|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
17-590 |
2.08e-121 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 371.00 E-value: 2.08e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 17 DEKTLQVLRDMANRLRIRSIKAT---NS--STTsyliPCSNAEIMSVLFFYTMRYKQEDPENPDNDRCILSKG------- 84
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVqkaNSghPGM----PMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGhgsmlly 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 85 ---------------------------------LPFVNVATGWPGQGLGAACGMAYTGKY---------FDQASYRVFCL 122
Cdd:PRK05899 77 sllhlagydlsiddlknfrqlgsktpghpeyghTPGVETTTGPLGQGLANAVGMALAEKYlaalfnrpgLDIVDHYTYVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 123 LGDEESTEGSVWEAFAFASYYNLDNLMAIFDVNRI---GHSSSMSVEHciaiYQKRCEAFGWNTYVVDGRDVKTLCHVFS 199
Cdd:PRK05899 157 CGDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRIsidGPTEGWFTED----VKKRFEAYGWHVIEVDGHDVEAIDAAIE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 200 QAAQVrGKPTAVVAKTFKARGMPNVEDAESWYGRPMPkerADAIVKLIEsqiqtnkilvpsppiedspQINIMNicmtsp 279
Cdd:PRK05899 233 EAKAS-TKPTLIIAKTIIGKGAPNKEGTHKVHGAPLG---AEEIAAAKK-------------------ELGWDY------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 280 pvyvaddkvstQRACGLALAKLGHENDRVIVLGSDTKNCNFSDIF------KKEHPERFIQCCIAEQNMVNVALGCSTRD 353
Cdd:PRK05899 284 -----------RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 354 RTIVFAYSFAAFFTRAFDQIRLGAISQININLIGCHCGVSTGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYL 433
Cdd:PRK05899 353 GFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKY 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 434 AANTKEM--CFIRTSQAETAIIYTTQETFQIGQAKVVRhsDNDKVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIK 511
Cdd:PRK05899 433 ALERKDGpsALVLTRQNLPVLERTAQEEGVAKGGYVLR--DDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTE 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 512 PLDIAtiisnakatggriitvEDHYPEGGIGGAVCAAVSMEPNIV----------VHNLAVMDVPRSGRCNEALDFSGIS 581
Cdd:PRK05899 511 LFDEQ----------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFT 574
|
....*....
gi 125347421 582 SRHIIVAVK 590
Cdd:PRK05899 575 VENIVAAAK 583
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
286-590 |
1.45e-97 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 299.69 E-value: 1.45e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 286 DKVSTQRACGLALAKLGHENDRVIVLGSDTKNCNFSDIFKKEHPERFIQCCIAEQNMVNVALGCSTRDRtIVFAYSFAAF 365
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 366 FT-RAFDQIRL-GAISQININLIGCHCGVSTGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAANTKEMCFI 443
Cdd:COG3958 81 LTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 444 RTSQAETAIIYTTQETFQIGQAKVVRhsDNDKVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAK 523
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLR--EGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125347421 524 ATgGRIITVEDHYPEGGIGGAVCAAVSMEPNIVVHNLAVMDVP-RSGRCNEALDFSGISSRHIIVAVK 590
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAK 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
29-238 |
2.66e-73 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; 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. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 235.09 E-value: 2.66e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 29 NRLRIRSIKATNSSTTSYL-IPCSNAEIMSVLFFYTMRYKQEDPENPDNDRCILSKG----------------------- 84
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPgGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGhaspalyavlalagylpeedlkt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 85 ----------------LPFVNVATGWPGQGLGAACGMAYTGKYFdQASYRVFCLLGDEESTEGSVWEAFAFASYYNLDNL 148
Cdd:cd02012 81 frqlgsrlpghpeyglTPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 149 MAIFDVNRIGHSSSMSVEHCIAIYQKRCEAFGWNTYVVDGRDVKTLCHVFSQAAQVRGKPTAVVAKTFKARGMPNVEDAE 228
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|
gi 125347421 229 SWYGRPMPKE 238
Cdd:cd02012 240 KWHGKPLGEE 249
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
17-249 |
1.83e-61 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 204.93 E-value: 1.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 17 DEKTLQVLRDMANRLRIRSIKATNSSTTSYL-IPCSNAEIMSVLFFYTMRYKQEDPENPDNDRCILSKG----------- 84
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPgGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGhaapalyavla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 85 ----------------------------LPFVNVATGWPGQGLGAACGMAYTGKYfDQASYRVFCLLGDEESTEGSVWEA 136
Cdd:COG3959 81 ekgyfpkeelatfrklgsrlqghpdmkkTPGVEMSTGSLGQGLSVAVGMALAAKL-DGKDYRVYVLLGDGELQEGQVWEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 137 FAFASYYNLDNLMAIFDVNRI---GHSSS-MSVEHciaiYQKRCEAFGWNTYVVDGRDVKTLCHVFSQAAQVRGKPTAVV 212
Cdd:COG3959 160 AMAAAHYKLDNLIAIVDRNGLqidGPTEDvMSLEP----LAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVII 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 125347421 213 AKTFKARGMPNVEDAESW-YGRPMPKERADAIVKLIES 249
Cdd:COG3959 236 AHTVKGKGVSFMENRPKWhGKAPNDEELEQALAELEAE 273
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
293-446 |
5.68e-55 |
|
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: 183.41 E-value: 5.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 293 ACGLALAKLGHENDRVIVLGSDTKNCNFSDIFKKEHPERFIQCCIAEQNMVNVALGCSTRDrTIVFAYSFAAFFTRAFDQ 372
Cdd:cd07033 2 AFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125347421 373 IR-LGAISQININLIGCHCGVSTGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAANTKEMCFIRTS 446
Cdd:cd07033 81 IRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLP 155
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
286-446 |
4.00e-41 |
|
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: 146.93 E-value: 4.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 286 DKVSTQRACGLALAKLGHENDRVIVLGSDTKNCNFSDIFKKEHPE---RFIQCCIAEQNMVNVALGCSTRDR-TIVFAYS 361
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 362 FAAFFTRAFDQIRLG-AISQININLIGCHCGVSTGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAANTKE- 439
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
....*...
gi 125347421 440 -MCFIRTS 446
Cdd:pfam02779 161 kPVVLRLP 168
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
49-505 |
1.56e-34 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 139.04 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 49 PCSNAEIMSVLFFYTMRYKQEDPENPDNDRCILSKG----------------------------------------LPFV 88
Cdd:PTZ00089 32 PMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGhasallysmlhltgydlsmedlknfrqlgsrtpghperhiTPGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 89 NVATGWPGQGLGAACGMA---------YTGKYFDQASYRVFCLLGDEESTEGSVWEAFAFASYYNLDNLMAIFDVNRI-- 157
Cdd:PTZ00089 112 EVTTGPLGQGIANAVGLAiaekhlaakFNRPGHPIFDNYVYVICGDGCLQEGVSQEALSLAGHLGLEKLIVLYDDNKIti 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 158 -GHSSSMSVEHCiaiyQKRCEAFGWNTYVVD--GRDVKTLCHVFSQAAQVRGKPTAVVAKTFKARGmPNVEDAESWYGRP 234
Cdd:PTZ00089 192 dGNTDLSFTEDV----EKKYEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYG-SSKAGTEKVHGAP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 235 MPKERADAIVKLI--------------------------ESQIQTNKILVP--------SPPIEDSPQINIMNICMTSPP 280
Cdd:PTZ00089 267 LGDEDIAQVKELFgldpekkfhvseevrqffeqhvekkkENYEAWKKRFAKytaafpkeAQAIERRFKGELPPGWEKKLP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 281 VYVADDK-VSTQRACGLALAKLGHENDRVIVLGSDTKNCNFSDI-----FKKEHPE-RFIQCCIAEQNMVNVALGCSTRD 353
Cdd:PTZ00089 347 KYTTNDKaIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPkeandFTKASPEgRYIRFGVREHAMCAIMNGIAAHG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 354 RTIVFAYSFAAFFTRAFDQIRLGAISQININLIGCHCGVSTGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYL 433
Cdd:PTZ00089 427 GFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRPADGTETSGAYAL 506
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125347421 434 A-ANTKEMCFIRTSQAETAIIYTTQETFQIGQAKVVRHSDND-KVIVIGAGVTLHEALVAAAELSKEdISIRVI 505
Cdd:PTZ00089 507 AlANAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFTNSpQLILVASGSEVSLCVEAAKALSKE-LNVRVV 579
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
177-564 |
2.40e-34 |
|
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: 137.84 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 177 EAFGWNtYV--VDGRDVKTLCHVFSQAAQVRGkPTAVVAKTFKARGM-PNVEDAESWYGrpmpkeradaiVKLIEsqIQT 253
Cdd:COG1154 242 EELGFK-YIgpIDGHDLDALVETLRNAKDLKG-PVLLHVVTKKGKGYaPAEKDPDKFHG-----------VGPFD--PET 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 254 NKILVPSPpiedspqinimnicmtSPPVYvaddkvstQRACGLALAKLGHENDRVIVL------GSDTkncnfsDIFKKE 327
Cdd:COG1154 307 GEPKKSKS----------------SAPSY--------TDVFGDTLVELAEKDPRIVAItaampeGTGL------DKFAER 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 328 HPERFIQCCIAEQNMVNVALGCSTRDRTIVFA-YSfaAFFTRAFDQI-------RLG-------AisqininligchcGV 392
Cdd:COG1154 357 FPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAiYS--TFLQRAYDQVihdvalqNLPvtfaidrA-------------GL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 393 sTGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAANTKEMCFIRTS--QAETAIIYTTQETFQIGQAKVVRh 470
Cdd:COG1154 422 -VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPrgNGPGVELPAELEPLPIGKGEVLR- 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 471 sDNDKVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAKaTGGRIITVEDHYPEGGIGGAVCAAVS 550
Cdd:COG1154 500 -EGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAR-EHDLVVTVEEGVLAGGFGSAVLEFLA 577
|
410
....*....|....*
gi 125347421 551 -MEPNIVVHNLAVMD 564
Cdd:COG1154 578 dAGLDVPVLRLGLPD 592
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
177-564 |
2.85e-34 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 137.14 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 177 EAFGWNtYV--VDGRDVKTLCHVFSQAAQVRGkPTAVVAKTFKARGMPNVE-DAESWYGrpmpkeradaiVKLIEsqIQT 253
Cdd:PRK05444 203 EELGFN-YIgpIDGHDLDALIETLKNAKDLKG-PVLLHVVTKKGKGYAPAEaDPIKYHG-----------VGKFD--PET 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 254 NKILVPSPPiedspqinimnicmtSPPVYvaddkvstQRACGLALAKLGHENDRVIVL------GSDTkncnfsDIFKKE 327
Cdd:PRK05444 268 GEQPKSSKP---------------GKPSY--------TKVFGETLCELAEKDPKIVAItaampeGTGL------VKFSKR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 328 HPERFIQCCIAEQNMVNVALGCSTRDRTIVFA-YSfaAFFTRAFDQI-------RLG---AISQininligchCGVsTGD 396
Cdd:PRK05444 319 FPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAiYS--TFLQRAYDQVihdvalqNLPvtfAIDR---------AGL-VGA 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 397 DNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAANTKEM-CFIRTSQAE-TAIIYTTQETFQIGQAKVVRhsDND 474
Cdd:PRK05444 387 DGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGpIAIRYPRGNgVGVELPELEPLPIGKGEVLR--EGE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 475 KVIVIGAGVTLHEALVAAAELSkediSIRVIDLFTIKPLDIATIISNAKaTGGRIITVEDHYPEGGIGGAVCAAVS-MEP 553
Cdd:PRK05444 465 DVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAA-KHDLVVTVEEGAIMGGFGSAVLEFLAdHGL 539
|
410
....*....|.
gi 125347421 554 NIVVHNLAVMD 564
Cdd:PRK05444 540 DVPVLNLGLPD 550
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
463-585 |
9.91e-34 |
|
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: 124.63 E-value: 9.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 463 GQAKVVRhsDNDKVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAKATgGRIITVEDHYPEGGIG 542
Cdd:pfam02780 1 GKAEILR--EGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 125347421 543 GAVCAAVS----MEPNIVVHNLAVMDVPRSGRCNEALDFSGISSRHI 585
Cdd:pfam02780 78 SEVAAALAeeafDGLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PLN02790 |
PLN02790 |
transketolase |
31-507 |
4.98e-30 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 125.13 E-value: 4.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 31 LRIRSIKATNSSTTSYLIPCsnAEIMSVLFFYTMRYKQEDPENPDNDRCILSKG-------------------------- 84
Cdd:PLN02790 4 LAIDAVNKANSGHPGLPMGC--APMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGhgcmlqyallhlagydsvqmedlkqf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 85 ---------------LPFVNVATGWPGQGLGAACGMAYTGKY---------FDQASYRVFCLLGDEESTEGSVWEAFAFA 140
Cdd:PLN02790 82 rqwgsrtpghpenfeTPGIEVTTGPLGQGIANAVGLALAEKHlaarfnkpdHKIVDHYTYCILGDGCQMEGISNEAASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 141 SYYNLDNLMAIFDVNRI---GHSSSMSVEHCIaiyqKRCEAFGWNTYVVDG--RDVKTLCHVFSQAAQVRGKPTAVVAKT 215
Cdd:PLN02790 162 GHWGLGKLIVLYDDNHIsidGDTEIAFTEDVD----KRYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 216 FKARGMPNVEDAESWYGRPMPKERADAIVKliesqiqtnKILVPSPPIEDSPQI-------------------------- 269
Cdd:PLN02790 238 TIGYGSPNKANSYSVHGAALGEKEVDATRK---------NLGWPYEPFHVPEDVkshwskhtkegaaleaewnakfaeyk 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 270 ----------------NIMNICMTSPPVYVADDKVSTQR----ACGLALAK-----LGHENDrvivLGSDTKNC--NFSD 322
Cdd:PLN02790 309 kkypeeaaelkslisgELPSGWEKALPTFTPEDPADATRnlsqKCLNALAKvlpglIGGSAD----LASSNMTLlkDFGD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 323 iFKKEHP-ERFIQCCIAEQNMVNVALGCST-RDRTIVFAYSFAAFFTRAFDQIRLGAISQININLIGCHCGVSTGDDNPY 400
Cdd:PLN02790 385 -FQKDTPeERNVRFGVREHGMGAICNGIALhSSGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPT 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 401 HMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLA-ANTKE---MCFIRTSQAETAIiyTTQETFQIGQAKVVRHSDNDK- 475
Cdd:PLN02790 464 HQPIEHLASLRAMPNILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPNLPG--TSIEGVEKGGYVISDNSSGNKp 541
|
570 580 590
....*....|....*....|....*....|...
gi 125347421 476 -VIVIGAGVTLHEALVAAAELSKEDISIRVIDL 507
Cdd:PLN02790 542 dLILIGTGSELEIAAKAAKELRKEGKKVRVVSM 574
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
333-446 |
6.02e-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: 106.03 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 333 IQCCIAEQNMVNVALGCSTRDRTIVFAySFAAFFTRAFDQIRLGAISQININLIGCHCGVSTGDDNPYHMALEDLAMFRA 412
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVE-IFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRA 96
|
90 100 110
....*....|....*....|....*....|....
gi 125347421 413 IPNCVVFYPSDAVSTEHAVYLAANTKEMCFIRTS 446
Cdd:smart00861 97 IPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
297-550 |
3.97e-23 |
|
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: 100.48 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 297 ALAKLGHENDRVIVLGSD----------TKNcnFSDIFkkeHPERFIQCCIAEQNMVNVALGCSTRD-RTIVFaYSFAAF 365
Cdd:COG0022 13 ALREEMERDPRVFVMGEDvgkyggvfgvTKG--LQEKF---GPDRVFDTPISEAGIVGAAIGAALAGlRPVVE-IQFADF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 366 FTRAFDQI-----RLGAIS--QININLI------GchcGVSTGddnPYH-MALEdlAMFRAIPNCVVFYPS---DAVste 428
Cdd:COG0022 87 IYPAFDQIvnqaaKLRYMSggQFKVPMVirtpygG---GIGAG---AQHsQSLE--AWFAHIPGLKVVAPStpyDAK--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 429 hAVYLAA-NTKEMC-FIrtsqaETAIIYTTQE-------TFQIGQAKVVRH-SDndkVIVIGAGVTLHEALVAAAELSKE 498
Cdd:COG0022 156 -GLLKAAiRDDDPViFL-----EHKRLYRLKGevpeedyTVPLGKARVVREgTD---VTIVTYGAMVHRALEAAEELAEE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 125347421 499 DISIRVIDLFTIKPLDIATIISNAKATgGRIITVEDHYPEGGIGGAVCAAVS 550
Cdd:COG0022 227 GISAEVIDLRTLSPLDEETILESVKKT-GRLVVVDEAPRTGGFGAEIAARIA 277
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
183-545 |
1.58e-22 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 102.11 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 183 TYV--VDGRDVKTLCHVFSQAAQVRGKPTAVVAKTFKARGMPNVEDAEswygrpmpkERADAIVKLiesQIQTNKILVPS 260
Cdd:PRK12571 248 TYVgpIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEADE---------DKYHAVGKF---DVVTGLQKKSA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 261 PpiedspqinimnicmtSPPVYVAddkvstqrACGLALAKLGHENDRVIVLGSDTKNCNFSDIFKKEHPERFIQCCIAEQ 340
Cdd:PRK12571 316 P----------------SAPSYTS--------VFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 341 NMVNVALGCSTRDRTIVFAYsFAAFFTRAFDQIRLG-AISQININLIGCHCGVsTGDDNPYHMALEDLAMFRAIPNCVVF 419
Cdd:PRK12571 372 HAVTFAAGLAAAGLKPFCAV-YSTFLQRGYDQLLHDvALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVM 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 420 YPSDAVSTEHAVYLAANtkemcfirTSQAETAIIYT-----------TQETFQIGQAKVVRhsDNDKVIVIGAGVTLHEA 488
Cdd:PRK12571 450 APRDEAELRHMLRTAAA--------HDDGPIAVRFPrgegvgveipaEGTILGIGKGRVPR--EGPDVAILSVGAHLHEC 519
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 125347421 489 LVAAAELSKEDISIRVIDLFTIKPLDIATIisnAKATGGRI-ITVEDHYPEGGIGGAV 545
Cdd:PRK12571 520 LDAADLLEAEGISVTVADPRFVKPLDEALT---DLLVRHHIvVIVEEQGAMGGFGAHV 574
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
53-508 |
4.20e-20 |
|
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439792 [Multi-domain] Cd Length: 661 Bit Score: 94.30 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 53 AEIMSVLFFYTMRYkqeDPENP---DNDRCILSKG----------------------------------------LPFVN 89
Cdd:COG0021 34 APIAYVLWTKFLKH---NPANPkwpNRDRFVLSAGhgsmllysllhltgydlslddlknfrqlgsktpghpeyghTPGVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 90 VATGwP-GQGLGAACGMAYTGKY----FDQASY-----RVFCLLGDEESTEGSVWEAFAFASYYNLDNLMAIFDVNRI-- 157
Cdd:COG0021 111 TTTG-PlGQGIANAVGMAIAERHlaarFNRPGHdivdhYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIVLYDDNGIsi 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 158 -GHSS-SMSVEHciaiyQKRCEAFGWNTY-VVDGRDVKTLCHVFSQAAQVRGKPTAVVAKTFKARGMPNVEDAESWYGRP 234
Cdd:COG0021 190 dGDTDlAFSEDV-----AKRFEAYGWHVIrVEDGHDLEAIDAAIEAAKAETDKPTLIICKTIIGYGSPNKQGTAKAHGAP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 235 MPKERADAivkliesqiqTNKIL-VPSPPIEDSPQI-------------------------------------NIMNicM 276
Cdd:COG0021 265 LGAEEIAA----------TKEALgWPPEPFEVPDEVyahwraagergaaaeaewnerfaayaaaypelaaeleRRLA--G 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 277 TSP-------PVYVADDK-VSTQRACGLALAKLGHENDRVIVlGS---------DTKNcnfSDIFKKEHPE-RFIQCCIA 338
Cdd:COG0021 333 ELPedwdaalPAFEADAKgVATRKASGKVLNALAPVLPELIG-GSadlagsnktTIKG---AGSFSPEDPSgRNIHFGVR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 339 EQNM---VN-VAL--GcstrdrTIVFAysfAAFFT-----RAfdQIRLGAISQININLIGCH--CGVstGDDNPYHMALE 405
Cdd:COG0021 409 EHAMgaiMNgIALhgG------LRPYG---GTFLVfsdymRP--AIRLAALMKLPVIYVFTHdsIGL--GEDGPTHQPVE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 406 DLAMFRAIPNCVVFYPSDAVSTEHAVYLAantkemcfIRTSQAETAIIYTTQ-------ETFQIGQAK----VVRHSDND 474
Cdd:COG0021 476 QLASLRAIPNLDVIRPADANETAAAWKLA--------LERKDGPTALILSRQnlptldrTAAAAEGVAkgayVLADAEGT 547
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 125347421 475 -KVIVIGAG--VTLheALVAAAELSKEDISIRVI-----DLF 508
Cdd:COG0021 548 pDVILIATGseVSL--AVEAAELLAAEGIKVRVVsmpswELF 587
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
304-552 |
2.17e-19 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 90.04 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 304 ENDRVIVLGSDTKNCNFS-----DIFKKEHPERFIQCCIAEQNMVNVALGCSTRDRTIVFAYSFAAFFTRAFDQI----- 373
Cdd:PTZ00182 51 RDPKVFVLGEDVAQYGGVykctkGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIvneaa 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 374 --RLGAISQININL-IGCHCGVStGDDNPYH-MALEdlAMFRAIPNCVVFYPSDAVSTEhAVYLAAntkemcfIRTSQA- 448
Cdd:PTZ00182 131 kyRYMSGGQFDCPIvIRGPNGAV-GHGGAYHsQSFE--AYFAHVPGLKVVAPSDPEDAK-GLLKAA-------IRDPNPv 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 449 ---ETAIIYTTQE--------TFQIGQAKVVRHSDNdkVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIAT 517
Cdd:PTZ00182 200 vffEPKLLYRESVevvpeadyTLPLGKAKVVREGKD--VTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRET 277
|
250 260 270
....*....|....*....|....*....|....*
gi 125347421 518 IISNAKATgGRIITVEDHYPEGGIGGAVCAAVsME 552
Cdd:PTZ00182 278 IVKSVKKT-GRCVIVHEAPPTCGIGAEIAAQI-ME 310
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
25-235 |
6.08e-18 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 85.13 E-value: 6.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 25 RDMANRLRIRSIKATNSSTTSYL-IPCSNAEIMSVLFFYTMRYKQEDPENPDNDRCILSKG------------------- 84
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPgAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGhgsmllysllhltgydlsm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 85 ---------------------LPFVNVATGWPGQGLGAACGMA---------YTGKYFDQASYRVFCLLGDEESTEGSVW 134
Cdd:pfam00456 83 edlksfrqlgsktpghpefghTAGVEVTTGPLGQGIANAVGMAiaernlaatYNRPGFDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 135 EAFAFASYYNLDNLMAIFDVNRIGHSSSMSVEHCIAIyQKRCEAFGWNT-YVVDGRDVKTLCHVFSQAAQVRGKPTAVVA 213
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDT-AARFEAYGWHViEVEDGHDVEAIAAAIEEAKAEKDKPTLIKC 241
|
250 260
....*....|....*....|..
gi 125347421 214 KTFKARGMPNVEDAESWYGRPM 235
Cdd:pfam00456 242 RTVIGYGSPNKQGTHDVHGAPL 263
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
462-566 |
1.67e-17 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 85.35 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 462 IGQAKVVRHSDNDKVIVIGAGVTLheALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAKATgGRIITVEDHYPEGGI 541
Cdd:PRK11892 331 IGKARIHREGKDVTIVSFSIGMTY--ALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGV 407
|
90 100 110
....*....|....*....|....*....|...
gi 125347421 542 GGAVCAAVsME--------PNIVVHNLavmDVP 566
Cdd:PRK11892 408 GAEIAARV-MEqafdyldaPVLRVTGK---DVP 436
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
91-543 |
3.70e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 78.60 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 91 ATGWPGQGLGAACGMAyTGKYFDQASYRVFCLLGDEESTEGSVWEAFAFASYYNLDNLMAIFDVNRI--------GHSSS 162
Cdd:PLN02234 175 GTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVslptanldGPTQP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 163 MSVEHC-IAIYQKRC-----------EAFGWNtYV--VDGRDVKTLCHVFSQAAQVRG-KPTAVVAKTFKARGMPNVEDA 227
Cdd:PLN02234 254 VGALSCaLSRLQSNCgmiretsstlfEELGFH-YVgpVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 228 ESWYgrpmpkeradaivkliesqiqtNKILVPSPpiEDSPQINimNIcmtsppvyvadDKVSTQRACGL-ALAKLGHEND 306
Cdd:PLN02234 333 DDKY----------------------HGVLKFDP--ETGKQFK--NI-----------SKTQSYTSCFVeALIAEAEADK 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 307 RVIVLGSDTKNCNFSDIFKKEHPERFIQCCIAEQNMVNVALGCSTRDRTiVFAYSFAAFFTRAFDQIrlgaISQININLI 386
Cdd:PLN02234 376 DIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQV----VHDVDLQKL 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 387 GCHCGVS----TGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAA--NTKEMCFIRTSQAETAIIYTTQET- 459
Cdd:PLN02234 451 PVRFAIDraglMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCFRYHRGNGIGVSLPPGNKg 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 460 --FQIGQAKVVRhsDNDKVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAKATgGRIITVEdhyp 537
Cdd:PLN02234 531 vpLQIGRGRILR--DGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSH-EVLITVE---- 603
|
....*.
gi 125347421 538 EGGIGG 543
Cdd:PLN02234 604 EGSIGG 609
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
456-552 |
4.73e-15 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 76.69 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 456 TQETFQIGQAKVVRHSDNdkVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAKATgGRIITVEDH 535
Cdd:PRK09212 186 EEESIPIGKAAILREGSD--VTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEG 262
|
90
....*....|....*..
gi 125347421 536 YPEGGIGGAVcAAVSME 552
Cdd:PRK09212 263 WPFAGVGAEI-AALIMK 278
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
462-549 |
5.16e-13 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 70.62 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 462 IGQAKVVRHSDNdkVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAKATGgRIITVEDHYPEGGI 541
Cdd:PLN02683 219 IGKAKIEREGKD--VTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTN-RLVTVEEGWPQHGV 295
|
....*...
gi 125347421 542 GGAVCAAV 549
Cdd:PLN02683 296 GAEICASV 303
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
102-542 |
1.11e-12 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 70.80 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 102 ACGMA----YTGKYFDqasyrVFCLLGDEESTEGSVWEAFAFASYYNlDNLMAIFDVNRighsssMSV-EHCIAIYQK-- 174
Cdd:PRK12315 122 ATGLAkardLKGEKGN-----IIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQ------MSIaENHGGLYKNlk 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 175 -------RCE-----AFGWN-TYVVDGRDVKTLCHVFSQAAQVRgKPTAVVAKTFKARGM-PNVEDAESWYGRpMPKEra 240
Cdd:PRK12315 190 elrdtngQSEnnlfkAMGLDyRYVEDGNDIESLIEAFKEVKDID-HPIVLHIHTLKGKGYqPAEENKEAFHWH-MPFD-- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 241 daivkliesqIQTNKILVPSPpIEDspqinimnicmtsppvyvaddkvstqrACGLALAKLGH---ENDRVIVLGSDTKN 317
Cdd:PRK12315 266 ----------LETGQSKVPAS-GES---------------------------YSSVTLDYLLKkikEGKPVVAINAAIPG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 318 C-NFSDiFKKEHPERFIQCCIAEQNMVNVALGCSTRD-RTIVFAYSfaAFFTRAFDQirlgaISQ---ININ--LIGCHC 390
Cdd:PRK12315 308 VfGLKE-FRKKYPDQYVDVGIAEQESVAFASGIAANGaRPVIFVNS--TFLQRAYDQ-----LSHdlaINNNpaVMIVFG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 391 GVSTGDDNPyHMALEDLAMFRAIPNcvvfypsdavstehAVYLAANTKE----M-----------CFIRtsQAETAIIY- 454
Cdd:PRK12315 380 GSISGNDVT-HLGIFDIPMISNIPN--------------LVYLAPTTKEeliaMlewaltqhehpVAIR--VPEHGVESg 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 455 -TTQETFQIGQAKVVRHSdnDKVIVIGAGvTLHEALVAAAELSKEDISIR--VIDLFTIKPLDIATiISNAKATGGRIIT 531
Cdd:PRK12315 443 pTVDTDYSTLKYEVTKAG--EKVAILALG-DFYELGEKVAKKLKEELGIDatLINPKFITGLDEEL-LEKLKEDHELVVT 518
|
490
....*....|.
gi 125347421 532 VEDHYPEGGIG 542
Cdd:PRK12315 519 LEDGILDGGFG 529
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
322-543 |
2.32e-12 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 69.93 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 322 DIFKKEHPERFIQCCIAEQNMVNVALGCSTRDRTiVFAYSFAAFFTRAFDQIRLGA-ISQININLIGCHCGVsTGDDNPY 400
Cdd:PLN02582 390 NLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQVVHDVdLQKLPVRFAMDRAGL-VGADGPT 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 401 HMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAA--NTKEMCFiRTSQAETAIIYTTQET----FQIGQAKVVRhsDND 474
Cdd:PLN02582 468 HCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAaiDDRPSCF-RYPRGNGIGVQLPPNNkgipIEVGKGRILL--EGE 544
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 125347421 475 KVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIATIISNAKaTGGRIITVEdhypEGGIGG 543
Cdd:PLN02582 545 RVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAK-SHEVLITVE----EGSIGG 608
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
304-543 |
4.58e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 65.89 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 304 ENDRVIVLGSDTKNCNFSDI-FKKEHPERFIQCCIAEQNMVNVALGCSTRDRTiVFAYSFAAFFTRAFDQIRLGAISQIN 382
Cdd:PLN02225 396 EKDRDIVVVHAGMEMDASLItFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRK 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 383 -INLIGCHCGVsTGDDNPYHMALEDLAMFRAIPNCVVFYPSDAVSTEHAVYLAA--NTKEMCF--IRTSQAETAIIYTTQ 457
Cdd:PLN02225 475 aVRFVITSAGL-VGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCFrfPRGSIVNMNYLVPTG 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 458 ETFQIGQAKVVrhSDNDKVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIaTIISNAKATGGRIITVEdhyp 537
Cdd:PLN02225 554 LPIEIGRGRVL--VEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDI-KLVRDLCQNHKFLITVE---- 626
|
....*.
gi 125347421 538 EGGIGG 543
Cdd:PLN02225 627 EGCVGG 632
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
96-220 |
3.59e-10 |
|
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: 61.36 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 96 GQGLGAACGMAYTGKYFDQASYrVFCLLGDEESTEGSVWEAFAFASyynLDNLMAIFDVNRIGHSSSMSVEHCIA---IY 172
Cdd:cd02000 107 GGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFAA---LWKLPVIFVCENNGYAISTPTSRQTAgtsIA 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 125347421 173 QkRCEAFGWNTYVVDGRDVKTLCHVFSQAAQ-VR--GKPTAVVAKTFKARG 220
Cdd:cd02000 183 D-RAAAYGIPGIRVDGNDVLAVYEAAKEAVErARagGGPTLIEAVTYRLGG 232
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
92-220 |
4.85e-06 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 47.54 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 92 TGWPGQGLGAACGMAytgKYFDQA--SYRVFCLLGDEESTEGSVWEAFAFASYYNlDNLMAIFDVNRigHSSSMSVEHCI 169
Cdd:cd02007 74 TGHSSTSISAALGMA---VARDLKgkKRKVIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNE--MSISPNVGTPG 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 125347421 170 AIYqkrcEAFGWN-TYVVDGRDVKTLCHVFSQAAQVRGkPTAVVAKTFKARG 220
Cdd:cd02007 148 NLF----EELGFRyIGPVDGHNIEALIKVLKEVKDLKG-PVLLHVVTKKGKG 194
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
96-256 |
2.10e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 46.78 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 96 GQGLGAACGMAYTGKYFDQ-----ASYRV-FCLLGDEESTEGSVWEAFAFASYYNLDnlmAIFDVNR----IG---HSSS 162
Cdd:CHL00149 131 GEGIPIALGAAFQSIYRQQvlkevQPLRVtACFFGDGTTNNGQFFECLNMAVLWKLP---IIFVVENnqwaIGmahHRST 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 163 MSVEhciaIYqKRCEAFGWNTYVVDGRDVKTLCHVFSQAAQvRGK----PTAVVAKTFKARG--------MPNVEDAESW 230
Cdd:CHL00149 208 SIPE----IH-KKAEAFGLPGIEVDGMDVLAVREVAKEAVE-RARqgdgPTLIEALTYRFRGhsladpdeLRSKQEKEAW 281
|
170 180
....*....|....*....|....*..
gi 125347421 231 YGR-PMPKERADAIVKLIESQIQTNKI 256
Cdd:CHL00149 282 VARdPIKKLKSYIIDNELASQKELNKI 308
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
113-156 |
3.41e-05 |
|
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.
Pssm-ID: 238975 [Multi-domain] Cd Length: 386 Bit Score: 46.53 E-value: 3.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 125347421 113 DQASYRVFCLLGDEESTEGSVWEAFAFASYYNLDNLMAIFDVNR 156
Cdd:cd02017 144 DTSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNL 187
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
305-593 |
9.74e-05 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 44.73 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 305 NDRVIVLGSDTKNCNFS-----DIFKKEHPERFIQCCIAEQNMVNVALGCS-TRDRTIVFAYSFAaFFTRAFDQIR---- 374
Cdd:CHL00144 21 DPRVFVIGEDVGHYGGSykvtkGLHEKYGDLRVLDTPIAENSFTGMAIGAAmTGLRPIVEGMNMG-FLLLAFNQISnnag 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 375 -LGAISQININL---IGCHCGVSTGDDNPYHMALEdlAMFRAIPNCVVFypsdAVSTEHavylaaNTKEM--CFIRTSQA 448
Cdd:CHL00144 100 mLHYTSGGNFTIpivIRGPGGVGRQLGAEHSQRLE--SYFQSVPGLQIV----ACSTPY------NAKGLlkSAIRSNNP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 449 ----ETAIIYTTQET-------FQIGQAKVVRhSDNDkVIVIGAGVTLHEALVAAAELSKEDISIRVIDLFTIKPLDIAT 517
Cdd:CHL00144 168 viffEHVLLYNLKEEipdneylLPLEKAEVVR-PGND-ITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 518 IISNAKATgGRIITVEDHYPEGGIGGAVCAAVSM----EPNIVVHNLAVMDVPR--SGRCNEAldfSGISSRHIIVAVKC 591
Cdd:CHL00144 246 ISKSVKKT-HKVLIVEECMKTGGIGAELIAQINEhlfdELDAPIVRLSSQDVPTpyNGPLEEA---TVIQPAQIIEAVEQ 321
|
..
gi 125347421 592 IL 593
Cdd:CHL00144 322 II 323
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
96-215 |
2.99e-04 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 41.86 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 96 GQGLGAACGMAYTGKyfdqaSYRVFCLLGDeesteGS---VWEAFAFASYYNLDNLMAIFDvNRIGHS--SSMSVEHCIA 170
Cdd:cd00568 49 GYGLPAAIGAALAAP-----DRPVVCIAGD-----GGfmmTGQELATAVRYGLPVIVVVFN-NGGYGTirMHQEAFYGGR 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 125347421 171 I---------YQKRCEAFGWNTYVVDgrDVKTLCHVFsQAAQVRGKPTAVVAKT 215
Cdd:cd00568 118 VsgtdlsnpdFAALAEAYGAKGVRVE--DPEDLEAAL-AEALAAGGPALIEVKT 168
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
297-424 |
4.72e-03 |
|
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: 38.23 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125347421 297 ALAKLGHENDRVIVLGSDTKNCN--F---SDIFKKEHPERFIQCCIAEQNMVNVALGCSTRD-RTIVfAYSFAAFFTRAF 370
Cdd:cd07036 6 ALDEEMERDPRVVVLGEDVGDYGgvFkvtKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGlRPIV-EIMFADFALPAF 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125347421 371 DQIRLGAI-------SQININL-IGCHCGVSTGdDNPYH-MALEdlAMFRAIPNCVVFYPSDA 424
Cdd:cd07036 85 DQIVNEAAklrymsgGQFKVPIvIRGPNGGGIG-GGAQHsQSLE--AWFAHIPGLKVVAPSTP 144
|
|
| |
