659
Cdd:PTZ00182 260 ISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNLEPA 339
|
330
....*....|....*.
gi 492489108 660 ILPNEETIYHAAKELL 675
Cdd:PTZ00182 340 YLPDKEKVVEAAKRVL 355
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
17-312 |
2.39e-90 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC 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 while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 282.85 E-value: 2.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 17 WFYLMTLGRAIDEKAPSYLLQSLGWSYHAPYAGHDGIQLAMGQVFDKDtDFLFPYYRDMLTVLSAGMTAEEIILNGISKA 96
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPG-DWVFPTYRDHGHALARGVDLKEMLAELFGKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 97 TDLtSGGRHMSNHFSKMEWHIENVSSATATHDLHAAGVARAMVYYGQKGVAITSHGESAASEGYVYEAINGASNERLPVI 176
Cdd:cd02000 80 TGP-CKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 177 FVFQDNGYGISVPKKDQTANRKVADNFSGFkNLRIIHCNGKDVFDSMNAMTEAKEYAIANRTPVIVQANCVRIGSHSNSD 256
Cdd:cd02000 159 FVCENNGYAISTPTSRQTAGTSIADRAAAY-GIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492489108 257 KHTLYRDENELTYVKSADPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKA 312
Cdd:cd02000 238 DPSRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
20-321 |
7.39e-55 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 189.46 E-value: 7.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 20 LMTLGRAIDEKapSYLLQSLG-WSYHAPYAGHDGIQLAMGQVFDKdTDFLFPYYRDMLTVLSAGMTAEEIILNGISKATD 98
Cdd:pfam00676 3 MMTLRRMEDAR--DALYKRQGiRGFYHLYAGQEAAQVGIAAALEP-GDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 99 LTSGGRHMsnHFSKMEWHIENVSSATATHDLHAAGVARAMVYYGQKGVAITSHGESAASEGYVYEAINGASNERLPVIFV 178
Cdd:pfam00676 80 GKGGSMHG--YYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 179 FQDNGYGISVPKKDQTANRKVADNFSGFkNLRIIHCNGKDVFDSMNAMTEAKEYAIANRTPVIVQANCVRIGSHSNSDKH 258
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADRARGY-GIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492489108 259 TLYRDENELTYV-KSADPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKAMAAPDPDPS 321
Cdd:pfam00676 237 STYRTRDEYEEVrKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
354-523 |
3.36e-47 |
|
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: 164.19 E-value: 3.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 354 AINKTLKAEFRHNPDTFIWGQDVAnkEKGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANG--MCRFDPkihvVIEGa 431
Cdd:cd07036 2 AINEALDEEMERDPRVVVLGEDVG--DYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGaaMNGLRP----IVEI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 432 EFADYFWPAVEQYV-ECTHEYWRSNGQFTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSFADDAAGLLRTS 510
Cdd:cd07036 75 MFADFALPAFDQIVnEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAA 154
|
170
....*....|...
gi 492489108 511 MRSKGFTLYLEPK 523
Cdd:cd07036 155 IRDDDPVIFLEHK 167
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
544-667 |
1.07e-40 |
|
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: 144.66 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 544 GKARIRRPGKDLTIITYGNTTHLCLNVAELLYKEkGWELEVIDLRTLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAE 623
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKE-GISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 492489108 624 IAGIIGSELFQYLDAPIQRVGSLFTPV-GFHPVLERAILPNEETI 667
Cdd:pfam02780 80 VAAALAEEAFDGLDAPVLRVGGPDFPEpGSADELEKLYGLTPEKI 124
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
47-337 |
5.10e-27 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 113.27 E-value: 5.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 47 YAGHDGIQLAMGQVFDKDtDFLFPYYRDMLTVLSAGMTAEEII--LNGISKATDLTSGGrhmSNHFSKME------WHIe 118
Cdd:PLN02269 65 YDGQEAVAVGMEAAITKE-DAIITAYRDHCTHLGRGGTVLEVFaeLMGRKDGCSRGKGG---SMHFYKKDanfyggHGI- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 119 nVSSATAThdlhAAGVARAMVYYGQKGVAITSHGESAASEGYVYEAINGASNERLPVIFVFQDNGYGISvpkkdqTANRK 198
Cdd:PLN02269 140 -VGAQVPL----GAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMG------TAEWR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 199 VADNFSGFK------NLRIihcNGKDVFDSMNAMTEAKEYAIANrTPVIVQANCVRIGSHSNSDKHTLYRDENELTYVKS 272
Cdd:PLN02269 209 AAKSPAYYKrgdyvpGLKV---DGMDVLAVKQACKFAKEHALSN-GPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQ 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492489108 273 A-DPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKAMAAPDPDPSTVKDYVLPEPYQPQKY 337
Cdd:PLN02269 285 ErDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYVKGLGVESY 350
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
401-527 |
4.57e-19 |
|
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: 83.69 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 401 FNAPIAEDYIVGTANGMCRFDPKIHVVIEGAeFADYfwpAVEQYvectheywRSNGQFTPN-ITLRLASGGYIG--GGLY 477
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFT-FFDR---AKDQI--------RSAGASGNVpVVFRHDGGGGVGedGPTH 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 492489108 478 HSQTIEGALTSLPGARIVYPSFADDAAGLLRTSMRSKGFT-LYLEPKALYN 527
Cdd:smart00861 86 HSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVvIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
347-677 |
1.45e-143 |
|
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: 421.35 E-value: 1.45e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 347 EKETLVTAINKTLKAEFRHNPDTFIWGQDVAnkEKGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANGMCrfdpkihv 426
Cdd:COG0022 2 RELTYREAINEALREEMERDPRVFVMGEDVG--KYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAA-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 427 vIEG----AE--FADYFWPAVEQYV-ECTHEYWRSNGQFTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSF 499
Cdd:COG0022 72 -LAGlrpvVEiqFADFIYPAFDQIVnQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 500 ADDAAGLLRTSMRSKGFTLYLEPKALYNAVEAstfVPE-DFEVPFGKARIRRPGKDLTIITYGNTTHLCLNVAELLyKEK 578
Cdd:COG0022 151 PYDAKGLLKAAIRDDDPVIFLEHKRLYRLKGE---VPEeDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEEL-AEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 579 GWELEVIDLRTLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAEIAGIIGSELFQYLDAPIQRVGSLFTPVGFHPVLER 658
Cdd:COG0022 227 GISAEVIDLRTLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEEAFDYLDAPVKRVTGPDTPIPYAPALEK 306
|
330
....*....|....*....
gi 492489108 659 AILPNEETIYHAAKELLLY 677
Cdd:COG0022 307 AYLPSADRIVAAVRELLAY 325
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
10-334 |
4.55e-99 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 307.84 E-value: 4.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 10 DKETLRKWFYLMTLGRAIDEKAPSYLLQSLGwSYHAPYAGHDGIQLAMGQVFDKDtDFLFPYYRDMLTVLSAGMTAEEII 89
Cdd:COG1071 18 SKEELLELYRDMLLIRRFEERALALQRQGKI-GFYHLSIGQEAAQVGAAAALRPG-DWIFPTYRDHGHALARGVDPKELM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 90 LNGISKATDLtSGGRHMSNHFSKMEWHIENVSSATATHDLHAAGVARAMVYYGQKGVAITSHGESAASEGYVYEAINGAS 169
Cdd:COG1071 96 AELFGKATGP-SKGRGGSMHFFDKELNFLGGSGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 170 NERLPVIFVFQDNGYGISVPKKDQTANRKVADNFSGFkNLRIIHCNGKDVFDSMNAMTEAKEYAIANRTPVIVQANCVRI 249
Cdd:COG1071 175 VWKLPVVFVCENNGYAISTPVERQTAVETIADRAAGY-GIPGVRVDGNDVLAVYAAVKEAVERARAGEGPTLIEAKTYRL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 250 GSHSNSDKHTLYRDENELTYVKSADPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKAMAAPDPDPSTVKDYVLP 329
Cdd:COG1071 254 GGHSTSDDPTRYRTKEEVEEWRERDPIERLRAYLLEEGLLTEEELEAIEAEAKAEVEEAVEFAEASPEPDPEELFDDVYA 333
|
....*
gi 492489108 330 EPYQP 334
Cdd:COG1071 334 EPPPH 338
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
342-675 |
2.37e-96 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 300.74 E-value: 2.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 342 QNEEGEKETLVTAINKTLKAEFRHNPDTFIWGQDVANKekGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANGMCRFD 421
Cdd:PTZ00182 28 SKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQY--GGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 422 pkIHVVIEGaEFADYFWPAVEQYVECTHEY-WRSNGQFTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSFA 500
Cdd:PTZ00182 106 --LRPIAEF-MFADFIFPAFDQIVNEAAKYrYMSGGQFDCPIVIRGPNGAVGHGGAYHSQSFEAYFAHVPGLKVVAPSDP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 501 DDAAGLLRTSMRSKGFTLYLEPKALYN-AVEASTfvPEDFEVPFGKARIRRPGKDLTIITYGNTTHLCLNVAELLYKEkG 579
Cdd:PTZ00182 183 EDAKGLLKAAIRDPNPVVFFEPKLLYReSVEVVP--EADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKE-G 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 580 WELEVIDLRTLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAEIAGIIGSELFQYLDAPIQRVGSLFTPVGFHPVLERA 659
Cdd:PTZ00182 260 ISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCFLYLEAPIKRVCGADTPFPYAKNLEPA 339
|
330
....*....|....*.
gi 492489108 660 ILPNEETIYHAAKELL 675
Cdd:PTZ00182 340 YLPDKEKVVEAAKRVL 355
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
17-312 |
2.39e-90 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC 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 while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 282.85 E-value: 2.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 17 WFYLMTLGRAIDEKAPSYLLQSLGWSYHAPYAGHDGIQLAMGQVFDKDtDFLFPYYRDMLTVLSAGMTAEEIILNGISKA 96
Cdd:cd02000 1 LYRTMVLIRRFDERLLELYRQGKIGGFYHLSIGQEAVAVGVAAALRPG-DWVFPTYRDHGHALARGVDLKEMLAELFGKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 97 TDLtSGGRHMSNHFSKMEWHIENVSSATATHDLHAAGVARAMVYYGQKGVAITSHGESAASEGYVYEAINGASNERLPVI 176
Cdd:cd02000 80 TGP-CKGRGGSMHIGDKEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 177 FVFQDNGYGISVPKKDQTANRKVADNFSGFkNLRIIHCNGKDVFDSMNAMTEAKEYAIANRTPVIVQANCVRIGSHSNSD 256
Cdd:cd02000 159 FVCENNGYAISTPTSRQTAGTSIADRAAAY-GIPGIRVDGNDVLAVYEAAKEAVERARAGGGPTLIEAVTYRLGGHSTSD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 492489108 257 KHTLYRDENELTYVKSADPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKA 312
Cdd:cd02000 238 DPSRYRTKEEVEEWKKRDPILRLRKYLIEAGILTEEELAAIEAEVKAEVEEAVEFA 293
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
354-677 |
1.02e-66 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 222.29 E-value: 1.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 354 AINKTLKAEFRHNPDTFIWGQDVAnkEKGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANG--MCRFDPkihvVIEGA 431
Cdd:PRK09212 9 ALRDAMQEEMERDPKVFLMGEEVG--EYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGaaFAGLRP----IVEFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 432 EFaDYFWPAVEQYVEC---THeyWRSNGQFTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSFADDAAGLLR 508
Cdd:PRK09212 83 TF-NFSMQAIDQIVNSaakTN--YMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 509 TSMRSKGFTLYLEPKALYNavEASTFVPEDFEVPFGKARIRRPGKDLTIITYGNTTHLCLNVAELLYKEkGWELEVIDLR 588
Cdd:PRK09212 160 TAIRDPNPVIFLENEILYG--HSHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKE-GISVEVIDLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 589 TLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAEIAGIIGSELFQYLDAPIQRVGSLFTPVGFHPVLERAILPNEETIY 668
Cdd:PRK09212 237 TLRPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDII 316
|
....*....
gi 492489108 669 HAAKELLLY 677
Cdd:PRK09212 317 EAVKKVCYR 325
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
350-672 |
4.12e-56 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 194.65 E-value: 4.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 350 TLVTAINKTLKAEFRHNPDTFIWGQDVAnkEKGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANGMCRFDPKihVVIE 429
Cdd:PLN02683 28 TVRDALNSALDEEMSADPKVFIMGEEVG--EYQGAYKITKGLLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLK--PVVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 430 GAEFaDYFWPAVEQYV-ECTHEYWRSNGQFTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSFADDAAGLLR 508
Cdd:PLN02683 104 FMTF-NFSMQAIDHIInSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 509 TSMRSKGFTLYLEPKALYNavEASTFVPE----DFEVPFGKARIRRPGKDLTIITYGNTTHLCLNVAELLYKEkGWELEV 584
Cdd:PLN02683 183 AAIRDPDPVVFLENELLYG--ESFPVSAEvldsSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKE-GISAEV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 585 IDLRTLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAEIAGIIGSELFQYLDAPIQRVGSLFTPVGFHPVLERAILPNE 664
Cdd:PLN02683 260 INLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVEESFDYLDAPVERIAGADVPMPYAANLERLALPQV 339
|
....*...
gi 492489108 665 ETIYHAAK 672
Cdd:PLN02683 340 EDIVRAAK 347
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
20-321 |
7.39e-55 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 189.46 E-value: 7.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 20 LMTLGRAIDEKapSYLLQSLG-WSYHAPYAGHDGIQLAMGQVFDKdTDFLFPYYRDMLTVLSAGMTAEEIILNGISKATD 98
Cdd:pfam00676 3 MMTLRRMEDAR--DALYKRQGiRGFYHLYAGQEAAQVGIAAALEP-GDYIIPGYRDHGNLLARGLSLEEIFAELYGRVAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 99 LTSGGRHMsnHFSKMEWHIENVSSATATHDLHAAGVARAMVYYGQKGVAITSHGESAASEGYVYEAINGASNERLPVIFV 178
Cdd:pfam00676 80 GKGGSMHG--YYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 179 FQDNGYGISVPKKDQTANRKVADNFSGFkNLRIIHCNGKDVFDSMNAMTEAKEYAIANRTPVIVQANCVRIGSHSNSDKH 258
Cdd:pfam00676 158 CENNQYGISTPAERASASTTYADRARGY-GIPGLHVDGMDPLAVYQASKFAAERARTGKGPFLIELVTYRYGGHSMSDDP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492489108 259 TLYRDENELTYV-KSADPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKAMAAPDPDPS 321
Cdd:pfam00676 237 STYRTRDEYEEVrKKKDPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKKAESAPEPHPE 300
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
296-672 |
3.37e-54 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 192.82 E-value: 3.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 296 EIADLAAKDLKAANRKAMAAPDPDPSTVKDYVLPEPYQPQKYKEGVQNEEGEKE-------TLVTAINKTLKAEFRHNPD 368
Cdd:PRK11892 82 ESASDAGAAPAAAAEAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAgtemvtmTVREALRDAMAEEMRRDED 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 369 TFIWGQDVAnkEKGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANG--MCRFDPkihvVIEGAEFaDYFWPAVEQYVE 446
Cdd:PRK11892 162 VFVMGEEVA--EYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGaaFAGLKP----IVEFMTF-NFAMQAIDQIIN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 447 C---THeyWRSNGQFTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSFADDAAGLLRTSMRSKGFTLYLEPK 523
Cdd:PRK11892 235 SaakTL--YMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIFLENE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 524 ALYnaveASTF-VP--EDFEVPFGKARIRRPGKDLTIITYGNTTHLCLNVAELLYKEkGWELEVIDLRTLIPLDKEAIFN 600
Cdd:PRK11892 313 ILY----GQSFdVPklDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKE-GIDAEVIDLRTIRPMDTETIVE 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492489108 601 SVKKTSKVLIVHEDKVFSGFGAEIAGIIGSELFQYLDAPIQRVGSLFTPVGFHPVLERAILPNEETIYHAAK 672
Cdd:PRK11892 388 SVKKTNRLVTVEEGWPQSGVGAEIAARVMEQAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVEAVK 459
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
351-677 |
1.43e-48 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 173.39 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 351 LVTAINKTLKAEFRHNPDTFIWGQDVANKekGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANG--MCRFDPkihvVI 428
Cdd:CHL00144 6 LFEALREAIDEEMARDPRVFVIGEDVGHY--GGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGaaMTGLRP----IV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 429 EGAEFAdYFWPAVEQYVE-CTHEYWRSNGQFTPNITLRlASGGyIGG--GLYHSQTIEGALTSLPGARIVYPSFADDAAG 505
Cdd:CHL00144 80 EGMNMG-FLLLAFNQISNnAGMLHYTSGGNFTIPIVIR-GPGG-VGRqlGAEHSQRLESYFQSVPGLQIVACSTPYNAKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 506 LLRTSMRSKGFTLYLEPKALYNAVEastFVP-EDFEVPFGKARIRRPGKDLTIITYGNTTHLCLNVAELLYkEKGWELEV 584
Cdd:CHL00144 157 LLKSAIRSNNPVIFFEHVLLYNLKE---EIPdNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLV-EKGYDPEI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 585 IDLRTLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAEIAGIIGSELFQYLDAPIQRVGSLFTPVGFHPVLERAILPNE 664
Cdd:CHL00144 233 IDLISLKPLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEHLFDELDAPIVRLSSQDVPTPYNGPLEEATVIQP 312
|
330
....*....|...
gi 492489108 665 ETIYHAAKELLLY 677
Cdd:CHL00144 313 AQIIEAVEQIITN 325
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
354-523 |
3.36e-47 |
|
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: 164.19 E-value: 3.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 354 AINKTLKAEFRHNPDTFIWGQDVAnkEKGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANG--MCRFDPkihvVIEGa 431
Cdd:cd07036 2 AINEALDEEMERDPRVVVLGEDVG--DYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGaaMNGLRP----IVEI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 432 EFADYFWPAVEQYV-ECTHEYWRSNGQFTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSFADDAAGLLRTS 510
Cdd:cd07036 75 MFADFALPAFDQIVnEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAA 154
|
170
....*....|...
gi 492489108 511 MRSKGFTLYLEPK 523
Cdd:cd07036 155 IRDDDPVIFLEHK 167
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
544-667 |
1.07e-40 |
|
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: 144.66 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 544 GKARIRRPGKDLTIITYGNTTHLCLNVAELLYKEkGWELEVIDLRTLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAE 623
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKE-GISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 492489108 624 IAGIIGSELFQYLDAPIQRVGSLFTPV-GFHPVLERAILPNEETI 667
Cdd:pfam02780 80 VAAALAEEAFDGLDAPVLRVGGPDFPEpGSADELEKLYGLTPEKI 124
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
47-337 |
5.10e-27 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 113.27 E-value: 5.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 47 YAGHDGIQLAMGQVFDKDtDFLFPYYRDMLTVLSAGMTAEEII--LNGISKATDLTSGGrhmSNHFSKME------WHIe 118
Cdd:PLN02269 65 YDGQEAVAVGMEAAITKE-DAIITAYRDHCTHLGRGGTVLEVFaeLMGRKDGCSRGKGG---SMHFYKKDanfyggHGI- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 119 nVSSATAThdlhAAGVARAMVYYGQKGVAITSHGESAASEGYVYEAINGASNERLPVIFVFQDNGYGISvpkkdqTANRK 198
Cdd:PLN02269 140 -VGAQVPL----GAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENNHYGMG------TAEWR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 199 VADNFSGFK------NLRIihcNGKDVFDSMNAMTEAKEYAIANrTPVIVQANCVRIGSHSNSDKHTLYRDENELTYVKS 272
Cdd:PLN02269 209 AAKSPAYYKrgdyvpGLKV---DGMDVLAVKQACKFAKEHALSN-GPIVLEMDTYRYHGHSMSDPGSTYRTRDEISGVRQ 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492489108 273 A-DPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKAMAAPDPDPSTVKDYVLPEPYQPQKY 337
Cdd:PLN02269 285 ErDPIERVRKLLLAHELATEAELKDIEKEIRKEVDDAVAKAKESPMPDPSELFTNVYVKGLGVESY 350
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
480-644 |
2.27e-22 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 98.23 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 480 QTIE--GALTSLPGARIVYPSFADDAAGLLRTSMRSKGFTlYLepKALYNAVEAstFVPEDFEVPFGKARIRRPGKDLTI 557
Cdd:COG3958 119 QALEdiALMRALPNMTVIVPADAVETEAAVRAAAEHDGPV-YL--RLGRGAVPV--VYDEDYEFEIGKARVLREGKDVTI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 558 ITYGNTTHLCLNVAELLyKEKGWELEVIDLRTLIPLDKEAIFNSVKKTSKVLIVHEDKVFSGFGAEIAGIigseLFQYLD 637
Cdd:COG3958 194 IATGIMVAEALEAAELL-AKEGISARVINMHTIKPLDEEAILKAARKTGAVVTAEEHSIIGGLGSAVAEV----LAENYP 268
|
....*..
gi 492489108 638 APIQRVG 644
Cdd:COG3958 269 VPLRRIG 275
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
353-527 |
3.36e-21 |
|
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: 91.07 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 353 TAINKTLKAEFRHNPDTFIWGQDVAnkekGGVFNITKGMQQEFGIERVFNAPIAEDYIVGTANGMCRFDPKIHVViEG-- 430
Cdd:pfam02779 7 KASGEALAELAKRDPRVVGGGADLA----GGTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGPLLPPV-EAtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 431 AEFADYFWPAVEQYVEctheYWRSNgqfTPNITLRLASGGYIGGGLYHSQTIEGALTSLPGARIVYPSFADDAAGLLRTS 510
Cdd:pfam02779 82 SDFLNRADDAIRHGAA----LGKLP---VPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAA 154
|
170
....*....|....*....
gi 492489108 511 MRSKGF--TLYLEPKALYN 527
Cdd:pfam02779 155 IRRDGRkpVVLRLPRQLLR 173
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
401-527 |
4.57e-19 |
|
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: 83.69 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 401 FNAPIAEDYIVGTANGMCRFDPKIHVVIEGAeFADYfwpAVEQYvectheywRSNGQFTPN-ITLRLASGGYIG--GGLY 477
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFT-FFDR---AKDQI--------RSAGASGNVpVVFRHDGGGGVGedGPTH 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 492489108 478 HSQTIEGALTSLPGARIVYPSFADDAAGLLRTSMRSKGFT-LYLEPKALYN 527
Cdd:smart00861 86 HSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVvIRLERKSLYR 136
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
486-644 |
4.39e-15 |
|
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: 78.90 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 486 LTSLPGARIVYPSFADDAAGLLRTSMRSKGftlylePKAL-Y---NAVEAStfVPEDFE-VPFGKARIRRPGKDLTIITY 560
Cdd:COG1154 438 LRCIPNMVIMAPKDENELRHMLYTALAYDG------PTAIrYprgNGPGVE--LPAELEpLPIGKGEVLREGKDVAILAF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 561 GNTTHLCLNVAELLyKEKGWELEVIDLRTLIPLDKEAIFNSVKKTSKVLIVhEDKVfsgfgaeIAGIIGSELFQYL---- 636
Cdd:COG1154 510 GTMVAEALEAAERL-AAEGISATVVDARFVKPLDEELILELAREHDLVVTV-EEGV-------LAGGFGSAVLEFLadag 580
|
....*....
gi 492489108 637 -DAPIQRVG 644
Cdd:COG1154 581 lDVPVLRLG 589
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
11-331 |
6.42e-15 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 77.68 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 11 KETLRKWFYLMTLGRAIDEKAPSYLLQSLGWSYHAPYAGHDGIQLAMGQVFDKDtDFLFPYYRDMLTVLSAGMTAEEIIL 90
Cdd:PLN02374 85 REEGLELYEDMVLGRSFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGFIKLLKKD-DSVVSTYRDHVHALSKGVPARAVMS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 91 NGISKATDL---TSGGRHMsnhFSKMEWHI-------ENVSSATathdlhaaGVARAMVY-------YGQKGVAITSHGE 153
Cdd:PLN02374 164 ELFGKATGCcrgQGGSMHM---FSKEHNLLggfafigEGIPVAT--------GAAFSSKYrrevlkeESCDDVTLAFFGD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 154 SAASEGYVYEAINGASNERLPVIFVFQDNGYGISVPKKDQTANRKVADNFSGFkNLRIIHCNGKDVFDSMNAMTEAKEYA 233
Cdd:PLN02374 233 GTCNNGQFFECLNMAALWKLPIVFVVENNLWAIGMSHLRATSDPEIWKKGPAF-GMPGVHVDGMDVLKVREVAKEAIERA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 234 IANRTPVIVQANCVRIGSHSNSDKHTLyRDENELTYVKSADPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKAM 313
Cdd:PLN02374 312 RRGEGPTLVECETYRFRGHSLADPDEL-RDPAEKAHYAARDPIAALKKYLIENGLATEAELKAIEKKIDEVVEDAVEFAD 390
|
330
....*....|....*...
gi 492489108 314 AAPDPDPSTVKDYVLPEP 331
Cdd:PLN02374 391 ASPLPPRSQLLENVFADP 408
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
10-327 |
2.31e-14 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 74.90 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 10 DKETLRKWFYLMTLGRAIDEKAPSYLLQSLGWSYHAPYAGHDGIQLAMGQVFDKdTDFLFPYYRDMLTVLSAGMTAEEII 89
Cdd:CHL00149 18 NSMWLLVLYEDMLLGRNFEDMCAQMYYRGKMFGFVHLYNGQEAVSTGVIKLLAE-TDYVCSTYRDHVHALSKGVPPKNVM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 90 LNGISKATDlTSGGRHMSNH-FSKMEWHI-------ENVSSATathdlhaaGVARAMVYYGQ-------KGVAITSHGES 154
Cdd:CHL00149 97 AELFGKETG-CSRGRGGSMHiFSAPHNFLggfafigEGIPIAL--------GAAFQSIYRQQvlkevqpLRVTACFFGDG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 155 AASEGYVYEAINGASNERLPVIFVFQDNGYGISVPKKDQTANRKVADNFSGFkNLRIIHCNGKDVFDSMNAMTEAKEYAI 234
Cdd:CHL00149 168 TTNNGQFFECLNMAVLWKLPIIFVVENNQWAIGMAHHRSTSIPEIHKKAEAF-GLPGIEVDGMDVLAVREVAKEAVERAR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 235 ANRTPVIVQANCVRIGSHSNSDKHTLyRDENELTYVKSADPLYKFHRMLIRYGRFTEEELKEIADLAAKDLKAANRKAMA 314
Cdd:CHL00149 247 QGDGPTLIEALTYRFRGHSLADPDEL-RSKQEKEAWVARDPIKKLKSYIIDNELASQKELNKIQREVKIEIEQAVQFAIS 325
|
330
....*....|...
gi 492489108 315 APDPDPSTVKDYV 327
Cdd:CHL00149 326 SPEPNISDLKKYL 338
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
535-625 |
4.28e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 65.87 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 535 VPEDFEVPFGKARIRRPGKDLTIITYGNTTHLCLNVAELLYkekgwELEVIDLRTLIPLDKEAIFNSVKKTSKVLIVHED 614
Cdd:PRK05444 446 LPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA-----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEG 520
|
90
....*....|.
gi 492489108 615 KVFSGFGAEIA 625
Cdd:PRK05444 521 AIMGGFGSAVL 531
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
104-631 |
3.94e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 62.82 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 104 RHMSNHfskmEWhIENVSSATAthdLHAA-GVARAMVYYGQKGVAITSHGESAASEGYVYEAINGASNERLPVIFVFQDN 182
Cdd:PRK12571 108 RSESEY----DP-FGAAHSSTS---ISAAlGFAKARALGQPDGDVVAVIGDGSLTAGMAYEALNNAGAADRRLIVILNDN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 183 GYGISVPkkdqtanrkVADNFSGFKNLRIihcngKDVFDSMNAMTEAkeyaIANRTPVIVQ--ANCVRIGSHSNSDKHTL 260
Cdd:PRK12571 180 EMSIAPP---------VGALAAYLSTLRS-----SDPFARLRAIAKG----VEERLPGPLRdgARRARELVTGMIGGGTL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 261 YrDENELTYVKSADPlykfHRMlirygrfteeelkeiadlaaKDLKAANRKAMAAPDpDPSTVkdYVLPEP---YQPQKY 337
Cdd:PRK12571 242 F-EELGFTYVGPIDG----HDM--------------------EALLSVLRAARARAD-GPVLV--HVVTEKgrgYAPAEA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 338 KE----GVQneegeKETLVTAINKTLKAEFRHNPDTFiwGQDVAN--KEKGGVFNITKGMQQEFGI--------ERVFNA 403
Cdd:PRK12571 294 DEdkyhAVG-----KFDVVTGLQKKSAPSAPSYTSVF--GEELTKeaAEDSDIVAITAAMPLGTGLdklqkrfpNRVFDV 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 404 PIAEDYIVGTANGMCRFDPKIHVVIegaeFADYFWPAVEQYVectHEYWRSNgqfTPnITLRLASGGYIG--GGLYHSQT 481
Cdd:PRK12571 367 GIAEQHAVTFAAGLAAAGLKPFCAV----YSTFLQRGYDQLL---HDVALQN---LP-VRFVLDRAGLVGadGATHAGAF 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 482 IEGALTSLPGARIVYPSFADDAAGLLRTSM-RSKGFTLYLEPKALYNAVEastfVPEDFEV-PFGKARIRRPGKDLTIIT 559
Cdd:PRK12571 436 DLAFLTNLPNMTVMAPRDEAELRHMLRTAAaHDDGPIAVRFPRGEGVGVE----IPAEGTIlGIGKGRVPREGPDVAILS 511
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492489108 560 YGNTTHLCLNVAELLYKEkGWELEVIDLRTLIPLDkEAIFNSVKKTSKVLIVHEDKVFSGFGAEIAGIIGSE 631
Cdd:PRK12571 512 VGAHLHECLDAADLLEAE-GISVTVADPRFVKPLD-EALTDLLVRHHIVVIVEEQGAMGGFGAHVLHHLADT 581
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
393-629 |
6.38e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 52.79 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 393 QEFGIERVFNAPIAEDYIVGTANGMCRFDPKIHVVIEGAefadYFWPAVEQYVectHEYWRSNGQftpnITLRLASGGYI 472
Cdd:PLN02225 418 QERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSA----FLQRAYDQVV---HDVDRQRKA----VRFVITSAGLV 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 473 GG-GLYHSQTIEGA-LTSLPGARIVYPSFADDAAGLLRTSM----RSKGFTLylePKAlyNAVEASTFVPEDFEVPFGKA 546
Cdd:PLN02225 487 GSdGPVQCGAFDIAfMSSLPNMIAMAPADEDELVNMVATAAyvtdRPVCFRF---PRG--SIVNMNYLVPTGLPIEIGRG 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 547 RIRRPGKDLTIITYGNTTHLCLNVAELLYKeKGWELEVIDLRTLIPLDKEAIfNSVKKTSKVLIVHEDKVFSGFGAEIAG 626
Cdd:PLN02225 562 RVLVEGQDVALLGYGAMVQNCLHAHSLLSK-LGLNVTVADARFCKPLDIKLV-RDLCQNHKFLITVEEGCVGGFGSHVAQ 639
|
...
gi 492489108 627 IIG 629
Cdd:PLN02225 640 FIA 642
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
536-624 |
7.11e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 52.41 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 536 PEDFEVPF--GKARIRRPGKDLTIITYGNTTHLCLNVAELLyKEKGWELEVIDLRTLIPLDKeAIFNSVKKTSKVLIVHE 613
Cdd:PLN02234 526 PGNKGVPLqiGRGRILRDGERVALLGYGSAVQRCLEAASML-SERGLKITVADARFCKPLDV-ALIRSLAKSHEVLITVE 603
|
90
....*....|.
gi 492489108 614 DKVFSGFGAEI 624
Cdd:PLN02234 604 EGSIGGFGSHV 614
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
544-625 |
7.20e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 49.13 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 544 GKARIRRPGKDLTIITYGNTTHLCLNVAELLyKEKGWELEVIDLRTLIPLDKeAIFNSVKKTSKVLIVHEDKVFSGFGAE 623
Cdd:PLN02582 535 GKGRILLEGERVALLGYGTAVQSCLAAASLL-ERHGLSATVADARFCKPLDR-ALIRSLAKSHEVLITVEEGSIGGFGSH 612
|
..
gi 492489108 624 IA 625
Cdd:PLN02582 613 VA 614
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
527-630 |
1.93e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 44.61 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 527 NAVEASTFVPEDFEVPfgKARIRRPGKDLTIITYGNTTHLCLNVAELLYKEKGWELEVIDLRTLIPLDKEAIfNSVKKTS 606
Cdd:PRK12315 437 HGVESGPTVDTDYSTL--KYEVTKAGEKVAILALGDFYELGEKVAKKLKEELGIDATLINPKFITGLDEELL-EKLKEDH 513
|
90 100
....*....|....*....|....*
gi 492489108 607 KVLIVHEDKVFSG-FGAEIAGIIGS 630
Cdd:PRK12315 514 ELVVTLEDGILDGgFGEKIARYYGN 538
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
354-515 |
3.48e-04 |
|
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: 41.66 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 354 AINKTLKAEFRHNPDTFIWGQDVANkekggvFNITKGMQQEFGiERVFNAPIAEDYIVGTANGMCRFDpKIHVVIEGAEF 433
Cdd:cd07033 2 AFGEALLELAKKDPRIVALSADLGG------STGLDKFAKKFP-DRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 434 ADYFWPAVEQYVeCTHEYwrsngqftpNITLRLASGGYIGGGLYHS-QTIE--GALTSLPGARIVYPSFADDAAGLLRTS 510
Cdd:cd07033 74 LQRAYDQIRHDV-ALQNL---------PVKFVGTHAGISVGEDGPThQGIEdiALLRAIPNMTVLRPADANETAAALEAA 143
|
....*
gi 492489108 511 MRSKG 515
Cdd:cd07033 144 LEYDG 148
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
480-596 |
6.64e-03 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 39.73 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492489108 480 QTIE--GALTSLPGARIVYPSFADDAAGLLRTSMRSKGftlylEPKALYNAVEASTFVPE--DFEVPFGKARIRRPGKDL 555
Cdd:PRK05899 401 QPVEqlASLRAIPNLTVIRPADANETAAAWKYALERKD-----GPSALVLTRQNLPVLERtaQEEGVAKGGYVLRDDPDV 475
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 492489108 556 TIITYGNTTHLCLNVAELLyKEKGWELEVIDLRTLIPLDKE 596
Cdd:PRK05899 476 ILIATGSEVHLALEAADEL-EAEGIKVRVVSMPSTELFDEQ 515
|
|
| |
