|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
9-620 |
4.87e-169 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 494.27 E-value: 4.87e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 9 DVKTVQVLRDTANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWV 88
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 89 EVG-DISESDLLNLRKLHSDLERHPTPR-LPFVDVATGSLGQGLGTACGMAYTGKYLDK---------ASYRVFCLMGDG 157
Cdd:PRK05899 81 LAGyDLSIDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGLANAVGMALAEKYLAAlfnrpgldiVDHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 158 ESSEGSVWEAFAFASHYNLDNLVAVFDVNRLGQSGPAPLEHGADI---YqnccEAFGWNTYLVDGHDVEALCQAFWQASQ 234
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVkkrF----EAYGWHVIEVDGHDVEAIDAAIEEAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 235 VKnKPTAIVAKTFKGRGIPNIEDAENWHGKPVPKERADAivkliesqiqTNENLipkspvedspqisitdikmtsppayk 314
Cdd:PRK05899 237 ST-KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAA----------AKKEL-------------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 315 vgdKIATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEIF------RKEHPERFIECIIAEQNMVSVALGCATRGRTIA 388
Cdd:PRK05899 280 ---GWDYRKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIP 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 389 FAGAFAAFFTRAFDQLRMGAISQANINLIGSHCGVSTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAA-N 467
Cdd:PRK05899 357 FGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeR 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 468 TKGMCFIRTSQPETAVIY-TPQENFEIGQAKVVRHGvnDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDA 546
Cdd:PRK05899 437 KDGPSALVLTRQNLPVLErTAQEEGVAKGGYVLRDD--PDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDE 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 547 AtiissakatggrvitvEDHYREGGIGEAVCAAVSREPDIL----------VHQLAVSGVPQRGKTSELLDMFGISTRHI 616
Cdd:PRK05899 515 Q----------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENI 578
|
....
gi 133778974 617 IAAV 620
Cdd:PRK05899 579 VAAA 582
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
21-269 |
1.24e-125 |
|
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: 371.07 E-value: 1.24e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 21 NRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVGDISESDLLN 100
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 101 LRKLHSDLERHPTPRL-PFVDVATGSLGQGLGTACGMAYTGKYLdKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNL 179
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 180 VAVFDVNRLGQSGPAPLEHGADIYQNCCEAFGWNTYLVDGHDVEALCQAFWQASQVKNKPTAIVAKTFKGRGIPNIEDAE 259
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|
gi 133778974 260 NWHGKPVPKE 269
Cdd:cd02012 240 KWHGKPLGEE 249
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
11-283 |
5.75e-107 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 323.95 E-value: 5.75e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 11 KTVQVLRDTANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEV 90
Cdd:COG3959 3 EDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 91 GDISESDLLNLRKLHSDLERHPTP-RLPFVDVATGSLGQGLGTACGMAYTGKyLDKASYRVFCLMGDGESSEGSVWEAFA 169
Cdd:COG3959 83 GYFPKEELATFRKLGSRLQGHPDMkKTPGVEMSTGSLGQGLSVAVGMALAAK-LDGKDYRVYVLLGDGELQEGQVWEAAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 170 FASHYNLDNLVAVFDVNRLGQSGPA----PLEHGADIYqnccEAFGWNTYLVDGHDVEALCQAFWQASQVKNKPTAIVAK 245
Cdd:COG3959 162 AAAHYKLDNLIAIVDRNGLQIDGPTedvmSLEPLAEKW----EAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAH 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 133778974 246 TFKGRGIPNIEDAENWHGKPVPKERADAIVKLIESQIQ 283
Cdd:COG3959 238 TVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELG 275
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
317-620 |
9.34e-103 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 314.33 E-value: 9.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 317 DKIATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHPERFIECIIAEQNMVSVALGCATRG------------ 384
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGkipfvstfapfl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 385 --RTIafagafaafftrafDQLRM-GAISQANINLIGSHCGVSTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHA 461
Cdd:COG3958 82 tgRAY--------------EQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 462 IYLAANTKGMCFIRTSQPETAVIYTPQENFEIGQAKVVRHGvnDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTI 541
Cdd:COG3958 148 VRAAAEHDGPVYLRLGRGAVPVVYDEDYEFEIGKARVLREG--KDVTIIATGIMVAEALEAAELLAKEGISARVINMHTI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 542 KPLDAATIISSAKATgGRVITVEDHYREGGIGEAVCAAVSREPDILVHQLAVSGVP-QRGKTSELLDMFGISTRHIIAAV 620
Cdd:COG3958 226 KPLDEEAILKAARKT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAA 304
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
323-477 |
3.04e-52 |
|
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: 176.48 E-value: 3.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 323 KTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHPERFIECIIAEQNMVSVALGCATRG-------------RTIaf 389
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGlkpfvstfsfflqRAY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 390 agafaafftrafDQLR-MGAISQANINLIGSHCGVSTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANT 468
Cdd:cd07033 79 ------------DQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEY 146
|
....*....
gi 133778974 469 KGMCFIRTS 477
Cdd:cd07033 147 DGPVYIRLP 155
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
20-536 |
8.89e-51 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 186.42 E-value: 8.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 20 ANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVG-DISESDL 98
Cdd:PTZ00089 10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGyDLSMEDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 99 LNLRKLHSDL----ERHPTPRlpfVDVATGSLGQGLGTACGMAYTGKYLdKASY----------RVFCLMGDGESSEGSV 164
Cdd:PTZ00089 90 KNFRQLGSRTpghpERHITPG---VEVTTGPLGQGIANAVGLAIAEKHL-AAKFnrpghpifdnYVYVICGDGCLQEGVS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 165 WEAFAFASHYNLDNLVAVFDVNRLGQSGPAPLEHGADIYQNcCEAFGWNTYLVD--GHDVEALCQAFWQASQVKNKPTAI 242
Cdd:PTZ00089 166 QEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKK-YEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 243 VAKTFKGRGiPNIEDAENWHGKPVPKERADAIVKLI--------------------------ESQIQTNENL------IP 290
Cdd:PTZ00089 245 IVKTTIGYG-SSKAGTEKVHGAPLGDEDIAQVKELFgldpekkfhvseevrqffeqhvekkkENYEAWKKRFakytaaFP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 291 KSPVEDSPQIS---ITDIKMTSPPAYKVGDKIATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEI-----FRKEHPE- 361
Cdd:PTZ00089 324 KEAQAIERRFKgelPPGWEKKLPKYTTNDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPkeandFTKASPEg 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 362 RFIECIIAEQNMVSVALGCATRGRTIAFAGAFAAFFTRAFDQLRMGAISQANINLIGSHCGVSTGEDGVSQMALEDLAMF 441
Cdd:PTZ00089 404 RYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 442 RSIPNCTVFYPSDAISTEHAIYLA-ANTKG---MCFIRTSQPetaviytPQENFEIGQ----AKVVRHGVND-KVTVIGA 512
Cdd:PTZ00089 484 RATPNLLVIRPADGTETSGAYALAlANAKTptiLCLSRQNTP-------PLPGSSIEGvlkgAYIVVDFTNSpQLILVAS 556
|
570 580
....*....|....*....|....
gi 133778974 513 GVTLHEALEAADHLSQQgISVRVI 536
Cdd:PTZ00089 557 GSEVSLCVEAAKALSKE-LNVRVV 579
|
|
| PLN02790 |
PLN02790 |
transketolase |
45-536 |
2.38e-48 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 179.45 E-value: 2.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 45 AAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVG--DISESDLLNLRKLHSDLERHP----TPRlpf 118
Cdd:PLN02790 23 CAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGydSVQMEDLKQFRQWGSRTPGHPenfeTPG--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 119 VDVATGSLGQGLGTACGMAYTGKYL---------DKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDVNRLG 189
Cdd:PLN02790 100 IEVTTGPLGQGIANAVGLALAEKHLaarfnkpdhKIVDHYTYCILGDGCQMEGISNEAASLAGHWGLGKLIVLYDDNHIS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 190 QSGPAPLEHGADIYQNcCEAFGWNTYLVDG--HDVEALCQAFWQASQVKNKPTAIVAKTFKGRGIPNIEDAENWHGKPVP 267
Cdd:PLN02790 180 IDGDTEIAFTEDVDKR-YEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTTTIGYGSPNKANSYSVHGAALG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 268 KERADAivkliesqiqTNENL-IPKSPVEDSPQI--------------------------------------SITDIKMT 308
Cdd:PLN02790 259 EKEVDA----------TRKNLgWPYEPFHVPEDVkshwskhtkegaaleaewnakfaeykkkypeeaaelksLISGELPS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 309 ----SPPAYKVGDKI-ATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEI-----FRKEHP-ERFIECIIAEQNMVSVA 377
Cdd:PLN02790 329 gwekALPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLkdfgdFQKDTPeERNVRFGVREHGMGAIC 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 378 LG-----------CAT--------RGrtiafagafaafftrafdQLRMGAISQANINLIGSHCGVSTGEDGVSQMALEDL 438
Cdd:PLN02790 409 NGialhssglipyCATffvftdymRA------------------AMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 439 AMFRSIPNCTVFYPSDAISTEHAIYLA-ANTKG---MCFIRTSQPETAViyTPQENFEIGqAKVVRHGVNDK---VTVIG 511
Cdd:PLN02790 471 ASLRAMPNILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPNLPG--TSIEGVEKG-GYVISDNSSGNkpdLILIG 547
|
570 580
....*....|....*....|....*
gi 133778974 512 AGVTLHEALEAADHLSQQGISVRVI 536
Cdd:PLN02790 548 TGSELEIAAKAAKELRKEGKKVRVV 572
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
208-621 |
6.06e-48 |
|
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: 177.90 E-value: 6.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 208 EAFGWNtYL--VDGHDVEALCQAFWQASQVKnKPTAIVAKTFKGRG-IPNIEDAENWHGkpVPKeradaivklIEsqIQT 284
Cdd:COG1154 242 EELGFK-YIgpIDGHDLDALVETLRNAKDLK-GPVLLHVVTKKGKGyAPAEKDPDKFHG--VGP---------FD--PET 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 285 NEnlIPKSPvedspqisitdikmTSPPAYkvgdkiatQKTYGLALAKLGRANERVIV-----LSGDTMNstfseIFRKEH 359
Cdd:COG1154 307 GE--PKKSK--------------SSAPSY--------TDVFGDTLVELAEKDPRIVAitaamPEGTGLD-----KFAERF 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 360 PERFIECIIAEQNMVSVALGCATRG-------------RTIafagafaafftrafDQLRMG----------AISQANInl 416
Cdd:COG1154 358 PDRFFDVGIAEQHAVTFAAGLATEGlkpvvaiystflqRAY--------------DQVIHDvalqnlpvtfAIDRAGL-- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 417 igshcgvsTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANTKGMCFIR---TSQPETAVIYTPQEnFEI 493
Cdd:COG1154 422 --------VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRyprGNGPGVELPAELEP-LPI 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 494 GQAKVVRHGvnDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKaTGGRVITVEDHYREGGIG 573
Cdd:COG1154 493 GKGEVLREG--KDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAR-EHDLVVTVEEGVLAGGFG 569
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 133778974 574 EAVCAAVSRE-PDILVHQLavsGVPQR----GKTSELLDMFGISTRHIIAAVT 621
Cdd:COG1154 570 SAVLEFLADAgLDVPVLRL---GLPDRfiehGSRAELLAELGLDAEGIARAIL 619
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
133-624 |
1.34e-46 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 173.34 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 133 ACGMAYTGKYLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDvNRLGQSGPapleHGAdIY--------Q 204
Cdd:PRK05444 126 ALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEALNNAGDLKSDLIVILND-NEMSISPN----VGA-LSnylarlrsS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 205 NCCEAFGWNtYL--VDGHDVEALCQAFwqaSQVKN--KPTAIVAKTFKGRGIPNIE-DAENWHGkpVPKeradaivklie 279
Cdd:PRK05444 200 TLFEELGFN-YIgpIDGHDLDALIETL---KNAKDlkGPVLLHVVTKKGKGYAPAEaDPIKYHG--VGK----------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 280 SQIQTNENLIPKSPvedspqisitdikmtSPPAYkvgdkiatQKTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEH 359
Cdd:PRK05444 263 FDPETGEQPKSSKP---------------GKPSY--------TKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 360 PERFIECIIAEQNMVSVALGCATRG-------------RTIafagafaafftrafDQLRMG-AISQANINLIGSHCGVsT 425
Cdd:PRK05444 320 PDRYFDVGIAEQHAVTFAAGLATEGlkpvvaiystflqRAY--------------DQVIHDvALQNLPVTFAIDRAGL-V 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 426 GEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLA-ANTKGMCFIRTsqP---ETAVIYTPQENFEIGQAKVVRH 501
Cdd:PRK05444 385 GADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRY--PrgnGVGVELPELEPLPIGKGEVLRE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 502 GvnDKVTVIGAGVTLHEALEAADHLSqqgiSVRVIDPFTIKPLDAATIISSAKaTGGRVITVEDHYREGGIGEAVCAAVS 581
Cdd:PRK05444 463 G--EDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAA-KHDLVVTVEEGAIMGGFGSAVLEFLA 535
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 133778974 582 RE-PDILVHQLavsGVPQR----GKTSELLDMFGISTRHIIAAVTLTL 624
Cdd:PRK05444 536 DHgLDVPVLNL---GLPDEfidhGSREELLAELGLDAEGIARRILELL 580
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
44-536 |
4.70e-45 |
|
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: 170.19 E-value: 4.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 44 SAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVG-DISESDLLNLRKLHSDL----ERHPTprlPF 118
Cdd:COG0021 32 GMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGyDLSLDDLKNFRQLGSKTpghpEYGHT---PG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 119 VDVATGSLGQGLGTACGMAYTGKYL----DKASY-----RVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDVNRLG 189
Cdd:COG0021 109 VETTTGPLGQGIANAVGMAIAERHLaarfNRPGHdivdhYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIVLYDDNGIS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 190 QSGPAPLEHGADI---YqnccEAFGWNTYLV-DGHDVEALCQAFWQASQVKNKPTAIVAKTFKGRGIPNIEDAENWHGKP 265
Cdd:COG0021 189 IDGDTDLAFSEDVakrF----EAYGWHVIRVeDGHDLEAIDAAIEAAKAETDKPTLIICKTIIGYGSPNKQGTAKAHGAP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 266 ---------------------VP---KERADAIV-----------KLIESQIQTN-------ENLI-PKSPVEDSPQIsi 302
Cdd:COG0021 265 lgaeeiaatkealgwppepfeVPdevYAHWRAAGergaaaeaewnERFAAYAAAYpelaaelERRLaGELPEDWDAAL-- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 303 tdikmtspPAYKVGDK-IATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEI-----FRKEHPE-RFIECIIAEQNMVS 375
Cdd:COG0021 343 --------PAFEADAKgVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIkgagsFSPEDPSgRNIHFGVREHAMGA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 376 VALG----------CAT--------RGrtiafagafaafftrafdQLRMGAISQANINLIGSH--CGVstGEDG-----V 430
Cdd:COG0021 415 IMNGialhgglrpyGGTflvfsdymRP------------------AIRLAALMKLPVIYVFTHdsIGL--GEDGpthqpV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 431 sqmalEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANtkgmcfiRTSQPeTAVIYT----PQENFEIGQAKVVRHG---V 503
Cdd:COG0021 475 -----EQLASLRAIPNLDVIRPADANETAAAWKLALE-------RKDGP-TALILSrqnlPTLDRTAAAAEGVAKGayvL 541
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 133778974 504 ND-----KVTVIGAG--VTLheALEAADHLSQQGISVRVI 536
Cdd:COG0021 542 ADaegtpDVILIATGseVSL--AVEAAELLAAEGIKVRVV 579
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
17-265 |
5.44e-42 |
|
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: 154.85 E-value: 5.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 17 RDTANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVG-DISE 95
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGyDLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 96 SDLLNLRKLHSDLERHPTPR-LPFVDVATGSLGQGLGTACGMAYTGKYL---------DKASYRVFCLMGDGESSEGSVW 165
Cdd:pfam00456 83 EDLKSFRQLGSKTPGHPEFGhTAGVEVTTGPLGQGIANAVGMAIAERNLaatynrpgfDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 166 EAFAFASHYNLDNLVAVFDVNRL---GQSGPAPLEHGADIYqnccEAFGWNT-YLVDGHDVEALCQAFWQASQVKNKPTA 241
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQIsidGETKISFTEDTAARF----EAYGWHViEVEDGHDVEAIAAAIEEAKAEKDKPTL 238
|
250 260
....*....|....*....|....
gi 133778974 242 IVAKTFKGRGIPNIEDAENWHGKP 265
Cdd:pfam00456 239 IKCRTVIGYGSPNKQGTHDVHGAP 262
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
317-477 |
5.59e-37 |
|
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: 135.76 E-value: 5.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 317 DKIATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHPE---RFIECIIAEQNMVSVALGCATRGR-TIAFAGA 392
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 393 FAAFFTRAFDQLRMG-AISQANINLIGSHCGVSTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANTKG- 470
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
....*...
gi 133778974 471 -MCFIRTS 477
Cdd:pfam02779 161 kPVVLRLP 168
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
494-616 |
1.33e-36 |
|
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: 132.72 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 494 GQAKVVRHGvnDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATgGRVITVEDHYREGGIG 573
Cdd:pfam02780 1 GKAEILREG--DDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 133778974 574 EAVCAAVSRE----PDILVHQLAVSGVPQRGKTSELLDMFGISTRHI 616
Cdd:pfam02780 78 SEVAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
122-621 |
2.96e-30 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 125.99 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 122 ATGSLGQGLGTACGMAytgkyLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDVNR-------------- 187
Cdd:PRK12571 121 SSTSISAALGFAKARA-----LGQPDGDVVAVIGDGSLTAGMAYEALNNAGAADRRLIVILNDNEMsiappvgalaayls 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 188 -----------------LGQSGPAPLE---HGADIY-------QNCCEAFGWnTYL--VDGHDVEALCQAFWQASQVKNK 238
Cdd:PRK12571 196 tlrssdpfarlraiakgVEERLPGPLRdgaRRARELvtgmiggGTLFEELGF-TYVgpIDGHDMEALLSVLRAARARADG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 239 PTAIVAKTFKGRGIPNIEDAEN-WHGkpvpkeradaiVKLIEsqiqtnenlipksPVEDSPQISITdikmtSPPAYKvgd 317
Cdd:PRK12571 275 PVLVHVVTEKGRGYAPAEADEDkYHA-----------VGKFD-------------VVTGLQKKSAP-----SAPSYT--- 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 318 kiatqKTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHPERFIECIIAEQNMVSVALGCATRGrTIAFAGAFAAFF 397
Cdd:PRK12571 323 -----SVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAG-LKPFCAVYSTFL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 398 TRAFDQLRMG-AISQANINLIGSHCGVsTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLA-ANTKGMCFIR 475
Cdd:PRK12571 397 QRGYDQLLHDvALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAaAHDDGPIAVR 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 476 TSQPETAVIYTPQEN--FEIGQAKVVRHGvnDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIissA 553
Cdd:PRK12571 476 FPRGEGVGVEIPAEGtiLGIGKGRVPREG--PDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALT---D 550
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 133778974 554 KATGGR-VITVEDHYREGGIGEAVCAAVSRE-PDILVHQLAVSGVPQR----GKTSELLDMFGISTRHIIAAVT 621
Cdd:PRK12571 551 LLVRHHiVVIVEEQGAMGGFGAHVLHHLADTgLLDGGLKLRTLGLPDRfidhASREEMYAEAGLTAPDIAAAVT 624
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
439-583 |
5.12e-26 |
|
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: 108.95 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 439 AMFRSIPNCTVFYPSDAistehaiylaANTKGM-----------CFIrtsqpETAVIYT-----PQENFE--IGQAKVVR 500
Cdd:COG0022 135 AWFAHIPGLKVVAPSTP----------YDAKGLlkaairdddpvIFL-----EHKRLYRlkgevPEEDYTvpLGKARVVR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 501 HGvNDkVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATgGRVITVEDHYREGGIGEAVCAAV 580
Cdd:COG0022 200 EG-TD-VTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKT-GRLVVVDEAPRTGGFGAEIAARI 276
|
...
gi 133778974 581 SRE 583
Cdd:COG0022 277 AEE 279
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
37-253 |
1.01e-25 |
|
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: 109.32 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 37 GQLTSCCSAAEVVSVLFFHtmkYKQTDPEHPDNDRfILSRGHAAPILYA-AWVEvGDISESDLLNLRKLHSD--LERHPT 113
Cdd:cd02017 31 GHIATFASAATLYEVGFNH---FFRARGEGGGGDL-VYFQGHASPGIYArAFLE-GRLTEEQLDNFRQEVGGggLSSYPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 114 PRLP--FVDVATGSLGQGLGTACGMAYTGKYL------DKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDV 185
Cdd:cd02017 106 PWLMpdFWEFPTVSMGLGPIQAIYQARFNRYLedrglkDTSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 186 NRLGQSGPAPlEHGADI--YQNCCEAFGWN-------------------------------------------------- 213
Cdd:cd02017 186 NLQRLDGPVR-GNGKIIqeLEGIFRGAGWNvikviwgskwdellakdgggalrqrmeetvdgdyqtlkakdgayvrehff 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 133778974 214 ----------TYLVD---------GHDVEALCQAFWQASQVKNKPTAIVAKTFKGRGIP 253
Cdd:cd02017 265 gkypelkalvTDLSDedlwalnrgGHDPRKVYAAYKKAVEHKGKPTVILAKTIKGYGLG 323
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
439-580 |
1.77e-21 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 96.20 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 439 AMFRSIPNCTVFYPSDAIstehaiylaaNTKGMCF--IRTSQP----ETAVIY------TPQENFE--IGQAKVVRHGvN 504
Cdd:PTZ00182 166 AYFAHVPGLKVVAPSDPE----------DAKGLLKaaIRDPNPvvffEPKLLYresvevVPEADYTlpLGKAKVVREG-K 234
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 133778974 505 DkVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATgGRVITVEDHYREGGIGEAVCAAV 580
Cdd:PTZ00182 235 D-VTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPTCGIGAEIAAQI 308
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
346-477 |
3.01e-21 |
|
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: 89.85 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 346 TMNSTFSEIFRKEhperFIECIIAEQNMVSVALGCATRGRTIAFAGAFAAFFTRAfDQLRMGAISQANINLIGSHCGVST 425
Cdd:smart00861 4 ATRKAFGEALAEL----AIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAK-DQIRSAGASGNVPVVFRHDGGGGV 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 133778974 426 GEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANTKGMCFIRTS 477
Cdd:smart00861 79 GEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
132-576 |
1.73e-20 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 95.46 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 132 TACGMAyTGKYLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNlDNLVAVFDVNRLGQSGpaplEHGAdIYQNCCE--- 208
Cdd:PRK12315 121 LATGLA-KARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAE----NHGG-LYKNLKElrd 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 209 -----------AFGWN-TYLVDGHDVEALCQAFwqaSQVK--NKPTAIVAKTFKGRGI-PNIEDAENWH---------GK 264
Cdd:PRK12315 194 tngqsennlfkAMGLDyRYVEDGNDIESLIEAF---KEVKdiDHPIVLHIHTLKGKGYqPAEENKEAFHwhmpfdletGQ 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 265 PV---PKERA-DAIVKLIESQIQtnenlipkspvEDSPQISITDikmtsppaykvgdkiATQKTYGLalaklgranervi 340
Cdd:PRK12315 271 SKvpaSGESYsSVTLDYLLKKIK-----------EGKPVVAINA---------------AIPGVFGL------------- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 341 vlsgdtmnstfsEIFRKEHPERFIECIIAEQNMVSVALGCATRGrTIAFAGAFAAFFTRAFDQLRMG-AISQANINLIGS 419
Cdd:PRK12315 312 ------------KEFRKKYPDQYVDVGIAEQESVAFASGIAANG-ARPVIFVNSTFLQRAYDQLSHDlAINNNPAVMIVF 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 420 HCGVStGEDgVSQMALEDLAMFRSIPNctvfypsdaistehAIYLAANTK---------GMC------FIRtsQPETAVI 484
Cdd:PRK12315 379 GGSIS-GND-VTHLGIFDIPMISNIPN--------------LVYLAPTTKeeliamlewALTqhehpvAIR--VPEHGVE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 485 Y--TPQENFEIGQAKVVRHGvnDKVTVIGAGVTLHEALEAADHLSQQ-GISVRVIDPFTIKPLDAATiISSAKATGGRVI 561
Cdd:PRK12315 441 SgpTVDTDYSTLKYEVTKAG--EKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVV 517
|
490
....*....|....*
gi 133778974 562 TVEDHYREGGIGEAV 576
Cdd:PRK12315 518 TLEDGILDGGFGEKI 532
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
463-583 |
8.18e-18 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 86.51 E-value: 8.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 463 YLAANTKGM--CFIRTSQP----ETAVIY-----TPQ-ENF--EIGQAKVVRHGvnDKVTVIGAGVTLHEALEAADHLSQ 528
Cdd:PRK11892 287 YSAADAKGLlkAAIRDPNPviflENEILYgqsfdVPKlDDFvlPIGKARIHREG--KDVTIVSFSIGMTYALKAAEELAK 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 133778974 529 QGISVRVIDPFTIKPLDAATIISSAKATgGRVITVEDHYREGGIGEAVCAAVSRE 583
Cdd:PRK11892 365 EGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVGAEIAARVMEQ 418
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
461-583 |
6.52e-17 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 82.08 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 461 AIYLAANTKGM--CFIRTSQP----ETAVIY-----TPQENF--EIGQAKVVRHGVNdkVTVIGAGVTLHEALEAADHLS 527
Cdd:PRK09212 147 APYFAADCKGLlkTAIRDPNPviflENEILYghsheVPEEEEsiPIGKAAILREGSD--VTIVTFSIQVKLALEAAELLE 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778974 528 QQGISVRVIDPFTIKPLDAATIISSAKATgGRVITVEDHYREGGIGEAVCAAVSRE 583
Cdd:PRK09212 225 KEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGVGAEIAALIMKE 279
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
493-583 |
6.90e-15 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 76.40 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 493 IGQAKVVRHGVNdkVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATgGRVITVEDHYREGGI 572
Cdd:PLN02683 219 IGKAKIEREGKD--VTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGWPQHGV 295
|
90
....*....|.
gi 133778974 573 GEAVCAAVSRE 583
Cdd:PLN02683 296 GAEICASVVEE 306
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
122-573 |
8.47e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 77.83 E-value: 8.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 122 ATGSLGQGLGTACGMAyTGKYLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDVNRLGQ-----SGPAPL 196
Cdd:PLN02234 175 GTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLptanlDGPTQP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 197 EHG-----ADIYQNCCEAFGWNTYL-----------VDGHDVEALCQAFWQASQVKN-KPTAIVAKTFKGRGIPNIEDAE 259
Cdd:PLN02234 254 VGAlscalSRLQSNCGMIRETSSTLfeelgfhyvgpVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERAD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 260 N-WHGkpvpkeradaIVKLiesqiqtnenlipkspvedspqisitdikmtSPPAYKVGDKIATQKTYGL----ALAKLGR 334
Cdd:PLN02234 334 DkYHG----------VLKF-------------------------------DPETGKQFKNISKTQSYTScfveALIAEAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 335 ANERVIVLSGDTMNSTFSEIFRKEHPERFIECIIAEQNMVSVALGCATRGRTIAFAGAFAAFFTRAFDQLRMGAISQANI 414
Cdd:PLN02234 373 ADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 415 NLIGSHCGVsTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAA--NTKGMCFiRTSQPETAVIYTPQEN-- 490
Cdd:PLN02234 453 RFAIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCF-RYHRGNGIGVSLPPGNkg 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 491 --FEIGQAKVVRHGvnDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATgGRVITVEdhyr 568
Cdd:PLN02234 531 vpLQIGRGRILRDG--ERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSH-EVLITVE---- 603
|
....*
gi 133778974 569 EGGIG 573
Cdd:PLN02234 604 EGSIG 608
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
122-247 |
6.04e-14 |
|
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: 72.91 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 122 ATGSLGQGLGTACGMAYTGKYLDKASYrVFCLMGDGESSEGSVWEAFAFASHYNLdNLVAVFDVNRLGQSGPAPLE-HGA 200
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFAALWKL-PVIFVCENNGYAISTPTSRQtAGT 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 133778974 201 DIYQNcCEAFGWNTYLVDGHDVEALCQAFWQASQ---VKNKPTAIVAKTF 247
Cdd:cd02000 180 SIADR-AAAYGIPGIRVDGNDVLAVYEAAKEAVErarAGGGPTLIEAVTY 228
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
122-247 |
2.57e-11 |
|
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: 65.55 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 122 ATGSLGQGLGTACGMAYTGKYL--DKAsyrVFCLMGDGESSEGSVWEAFAFAShynLDNLVAVFDV--NRLGQSGPAPLE 197
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAKLRgeDEV---AVAFFGDGATSEGDFHEALNFAA---VWKLPVVFVCenNGYAISTPVERQ 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 133778974 198 -HGADIYQNcCEAFGWNTYLVDGHDVEALCQAFWQAsqVK-----NKPTAIVAKTF 247
Cdd:COG1071 199 tAVETIADR-AAGYGIPGVRVDGNDVLAVYAAVKEA--VEraragEGPTLIEAKTY 251
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
217-573 |
3.00e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 66.46 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 217 VDGHDVEALCQAFWQASQVKNK-PTAIVAKTFKGRGIPNIEDA-ENWHGkpvpkeradaivkliesqiqtnenlipkspv 294
Cdd:PLN02582 289 VDGHNIDDLVTILREVKSTKTTgPVLIHVVTEKGRGYPYAERAaDKYHG------------------------------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 295 edspqisITDIKMTSPPAYKVGDKIATQKTY-GLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHPERFIECIIAEQNM 373
Cdd:PLN02582 338 -------VVKFDPATGKQFKVKAKTQSYTTYfAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 374 VSVALGCATRGRTIAFAGAFAAFFTRAFDQLRMGAISQANINLIGSHCGVsTGEDGVSQMALEDLAMFRSIPNCTVFYPS 453
Cdd:PLN02582 411 VTFAAGLACEGLKPFCAIYSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPS 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 454 DAISTEHAIYLAA--NTKGMCFiRTSQPETAVIYTPQEN----FEIGQAKVVRHGvnDKVTVIGAGVTLHEALEAADHLS 527
Cdd:PLN02582 490 DEAELFHMVATAAaiDDRPSCF-RYPRGNGIGVQLPPNNkgipIEVGKGRILLEG--ERVALLGYGTAVQSCLAAASLLE 566
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 133778974 528 QQGISVRVIDPFTIKPLDAATIISSAKaTGGRVITVEdhyrEGGIG 573
Cdd:PLN02582 567 RHGLSATVADARFCKPLDRALIRSLAK-SHEVLITVE----EGSIG 607
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
110-246 |
1.38e-09 |
|
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: 57.27 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 110 RHPTPRLPFVDVATGSLGQGLGTACGMAYTGKylDKasyRVFCLMGDGESSEGsvWEAFAFASHYNLDNLVAVFDVNRLG 189
Cdd:cd00568 32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNNGGYG 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 133778974 190 QSGPAPLEHGADIYQNC----------CEAFGWNTYLVDghDVEALCQAFWQASQVKnKPTAIVAKT 246
Cdd:cd00568 105 TIRMHQEAFYGGRVSGTdlsnpdfaalAEAYGAKGVRVE--DPEDLEAALAEALAAG-GPALIEVKT 168
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
53-252 |
4.16e-09 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 59.77 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 53 FFHTmkykqtdPEHPDNDRFILSRGHAAPILYA-AWVEvGDISESDLLNLRK------LHSdlerHPTPRL-P-FVDVAT 123
Cdd:PRK09405 127 FFRA-------PNEPHGGDLVFFQGHASPGIYArAFLE-GRLTEEQLDNFRQevdgkgLSS----YPHPWLmPdFWQFPT 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 124 GSLGQGLGTACGMAYTGKYL------DKASYRVFCLMGDGESSE----GsvweAFAFASHYNLDNLVAVFDVN--RLgqS 191
Cdd:PRK09405 195 VSMGLGPIMAIYQARFLKYLenrglkDTSDQKVWAFLGDGEMDEpeslG----AISLAAREKLDNLIFVINCNlqRL--D 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 192 GPA--------PLE---HGAdiyqncceafGWN-----------------------------------TY---------- 215
Cdd:PRK09405 269 GPVrgngkiiqELEgifRGA----------GWNvikviwgsrwdpllakdtsgklvqlmnetvdgdyqTYkakdgayvre 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133778974 216 -----------LVD-------------GHDVEALCQAFWQASQVKNKPTAIVAKTFKGRGI 252
Cdd:PRK09405 339 hffgkypetkaLVAdmsdddiwalnrgGHDPRKVYAAYKAAVEHKGQPTVILAKTIKGYGM 399
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
28-251 |
4.73e-09 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 59.56 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 28 IRATCASGS--GQLTSCCSAAEVVSVLFFHTMKYKqtDPEHPDNDRFIlsRGHAAPILYA-AWVEvGDISESDLLNLRKL 104
Cdd:PRK13012 105 VRANRAYGElgGHIASYASAADLFEVGFNHFFRGR--DDAGGGDLVYF--QPHSAPGIYArAFLE-GRLSEEQLDHFRQE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 105 HS--DLERHPTPRL-P-FVDVATGSLGQGLGTACGMAYTGKYL------DKASYRVFCLMGDGESSEGSVWEAFAFASHY 174
Cdd:PRK13012 180 IGgpGLSSYPHPWLmPdFWQFPTGSMGIGPINAIYQARFMRYLqhrglkDTSGRKVWGFFGDGEMDEPESIAALSLAARE 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 175 NLDNLVAVFDVN--RLgqSGPA--------PLE---------------------------HGA--DIYQNCCEA------ 209
Cdd:PRK13012 260 GLDNLVFVINCNlqRL--DGPVrgngriiqELEalfrgagwnvikvlwgsdwdalfardtTGAlvRRFAETVDGqfqtfk 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 133778974 210 -----------FGWNTYLVD----------------GHDVEALCQAFWQASQVKNKPTAIVAKTFKGRG 251
Cdd:PRK13012 338 andgaynrehfFGQDPELAAlvahlsdedidrlkrgGHDPRKVYAAYAAAVRHKGQPTVILAKTKKGYG 406
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
123-251 |
7.28e-09 |
|
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: 56.02 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 123 TGSLGQGLGTACGMAYTGKYLDKaSYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDvNRLGQSGPapleHGADi 202
Cdd:cd02007 74 TGHSSTSISAALGMAVARDLKGK-KRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILND-NEMSISPN----VGTP- 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 133778974 203 yQNCCEAFGWN-TYLVDGHDVEALCQAFWQASQVKnKPTAIVAKTFKGRG 251
Cdd:cd02007 147 -GNLFEELGFRyIGPVDGHNIEALIKVLKEVKDLK-GPVLLHVVTKKGKG 194
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
439-580 |
4.96e-08 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 55.13 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 439 AMFRSIPNCTVFypsdAISTEHaiylaaNTKGM--CFIRTSQP----ETAVIYTPQENFE-------IGQAKVVRHGvND 505
Cdd:CHL00144 135 SYFQSVPGLQIV----ACSTPY------NAKGLlkSAIRSNNPviffEHVLLYNLKEEIPdneyllpLEKAEVVRPG-ND 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 133778974 506 kVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATgGRVITVEDHYREGGIGEAVCAAV 580
Cdd:CHL00144 204 -ITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKT-HKVLIVEECMKTGGIGAELIAQI 276
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
339-625 |
3.09e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 53.57 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 339 VIVLSGDTMNSTFSeIFRKEHPERFIECIIAEQNMVSVALGCATRGRTiAFAGAFAAFFTRAFDQLRMGAISQAN-INLI 417
Cdd:PLN02225 402 VVVHAGMEMDASLI-TFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFV 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 418 GSHCGVsTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAA--NTKGMC--FIRTSQPETAVIYTPQENFEI 493
Cdd:PLN02225 480 ITSAGL-VGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCfrFPRGSIVNMNYLVPTGLPIEI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 494 GQAKVVRHGVNdkVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDaATIISSAKATGGRVITVEDHYrEGGIG 573
Cdd:PLN02225 559 GRGRVLVEGQD--VALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLD-IKLVRDLCQNHKFLITVEEGC-VGGFG 634
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 133778974 574 EAVCAAVSRE----------PDILvhqlaVSGVPQRGKTSELLDMFGISTRHiIAAVTLTLM 625
Cdd:PLN02225 635 SHVAQFIALDgqldgnikwrPIVL-----PDGYIEEASPREQLALAGLTGHH-IAATALSLL 690
|
|
| XFP_N |
pfam09364 |
XFP N-terminal domain; Bacterial enzyme splits fructose-6-P and/or xylulose-5-P with the aid ... |
72-266 |
3.38e-06 |
|
XFP N-terminal domain; Bacterial enzyme splits fructose-6-P and/or xylulose-5-P with the aid of inorganic phosphate into either acetyl-P and erythrose-4-P and/or acetyl-P and glyeraldehyde-3-P EC:4.1.2.9, EC:4.1.2.22. This family is distantly related to transketolases e.g. pfam02779.
Pssm-ID: 401348 Cd Length: 364 Bit Score: 49.77 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 72 FILSRGHAAP-ILYAAWVEvGDISE------SDLLNLRKLHSDLE------RHPTPRLPfvdvatGSLGQG--LGTACGM 136
Cdd:pfam09364 76 YMVGPGHGGPaMVSPSYLD-GSYTEfypeitKDEEGLKRLFKQFSfpggipSHMTPETP------GSIHEGgeLGYALSH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 137 AYtGKYLDKASYRVFCLMGDGESSEGSV---WEAFAFASHYNLDNLVAVFDVNRLGQSGPAPLEHGADI-YQNCCEAFGW 212
Cdd:pfam09364 149 AY-GAVLDNPDLIVPCVVGDGEAETGPLatsWHSNKFINPRTDGAVLPILHLNGYKISNPTILARISDEeLHKFFEGMGY 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133778974 213 NTYLVDGHDVEALCQAF-----WQASQVKN------------KPT--AIVAKTFKGRGIPNIEDaenwhGKPV 266
Cdd:pfam09364 228 HPYFVENEDPMSMHRLMaetfdTAVEEIHDiqkaartndmteRPRwpMVILRTPKGWTGPKYVD-----GKKT 295
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
122-248 |
1.44e-05 |
|
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: 47.32 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 122 ATGSLGQGLGTACGMAYTGKYLDKASYrVFCLMGDGESSEGSVWEAFAFASHYNLDnLVAVFDVNRLGQSGPAPLEHGAD 201
Cdd:pfam00676 99 GNGILGAQVPLGAGIALAAKYRGKKEV-AITLYGDGAANQGDFFEGLNFAALWKLP-VIFVCENNQYGISTPAERASAST 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 133778974 202 IYQNCCEAFGWNTYLVDGHDVEALCQAFWQASQVK---NKPTAIVAKTFK 248
Cdd:pfam00676 177 TYADRARGYGIPGLHVDGMDPLAVYQASKFAAERArtgKGPFLIELVTYR 226
|
|
| TPP_PK |
cd02011 |
Thiamine pyrophosphate (TPP) family, Phosphoketolase (PK) subfamily, TPP-binding module; PK ... |
77-267 |
5.42e-04 |
|
Thiamine pyrophosphate (TPP) family, Phosphoketolase (PK) subfamily, TPP-binding module; PK catalyzes the conversion of D-xylulose 5-phosphate and phosphate to acetyl phosphate, D-glyceraldehyde-3-phosphate and H2O. This enzyme requires divalent magnesium ions and TPP for activity.
Pssm-ID: 238969 [Multi-domain] Cd Length: 227 Bit Score: 41.94 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 77 GHAAP-ILYAAWVEvGDISE------SDLLNLRKLHSDLE------RHPTPRLPfvdvatGSLGQG--LGTACGMAYtGK 141
Cdd:cd02011 3 GHGGPaVLANLYLE-GSYSEfypeisQDEEGMRKLFKQFSfpggipSHAAPETP------GSIHEGgeLGYSLSHAY-GA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 142 YLDKASYRVFCLMGDGESSEG---SVWEAFAFASHYNLDNLVAVFDVNRLGQSGP---APLEHgaDIYQNCCEAFGWNTY 215
Cdd:cd02011 75 VFDNPDLIVACVVGDGEAETGplaTSWHSNKFLNPATDGAVLPILHLNGYKISNPtilARISH--EELEALFRGYGYEPY 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 133778974 216 LVDGHDVEALCQAF-----WQASQVKNKPTA--------------IVAKTFKGRGIPNIEDAE----NWHGKPVP 267
Cdd:cd02011 153 FVEGDDPETMHQAMaatldWAIEEIKAIQKRareggdasrprwpmIVLRTPKGWTGPKEVDGKklegSFRSHQVP 227
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
126-303 |
4.71e-03 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 39.46 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 126 LGQGLGTACGMAYTGKYL-----DKASYRV-FCLMGDGESSEGSVWEAFAFASHYNL-------DNLVAVFDVNRLGQSG 192
Cdd:CHL00149 130 IGEGIPIALGAAFQSIYRqqvlkEVQPLRVtACFFGDGTTNNGQFFECLNMAVLWKLpiifvveNNQWAIGMAHHRSTSI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133778974 193 PaplehgaDIYQNCcEAFGWNTYLVDGHDVEALCQAFWQASQVKNK---PTAIVAKTFKGRG--------IPNIEDAENW 261
Cdd:CHL00149 210 P-------EIHKKA-EAFGLPGIEVDGMDVLAVREVAKEAVERARQgdgPTLIEALTYRFRGhsladpdeLRSKQEKEAW 281
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 133778974 262 HGK-PVPKERADAIVKLIESQIQTNE-NLIPKSPVEDSPQISIT 303
Cdd:CHL00149 282 VARdPIKKLKSYIIDNELASQKELNKiQREVKIEIEQAVQFAIS 325
|
|
| |
