|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
1-615 |
0e+00 |
|
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: 1196.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 1 MYPLLENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHK 80
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 81 ILTGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNN 160
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 161 AGAMDTDLLVILNDNDMSISPNVGALNNYLAKLMSGRFYAAMREGSSKVL----GIAPPLKEIASKVEEHVKGFFTPGTL 236
Cdd:COG1154 161 AGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLkklpGIGPPLYELARRAKEGLKGLVVPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 237 FEEFGFNYIGPIDGHDVDVLVDTLKNIRSLKGPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGLASgKGGAGKPQY 316
Cdd:COG1154 241 FEELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPK-KSKSSAPSY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 317 TQVFGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYD 396
Cdd:COG1154 320 TDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 397 QLIHDVALQNLPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTPTAVRYPRGTGP 476
Cdd:COG1154 400 QVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGNGP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 477 GAEIQQQMAALPIGKGVVRRRGKQVAILAFGSMVHPALA-----AAEALDATVADMRFVKPLDAELIRELAQTHELVVTV 551
Cdd:COG1154 480 GVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEaaerlAAEGISATVVDARFVKPLDEELILELAREHDLVVTV 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759930713 552 EENVVMGGAGSGCGEALQAMGLAVPTLHLGLPDDYVEHGDPALLLSLCGLDAAGIEKSIRERLA 615
Cdd:COG1154 560 EEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-614 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 1085.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 1 MYPLLENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHK 80
Cdd:PRK05444 3 KYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 81 ILTGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGV-DRKSVAIIGDGAMTAGQAFEALN 159
Cdd:PRK05444 83 ILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGeDRKVVAVIGDGALTGGMAFEALN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 160 NAGAMDTDLLVILNDNDMSISPNVGALNNYLAKLMSGrfyaamregsskvlgiapplkeiaskveehvkgfftpgTLFEE 239
Cdd:PRK05444 163 NAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRSS--------------------------------------TLFEE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 240 FGFNYIGPIDGHDVDVLVDTLKNIRSLKGPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGLASGKGGAGKPQYTQV 319
Cdd:PRK05444 205 LGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKSSKPGKPSYTKV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 320 FGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYDQLI 399
Cdd:PRK05444 285 FGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQVI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 400 HDVALQNLPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDT-PTAVRYPRGTGPGA 478
Cdd:PRK05444 365 HDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDgPIAIRYPRGNGVGV 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 479 EIqQQMAALPIGKGVVRRRGKQVAILAFGSMVHPALAAAEA-LDATVADMRFVKPLDAELIRELAQTHELVVTVEENVVM 557
Cdd:PRK05444 445 EL-PELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERlASATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIM 523
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 759930713 558 GGAGSGCGEALQAMGLAVPTLHLGLPDDYVEHGDPALLLSLCGLDAAGIEKSIRERL 614
Cdd:PRK05444 524 GGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
8-615 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 129308 [Multi-domain] Cd Length: 617 Bit Score: 878.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 8 INSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKILTGRRE 87
Cdd:TIGR00204 4 INSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTGRRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 88 RMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAGAMDTD 167
Cdd:TIGR00204 84 KFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDLKTD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 168 LLVILNDNDMSISPNVGALNNYLAKLMSGRFYAAMREGSSKVLGIAPPLKE-IASKVEEHVKGFFTPGTLFEEFGFNYIG 246
Cdd:TIGR00204 164 MIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNyLAKRTEESMKGLVVPGTFFEELGFNYIG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 247 PIDGHDVDVLVDTLKNIRSLKGPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGlASGKGGAGKPQYTQVFGDWLCD 326
Cdd:TIGR00204 244 PVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTG-CLPKSKSALPSYSKIFSDTLCE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 327 MAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYDQLIHDVALQN 406
Cdd:TIGR00204 323 LAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVCIQK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 407 LPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDT-PTAVRYPRGTGPGAEIQQQMA 485
Cdd:TIGR00204 403 LPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDgPIAVRYPRGNAVGVELTPEPE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 486 ALPIGKGVVRRRGKQVAILAFGSMVHPALAA-----AEALDATVADMRFVKPLDAELIRELAQTHELVVTVEENVVMGGA 560
Cdd:TIGR00204 483 KLPIGKSEVLRKGEKILILGFGTLVPEALEVaeslnEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVEENAIMGGA 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 759930713 561 GSGCGEALQAMGLAVPTLHLGLPDDYVEHGDPALLLSLCGLDAAGIEKSIRERLA 615
Cdd:TIGR00204 563 GSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
5-276 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).
Pssm-ID: 463832 [Multi-domain] Cd Length: 274 Bit Score: 544.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 5 LENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKILTG 84
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 85 RRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAGAM 164
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 165 DTDLLVILNDNDMSISPNVGALNNYLAKLMSGRFYAAMREGSSKVL--GIAPPLKEIASKVEEHVKGFFTPGTLFEEFGF 242
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLkpKIGPPLYELARRAKESLKGLVVPGTLFEELGF 240
|
250 260 270
....*....|....*....|....*....|....
gi 759930713 243 NYIGPIDGHDVDVLVDTLKNIRSLKGPQFLHIVT 276
Cdd:pfam13292 241 KYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
41-282 |
2.49e-123 |
|
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: 362.25 E-value: 2.49e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 41 GGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKILTGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTS 120
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 121 IGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAGAMDTDLLVILNDNDMSISPNVGalnnylaklmsgrfya 200
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 201 amregsskvlgiapplkeiaskveehvkgffTPGTLFEEFGFNYIGPIDGHDVDVLVDTLKNIRSLKGPQFLHIVTKKGQ 280
Cdd:cd02007 145 -------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKGK 193
|
..
gi 759930713 281 GY 282
Cdd:cd02007 194 GY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
338-477 |
7.52e-48 |
|
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: 163.81 E-value: 7.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 338 TPAMREGSGMVrFEKEhpdrYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYDQLIHDVALQNLPVMFALDRAG 417
Cdd:smart00861 2 KIATRKAFGEA-LAEL----AIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGG 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 418 LVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTPTAVRYPRGTGPG 477
Cdd:smart00861 77 GVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
1-615 |
0e+00 |
|
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: 1196.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 1 MYPLLENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHK 80
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 81 ILTGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNN 160
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 161 AGAMDTDLLVILNDNDMSISPNVGALNNYLAKLMSGRFYAAMREGSSKVL----GIAPPLKEIASKVEEHVKGFFTPGTL 236
Cdd:COG1154 161 AGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLkklpGIGPPLYELARRAKEGLKGLVVPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 237 FEEFGFNYIGPIDGHDVDVLVDTLKNIRSLKGPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGLASgKGGAGKPQY 316
Cdd:COG1154 241 FEELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPK-KSKSSAPSY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 317 TQVFGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYD 396
Cdd:COG1154 320 TDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 397 QLIHDVALQNLPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTPTAVRYPRGTGP 476
Cdd:COG1154 400 QVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGNGP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 477 GAEIQQQMAALPIGKGVVRRRGKQVAILAFGSMVHPALA-----AAEALDATVADMRFVKPLDAELIRELAQTHELVVTV 551
Cdd:COG1154 480 GVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEaaerlAAEGISATVVDARFVKPLDEELILELAREHDLVVTV 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759930713 552 EENVVMGGAGSGCGEALQAMGLAVPTLHLGLPDDYVEHGDPALLLSLCGLDAAGIEKSIRERLA 615
Cdd:COG1154 560 EEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-614 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 1085.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 1 MYPLLENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHK 80
Cdd:PRK05444 3 KYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 81 ILTGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGV-DRKSVAIIGDGAMTAGQAFEALN 159
Cdd:PRK05444 83 ILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGeDRKVVAVIGDGALTGGMAFEALN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 160 NAGAMDTDLLVILNDNDMSISPNVGALNNYLAKLMSGrfyaamregsskvlgiapplkeiaskveehvkgfftpgTLFEE 239
Cdd:PRK05444 163 NAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRSS--------------------------------------TLFEE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 240 FGFNYIGPIDGHDVDVLVDTLKNIRSLKGPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGLASGKGGAGKPQYTQV 319
Cdd:PRK05444 205 LGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKSSKPGKPSYTKV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 320 FGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYDQLI 399
Cdd:PRK05444 285 FGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQVI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 400 HDVALQNLPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDT-PTAVRYPRGTGPGA 478
Cdd:PRK05444 365 HDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDgPIAIRYPRGNGVGV 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 479 EIqQQMAALPIGKGVVRRRGKQVAILAFGSMVHPALAAAEA-LDATVADMRFVKPLDAELIRELAQTHELVVTVEENVVM 557
Cdd:PRK05444 445 EL-PELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERlASATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIM 523
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 759930713 558 GGAGSGCGEALQAMGLAVPTLHLGLPDDYVEHGDPALLLSLCGLDAAGIEKSIRERL 614
Cdd:PRK05444 524 GGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
8-615 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 129308 [Multi-domain] Cd Length: 617 Bit Score: 878.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 8 INSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKILTGRRE 87
Cdd:TIGR00204 4 INSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTGRRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 88 RMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAGAMDTD 167
Cdd:TIGR00204 84 KFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDLKTD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 168 LLVILNDNDMSISPNVGALNNYLAKLMSGRFYAAMREGSSKVLGIAPPLKE-IASKVEEHVKGFFTPGTLFEEFGFNYIG 246
Cdd:TIGR00204 164 MIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNyLAKRTEESMKGLVVPGTFFEELGFNYIG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 247 PIDGHDVDVLVDTLKNIRSLKGPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGlASGKGGAGKPQYTQVFGDWLCD 326
Cdd:TIGR00204 244 PVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTG-CLPKSKSALPSYSKIFSDTLCE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 327 MAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYDQLIHDVALQN 406
Cdd:TIGR00204 323 LAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVCIQK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 407 LPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDT-PTAVRYPRGTGPGAEIQQQMA 485
Cdd:TIGR00204 403 LPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDgPIAVRYPRGNAVGVELTPEPE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 486 ALPIGKGVVRRRGKQVAILAFGSMVHPALAA-----AEALDATVADMRFVKPLDAELIRELAQTHELVVTVEENVVMGGA 560
Cdd:TIGR00204 483 KLPIGKSEVLRKGEKILILGFGTLVPEALEVaeslnEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVEENAIMGGA 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 759930713 561 GSGCGEALQAMGLAVPTLHLGLPDDYVEHGDPALLLSLCGLDAAGIEKSIRERLA 615
Cdd:TIGR00204 563 GSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
3-615 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 774.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 3 PLLENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKIL 82
Cdd:PRK12571 7 PLLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCYPHKIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 83 TGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAG 162
Cdd:PRK12571 87 TGRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYEALNNAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 163 AMDTDLLVILNDNDMSISPNVGALNNYLAKLMSGRFYAAMREGSSKVLGIAP-PLKEIASKVEEHVKGFFTPGTLFEEFG 241
Cdd:PRK12571 167 AADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIAKGVEERLPgPLRDGARRARELVTGMIGGGTLFEELG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 242 FNYIGPIDGHDVDVLVDTLKNIRSLK-GPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGLASgKGGAGKPQYTQVF 320
Cdd:PRK12571 247 FTYVGPIDGHDMEALLSVLRAARARAdGPVLVHVVTEKGRGYAPAEADEDKYHAVGKFDVVTGLQK-KSAPSAPSYTSVF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 321 GDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYDQLIH 400
Cdd:PRK12571 326 GEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQRGYDQLLH 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 401 DVALQNLPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDT-PTAVRYPRGTGPGAE 479
Cdd:PRK12571 406 DVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDgPIAVRFPRGEGVGVE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 480 IQQQMAALPIGKGVVRRRGKQVAILAFGSMVHPALAAAEA-----LDATVADMRFVKPLDAELIRELAQTHElVVTVEEN 554
Cdd:PRK12571 486 IPAEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLleaegISVTVADPRFVKPLDEALTDLLVRHHI-VVIVEEQ 564
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759930713 555 VVMGGAGSGCGEALQAMGLA---VPTLHLGLPDDYVEHGDPALLLSLCGLDAAGIEKSIRERLA 615
Cdd:PRK12571 565 GAMGGFGAHVLHHLADTGLLdggLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALA 628
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
3-610 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 663.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 3 PLLENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKIL 82
Cdd:PLN02582 32 PLLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQSYPHKIL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 83 TGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAG 162
Cdd:PLN02582 112 TGRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 163 AMDTDLLVILNDN-DMSI--------SPNVGALNNYLAKLMSGRFYAAMRE---GSSKVLGiaPPLKEIASKVEEHVKGF 230
Cdd:PLN02582 192 YLDSDMIVILNDNkQVSLptatldgpAPPVGALSSALSRLQSSRPLRELREvakGVTKQIG--GPMHELAAKVDEYARGM 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 231 F--TPGTLFEEFGFNYIGPIDGHDVDVLVDTLKNIRSLK--GPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGLAS 306
Cdd:PLN02582 270 IsgSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKttGPVLIHVVTEKGRGYPYAERAADKYHGVVKFDPATGKQF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 307 gKGGAGKPQYTQVFGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAI 386
Cdd:PLN02582 350 -KVKAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 387 YSTFLQRGYDQLIHDVALQNLPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQL-DTP 465
Cdd:PLN02582 429 YSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIdDRP 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 466 TAVRYPRGTGPGAEIQQQMAALPI--GKGVVRRRGKQVAILAFGSMVH-----PALAAAEALDATVADMRFVKPLDAELI 538
Cdd:PLN02582 509 SCFRYPRGNGIGVQLPPNNKGIPIevGKGRILLEGERVALLGYGTAVQsclaaASLLERHGLSATVADARFCKPLDRALI 588
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759930713 539 RELAQTHELVVTVEENVVmGGAGSGCGEALQAMGLAVPTLH---LGLPDDYVEHGDPALLLSLCGLDAAGIEKSI 610
Cdd:PLN02582 589 RSLAKSHEVLITVEEGSI-GGFGSHVAQFMALDGLLDGKLKwrpLVLPDRYIDHGAPADQLAEAGLTPSHIAATV 662
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
5-276 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).
Pssm-ID: 463832 [Multi-domain] Cd Length: 274 Bit Score: 544.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 5 LENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKILTG 84
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 85 RRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAGAM 164
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 165 DTDLLVILNDNDMSISPNVGALNNYLAKLMSGRFYAAMREGSSKVL--GIAPPLKEIASKVEEHVKGFFTPGTLFEEFGF 242
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLkpKIGPPLYELARRAKESLKGLVVPGTLFEELGF 240
|
250 260 270
....*....|....*....|....*....|....
gi 759930713 243 NYIGPIDGHDVDVLVDTLKNIRSLKGPQFLHIVT 276
Cdd:pfam13292 241 KYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
3-593 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 543.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 3 PLLENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKIL 82
Cdd:PLN02234 65 PLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKIL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 83 TGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAG 162
Cdd:PLN02234 145 TGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 163 AMDTDLLVILNDNDM---------SISPNVGALNNYLAKLMSGrfYAAMREGSSkvlgiapplkeiaskveehvkgfftp 233
Cdd:PLN02234 225 YLHSNMIVILNDNKQvslptanldGPTQPVGALSCALSRLQSN--CGMIRETSS-------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 234 gTLFEEFGFNYIGPIDGHDVDVLVDTLKNIRSLK--GPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGlASGKGGA 311
Cdd:PLN02234 277 -TLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETG-KQFKNIS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 312 GKPQYTQVFGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFL 391
Cdd:PLN02234 355 KTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFM 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 392 QRGYDQLIHDVALQNLPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDT-PTAVRY 470
Cdd:PLN02234 435 QRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDrPSCFRY 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 471 PRGTGPGAEIQQQMAALP--IGKGVVRRRGKQVAILAFGSMVH-----PALAAAEALDATVADMRFVKPLDAELIRELAQ 543
Cdd:PLN02234 515 HRGNGIGVSLPPGNKGVPlqIGRGRILRDGERVALLGYGSAVQrcleaASMLSERGLKITVADARFCKPLDVALIRSLAK 594
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 759930713 544 THELVVTVEENVVmGGAGSGCGEALQAMGLAVPTLHlgLPDDYVEHGDPA 593
Cdd:PLN02234 595 SHEVLITVEEGSI-GGFGSHVVQFLALDGLLDGKLK--VYRTWITNGSTS 641
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
3-561 |
1.88e-166 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 487.21 E-value: 1.88e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 3 PLLENINSPADLRLLPRTQLPQLAGELREFLVESVSKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKIL 82
Cdd:PRK12315 1 MYLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 83 TGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAG 162
Cdd:PRK12315 81 TGRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 163 AMDTDLLVILNDNDMSISPNVGALNNYLAKLmsgrfyaamREGSSKvlgiapplkeiaskveehvkgffTPGTLFEEFGF 242
Cdd:PRK12315 161 ELKSNLIIIVNDNQMSIAENHGGLYKNLKEL---------RDTNGQ-----------------------SENNLFKAMGL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 243 NYIGPIDGHDVDVLVDTLKNIRSLKGPQFLHIVTKKGQGYKLAENDPVKYHGVTKFDPANGlaSGKGGAGKPQYTQVFGD 322
Cdd:PRK12315 209 DYRYVEDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKGYQPAEENKEAFHWHMPFDLETG--QSKVPASGESYSSVTLD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 323 WLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYDQLIHDV 402
Cdd:PRK12315 287 YLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQRAYDQLSHDL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 403 ALQNLPVMFALDRAGLVGADgPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAF-QLDTPTAVRYPRGTGP-GAEI 480
Cdd:PRK12315 367 AINNNPAVMIVFGGSISGND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALtQHEHPVAIRVPEHGVEsGPTV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 481 QQQMAALpigKGVVRRRGKQVAILAFGSM------VHPALAAAEALDATVADMRFVKPLDAELIRELAQTHELVVTVEEN 554
Cdd:PRK12315 446 DTDYSTL---KYEVTKAGEKVAILALGDFyelgekVAKKLKEELGIDATLINPKFITGLDEELLEKLKEDHELVVTLEDG 522
|
....*..
gi 759930713 555 VVMGGAG 561
Cdd:PRK12315 523 ILDGGFG 529
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
3-601 |
3.48e-133 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 406.02 E-value: 3.48e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 3 PLLENINSPADLRLLPRTQLPQLAGELREFLVESV-SKTGGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKI 81
Cdd:PLN02225 77 PILDSIETPLQLKNLSVKELKLLADEIRTELHSVLwKKTQKSMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAHKV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 82 LTgRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNA 161
Cdd:PLN02225 157 LT-RRWSAIPSRQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGKRDRVVAVIDNATITAGQAYEAMSNA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 162 GAMDTDLLVILNDNDMSISPN--------VGALNNYLAKLMSGRFYAAMRE-GSSKVLGIAPPLKEIASKVEEHVKGFFT 232
Cdd:PLN02225 236 GYLDSNMIVILNDSRHSLHPNmeegskasISALSSIMSKIQSSKIFRKFRElAKAMTKRIGKGMYEWAAKVDEYARGMVG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 233 P--GTLFEEFGFNYIGPIDGHDVDVLVDTLKNIRSLK--GPQFLHIVTKKGQGYKLAENDPVKyhgvtkfdpanglasgk 308
Cdd:PLN02225 316 PtgSTLFEELGLYYIGPVDGHNIEDLVCVLREVSSLDsmGPVLVHVITEENRDAETGKNIMVK----------------- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 309 ggaGKPQYTQVFGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYS 388
Cdd:PLN02225 379 ---DRRTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPS 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 389 TFLQRGYDQLIHDVALQNLPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYT-AFQLDTPTA 467
Cdd:PLN02225 456 AFLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATaAYVTDRPVC 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 468 VRYPRGTgpgaeIQQQMAALP------IGKGVVRRRGKQVAILAFGSMVHP-----ALAAAEALDATVADMRFVKPLDAE 536
Cdd:PLN02225 536 FRFPRGS-----IVNMNYLVPtglpieIGRGRVLVEGQDVALLGYGAMVQNclhahSLLSKLGLNVTVADARFCKPLDIK 610
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759930713 537 LIRELAQTHELVVTVEENVVmGGAGSGCGEALQAMGLAVPTLH---LGLPDDYVEHGDPALLLSLCGL 601
Cdd:PLN02225 611 LVRDLCQNHKFLITVEEGCV-GGFGSHVAQFIALDGQLDGNIKwrpIVLPDGYIEEASPREQLALAGL 677
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
41-282 |
2.49e-123 |
|
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: 362.25 E-value: 2.49e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 41 GGHFASNLGSIELTIALHYVFDTPHDRLVWDVGHQTYPHKILTGRRERMHTMRQHNGLAGFPKREESEYDTFGVGHSSTS 120
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 121 IGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAGAMDTDLLVILNDNDMSISPNVGalnnylaklmsgrfya 200
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 201 amregsskvlgiapplkeiaskveehvkgffTPGTLFEEFGFNYIGPIDGHDVDVLVDTLKNIRSLKGPQFLHIVTKKGQ 280
Cdd:cd02007 145 -------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKGK 193
|
..
gi 759930713 281 GY 282
Cdd:cd02007 194 GY 195
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
318-614 |
5.16e-75 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 241.91 E-value: 5.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 318 QVFGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFL-QRGYD 396
Cdd:COG3958 8 DAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLtGRAYE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 397 QLIHDVALQNLPV-MFALDrAGL-VGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTPTAVRYPRGT 474
Cdd:COG3958 88 QIRNDIAYPNLNVkIVGSH-AGLsYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRLGRGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 475 GPgaEIQQQMAALPIGKGVVRRRGKQVAILAFGSMVHP-----ALAAAEALDATVADMRFVKPLDAELIRELAQTHELVV 549
Cdd:COG3958 167 VP--VVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEaleaaELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVV 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759930713 550 TVEENVVMGGAGSGCGEALqAMGLAVPTLHLGLPDDYVEHGDPALLLSLCGLDAAGIEKSIRERL 614
Cdd:COG3958 245 TAEEHSIIGGLGSAVAEVL-AENYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
318-472 |
1.70e-74 |
|
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: 235.03 E-value: 1.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 318 QVFGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYDQ 397
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759930713 398 LIHDVALQNLPVMFALDRAGL-VGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTPTAVRYPR 472
Cdd:cd07033 81 IRHDVALQNLPVKFVGTHAGIsVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
313-473 |
2.26e-51 |
|
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: 174.66 E-value: 2.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 313 KPQYTQVFGDWLCDMAKLDKRLVGITPAMREGSGMVRFEKEHPD---RYYDVAIAEQHAVTFAGGMACDG--LKPVVAIY 387
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEATF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 388 STFLQRGYDQLIHDVALQNLPVMFALDRAGL-VGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDT-- 464
Cdd:pfam02779 82 SDFLNRADDAIRHGAALGKLPVPFVVTRDPIgVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGrk 161
|
....*....
gi 759930713 465 PTAVRYPRG 473
Cdd:pfam02779 162 PVVLRLPRQ 170
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
338-477 |
7.52e-48 |
|
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: 163.81 E-value: 7.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 338 TPAMREGSGMVrFEKEhpdrYYDVAIAEQHAVTFAGGMACDGLKPVVAIYSTFLQRGYDQLIHDVALQNLPVMFALDRAG 417
Cdd:smart00861 2 KIATRKAFGEA-LAEL----AIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGG 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 418 LVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTPTAVRYPRGTGPG 477
Cdd:smart00861 77 GVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKSLYR 136
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
318-472 |
3.75e-31 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 118.60 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 318 QVFGDWLCDMAKLdkrlVGITPAMREGSGMVRFEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIY-STFLQRGYD 396
Cdd:cd06586 1 AAFAEVLTAWGVR----HVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTsGTGLLNAIN 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759930713 397 QLIhDVALQNLPVMFALDRAGLVGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLY---TAFQLDTPTAVRYPR 472
Cdd:cd06586 77 GLA-DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHairTAYASQGPVVVRLPR 154
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
121-511 |
1.31e-29 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 123.71 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 121 IGAALGMAVAAKTLG----------VDRKSVAIIGDGAMTAGQAFEALNNAGAMDTD-LLVILNDNDMSIspnvgalnny 189
Cdd:PRK05899 124 LANAVGMALAEKYLAalfnrpgldiVDHYTYVLCGDGDLMEGISHEACSLAGHLKLGnLIVIYDDNRISI---------- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 190 laklmsgrfyaamrEGsskvlgiapplkeiaskveeHVKGFFTPGTL--FEEFGFNYIgPIDGHDVDVLVDTLKNIRSLK 267
Cdd:PRK05899 194 --------------DG--------------------PTEGWFTEDVKkrFEAYGWHVI-EVDGHDVEAIDAAIEEAKAST 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 268 GPQFLHIVTKKGQGYKLAENDPvKYHGvtKFDPANGLASGKGGAGKPqYTQVFGDWLCDMAKLDKRLVG----ITPA-MR 342
Cdd:PRK05899 239 KPTLIIAKTIIGKGAPNKEGTH-KVHG--APLGAEEIAAAKKELGWD-YRKASGKALNALAKALPELVGgsadLAGSnNT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 343 EGSGMVRF-EKEHPDRYYDVAIAEQHAVTFAGGMACDG-LKPVVAIYSTFLQRGYDQlIHDVALQNLPVMFALDRAGL-V 419
Cdd:PRK05899 315 KIKGSKDFaPEDYSGRYIHYGVREFAMAAIANGLALHGgFIPFGGTFLVFSDYARNA-IRLAALMKLPVIYVFTHDSIgV 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 420 GADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAF-QLDTPTAVRYPRGTGPGAEIQQQMAALPIGKGVVRRRG 498
Cdd:PRK05899 394 GEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGPSALVLTRQNLPVLERTAQEEGVAKGGYVLRDDP 473
|
410
....*....|...
gi 759930713 499 kQVAILAFGSMVH 511
Cdd:PRK05899 474 -DVILIATGSEVH 485
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
490-606 |
5.59e-25 |
|
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: 99.98 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 490 GKGVVRRRGKQVAILAFGSMVHP-----ALAAAEALDATVADMRFVKPLDAELIRELAQTHELVVTVEENVVMGGAGSGC 564
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEaleaaELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 759930713 565 GEALQ---AMGLAVPTLHLGLPdDYVEHGDPALLLSLCGLDAAGI 606
Cdd:pfam02780 81 AAALAeeaFDGLDAPVLRVGGP-DFPEPGSADELEKLYGLTPEKI 124
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
355-562 |
2.98e-17 |
|
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: 83.14 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 355 PDRYYDVAIAEQhavTFAG---GMACDGLKPVVAI-YSTFLQRGYDQLIHDVA--------LQNLPVMFaldRA---GLV 419
Cdd:COG0022 50 PDRVFDTPISEA---GIVGaaiGAALAGLRPVVEIqFADFIYPAFDQIVNQAAklrymsggQFKVPMVI---RTpygGGI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 420 GAdGPTHAGAFDlSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTPTAV-----RYP-RGTGPGAEiqqqmAALPIGKGV 493
Cdd:COG0022 124 GA-GAQHSQSLE-AWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDPVIFlehkrLYRlKGEVPEED-----YTVPLGKAR 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759930713 494 VRRRGKQVAILAFGSMVHP-----ALAAAEALDATVADMRFVKPLDAELIRE-LAQTHELVVtVEENVVMGGAGS 562
Cdd:COG0022 197 VVREGTDVTIVTYGAMVHRaleaaEELAEEGISAEVIDLRTLSPLDEETILEsVKKTGRLVV-VDEAPRTGGFGA 270
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
28-294 |
8.46e-17 |
|
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: 80.63 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 28 ELREFLVESVSKTG-GHFASNLGSIELTIAL-----HYVFDTPH----DRLVWDVGHQT---YPHKILTG--RRERMHTM 92
Cdd:cd02012 2 RIRRLSIDMVQKAGsGHPGGSLSAADILAVLyfkvlKYDPADPKwpnrDRFVLSKGHASpalYAVLALAGylPEEDLKTF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 93 RQHNG-LAGFPKREEseydTFGVgHSSTS-----IGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAGAMDT 166
Cdd:cd02012 82 RQLGSrLPGHPEYGL----TPGV-EVTTGslgqgLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 167 D-LLVILNDNDMSIS---PNVGALNNYLAKlmsgrfyaamregsskvlgiapplkeiaskveehvkgfftpgtlFEEFGF 242
Cdd:cd02012 157 DnLIAIVDSNRIQIDgptDDILFTEDLAKK--------------------------------------------FEAFGW 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 759930713 243 NYIgPIDGHDVDVLVDTLKNIRSLKG-PQFLHIVTKKGQGYKLAENDPvKYHG 294
Cdd:cd02012 193 NVI-EVDGHDVEEILAALEEAKKSKGkPTLIIAKTIKGKGVPFMENTA-KWHG 243
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
350-562 |
4.05e-16 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 80.03 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 350 FEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAI-YSTFLQRGYDQLIHDVA--------LQNLPVMFaldRA--GL 418
Cdd:PTZ00182 76 LDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFmFADFIFPAFDQIVNEAAkyrymsggQFDCPIVI---RGpnGA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 419 VGADGPTHAGAFDlSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTPTAVRYPRGTGPGAEIQQQMAA--LPIGKGVVRR 496
Cdd:PTZ00182 153 VGHGGAYHSQSFE-AYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEADytLPLGKAKVVR 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759930713 497 RGKQVAILAFGSMVHPALAAAEALDAT-----VADMRFVKPLDAELIRE-LAQTHELvVTVEENVVMGGAGS 562
Cdd:PTZ00182 232 EGKDVTIVGYGSQVHVALKAAEELAKEgisceVIDLRSLRPWDRETIVKsVKKTGRC-VIVHEAPPTCGIGA 302
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
351-562 |
1.32e-14 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 75.14 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 351 EKEHPDRYYDVAIAEqHAvtFAG---GMACDGLKPVVAIYS-TFLQRGYDQLIHDVALQN--------LPVMF--ALDRA 416
Cdd:PRK09212 46 EQFGPKRVIDTPITE-HG--FAGlavGAAFAGLRPIVEFMTfNFSMQAIDQIVNSAAKTNymsggqlkCPIVFrgPNGAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 417 GLVGADgptHAGAFDLSYLRcIPNMTVMAPSDENECRQLLYTAFQLDTPTA-VRYPRGTGPGAEIQQQMAALPIGKGVVR 495
Cdd:PRK09212 123 ARVAAQ---HSQCYAAWYSH-IPGLKVVAPYFAADCKGLLKTAIRDPNPVIfLENEILYGHSHEVPEEEESIPIGKAAIL 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759930713 496 RRGKQVAILAFGSMVHPALAAAEALD-----ATVADMRFVKPLDAELIRELAQTHELVVTVEENVVMGGAGS 562
Cdd:PRK09212 199 REGSDVTIVTFSIQVKLALEAAELLEkegisVEVIDLRTLRPLDTETIIESVKKTNRLVVVEEGWPFAGVGA 270
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
350-562 |
1.46e-13 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 72.54 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 350 FEKEHPDRYYDVAIAEQHAVTFAGGMACDGLKPVVAIYS-TFLQRGYDQLIHDVALQN--------LPVMFALDRAGLVG 420
Cdd:PLN02683 68 LQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTfNFSMQAIDHIINSAAKTNymsagqisVPIVFRGPNGAAAG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 421 AdGPTHAGAFDLSYLRCiPNMTVMAPSDENECRQLLYTAFQLDTPTAV-----RYPRGTGPGAEIQQQMAALPIGKGVVR 495
Cdd:PLN02683 148 V-GAQHSQCFAAWYSSV-PGLKVLAPYSSEDARGLLKAAIRDPDPVVFlenelLYGESFPVSAEVLDSSFVLPIGKAKIE 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759930713 496 RRGKQVAILAFGSMV-----HPALAAAEALDATVADMRFVKPLDAELIRELAQTHELVVTVEENVVMGGAGS 562
Cdd:PLN02683 226 REGKDVTIVAFSKMVgyalkAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGA 297
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
21-295 |
1.97e-12 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 67.80 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 21 QLPQLAGELREFLVESVSKTG-GHFASNLGSIELTIALHYVF-----DTPH----DRLVWDVGHQT---YPHKILTGR-- 85
Cdd:COG3959 7 ELEEKARQIRRDILRMIYAAGsGHPGGSLSAADILAALYFKVmnidpKNPDwpdrDRFILSKGHAApalYAVLAEKGYfp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 86 RERMHTMRQHNG-LAGFPKREeseyDTFGVGHSSTSIG----AALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNN 160
Cdd:COG3959 87 KEELATFRKLGSrLQGHPDMK----KTPGVEMSTGSLGqglsVAVGMALAAKLDGKDYRVYVLLGDGELQEGQVWEAAMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 161 AGAMDTD-LLVILNDNDMSIspnvgalnnylaklmSGRfyaamregSSKVLGIAPplkeIASKveehvkgfftpgtlFEE 239
Cdd:COG3959 163 AAHYKLDnLIAIVDRNGLQI---------------DGP--------TEDVMSLEP----LAEK--------------WEA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 759930713 240 FGFNYIgPIDGHDVDVLVDTLKNIRSLKG-PQFlhIV--TKKGQGYKLAENDPvKYHGV 295
Cdd:COG3959 202 FGWHVI-EVDGHDIEALLAALDEAKAVKGkPTV--IIahTVKGKGVSFMENRP-KWHGK 256
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
355-465 |
9.45e-10 |
|
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: 57.87 E-value: 9.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 355 PDRYYDVAIAEQHAVTFAGGMACDGLKPVVAI-YSTFLQRGYDQLIHDVA--------LQNLPVMFaldRA--GLVGADG 423
Cdd:cd07036 43 PDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFALPAFDQIVNEAAklrymsggQFKVPIVI---RGpnGGGIGGG 119
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 759930713 424 PTHAGAFDlSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTP 465
Cdd:cd07036 120 AQHSQSLE-AWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
52-276 |
9.89e-08 |
|
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: 51.87 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 52 ELTIALHYVFDtPHDRLVWDVGHQTYPHkiltgrrermhtmrqhnGLAGFPKREESEYDTFGVGHSSTSIGAALGMAVAA 131
Cdd:cd00568 1 RVLAALRAALP-EDAIVVNDAGNSAYWA-----------------YRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 132 KtlgvDRKSVAIIGDGAMtaGQAFEALNNAGAMDTDLLVILNDNDMsispnvgalnnylaklmsgrfYAAMREGSSKVLG 211
Cdd:cd00568 63 P----DRPVVCIAGDGGF--MMTGQELATAVRYGLPVIVVVFNNGG---------------------YGTIRMHQEAFYG 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759930713 212 IAPPLKEIaskveehvkGFFTPGTLFEEFGFNYIGPIDGHDVDvlvDTLKNIRSLKGPQFLHIVT 276
Cdd:cd00568 116 GRVSGTDL---------SNPDFAALAEAYGAKGVRVEDPEDLE---AALAEALAAGGPALIEVKT 168
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
66-511 |
2.14e-07 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 53.91 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 66 DRLVWDVGHQT---YPHKILTGRRERMHTM---RQHNGLA-GFPKReeseYDTFGV----GHSSTSIGAALGMAVAAKTL 134
Cdd:PTZ00089 60 DRFVLSNGHASallYSMLHLTGYDLSMEDLknfRQLGSRTpGHPER----HITPGVevttGPLGQGIANAVGLAIAEKHL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 135 G----------VDRKSVAIIGDGAMTAGQAFEALNNAGAMDTD-LLVILNDNDMSISpnvGALNNYLAKLMSGRfYAAMR 203
Cdd:PTZ00089 136 AakfnrpghpiFDNYVYVICGDGCLQEGVSQEALSLAGHLGLEkLIVLYDDNKITID---GNTDLSFTEDVEKK-YEAYG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 204 EGSSKVLGIAPPLKEIASKVEE--HVKGffTPGTLFEE----FGFNYIGPIDGHDVDVLVDTLKNIRSLKG--PQ----- 270
Cdd:PTZ00089 212 WHVIEVDNGNTDFDGLRKAIEEakKSKG--KPKLIIVKttigYGSSKAGTEKVHGAPLGDEDIAQVKELFGldPEkkfhv 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 271 -------FLHIVTKKGQGYKLAENDPVKYhgvTKFDPANGLASGKGGAGKpqytqVFGDWLCDMAKL---DKR------- 333
Cdd:PTZ00089 290 seevrqfFEQHVEKKKENYEAWKKRFAKY---TAAFPKEAQAIERRFKGE-----LPPGWEKKLPKYttnDKAiatrkas 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 334 ------LVGITPAMREGS------------GMVRFEKEHPD-RYYDVAIAEQHAVTFAGGM-ACDGLKPVVAiysTFLQ- 392
Cdd:PTZ00089 362 envlnpLFQILPELIGGSadltpsnltrpkEANDFTKASPEgRYIRFGVREHAMCAIMNGIaAHGGFIPFGA---TFLNf 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 393 RGYD-QLIHDVALQNLPVMFAL--DRAGLvGADGPTHAGAFDLSYLRCIPNMTVMAPSDENECRQLLYTAF-QLDTPTAV 468
Cdd:PTZ00089 439 YGYAlGAVRLAALSHHPVIYVAthDSIGL-GEDGPTHQPVETLALLRATPNLLVIRPADGTETSGAYALALaNAKTPTIL 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 759930713 469 RYPRGTGPgaeIQQQMAALPIGKG--VVRR--RGKQVAILAFGSMVH 511
Cdd:PTZ00089 518 CLSRQNTP---PLPGSSIEGVLKGayIVVDftNSPQLILVASGSEVS 561
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
84-180 |
4.86e-07 |
|
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: 51.73 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 84 GRRERMH-TMRQHNGLAGFpkreeseydtfgvGHSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAG 162
Cdd:cd02000 85 GRGGSMHiGDKEKNFFGGN-------------GIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAA 151
|
90
....*....|....*...
gi 759930713 163 AMDTDLLVILNDNDMSIS 180
Cdd:cd02000 152 LWKLPVIFVCENNGYAIS 169
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
357-562 |
8.00e-06 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 48.20 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 357 RYYDVAIAEQHAVTFAGGMACDGLKPVV-AIYSTFLQRGYDQ------LIHDVALQNLPVMFALDRAGLVGAD-GPTHAG 428
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAMTGLRPIVeGMNMGFLLLAFNQisnnagMLHYTSGGNFTIPIVIRGPGGVGRQlGAEHSQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 429 AFDlSYLRCIPNMTVMAPSDENECRQLLYTAFQLDTPT-----AVRYprgtGPGAEIQQQMAALPIGKGVVRRRGKQVAI 503
Cdd:CHL00144 132 RLE-SYFQSVPGLQIVACSTPYNAKGLLKSAIRSNNPViffehVLLY----NLKEEIPDNEYLLPLEKAEVVRPGNDITI 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759930713 504 LAFGSMVHPALAAAEALDAT-----VADMRFVKPLDAELI-RELAQTHElVVTVEENVVMGGAGS 562
Cdd:CHL00144 207 LTYSRMRHHVLQAVKVLVEKgydpeIIDLISLKPLDLGTIsKSVKKTHK-VLIVEECMKTGGIGA 270
|
|
| PLN02790 |
PLN02790 |
transketolase |
350-451 |
9.84e-06 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 48.48 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 350 FEKEHP-DRYYDVAIAEQHAVTFAGGMA--CDGLKPVVAiysTFLQRGyDQLIHDV---ALQNLPVMFAL--DRAGLvGA 421
Cdd:PLN02790 385 FQKDTPeERNVRFGVREHGMGAICNGIAlhSSGLIPYCA---TFFVFT-DYMRAAMrlsALSEAGVIYVMthDSIGL-GE 459
|
90 100 110
....*....|....*....|....*....|
gi 759930713 422 DGPTHAGAFDLSYLRCIPNMTVMAPSDENE 451
Cdd:PLN02790 460 DGPTHQPIEHLASLRAMPNILMLRPADGNE 489
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
116-269 |
2.19e-05 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 45.35 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 116 HSSTSIGAALGMAVAAKTLGVDRKSVAIIGDGA-----MTagqafeALNNAGAMDTDLLVILNDNDmsispnvgalnnyl 190
Cdd:cd02008 48 DTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTffhsgIL------GLINAVYNKANITVVILDNR-------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 191 aklmsgrfYAAMrEGSSKVLGIAPPLKEIASKV--EEHVKGfftpgtlfeeFGFNYIGPIDGHDVDVLVDTLKNIRSLKG 268
Cdd:cd02008 108 --------TTAM-TGGQPHPGTGKTLTEPTTVIdiEALVRA----------IGVKRVVVVDPYDLKAIREELKEALAVPG 168
|
.
gi 759930713 269 P 269
Cdd:cd02008 169 V 169
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
119-180 |
2.23e-05 |
|
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: 47.06 E-value: 2.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759930713 119 TSIGAALGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAGAMDTDLLVILNDNDMSIS 180
Cdd:COG1071 131 GQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAIS 192
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
82-180 |
1.84e-04 |
|
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: 43.85 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 82 LTGRRERMHTMRQHnglaGFPKREESE-YDTFGVGHSSTSIGAalGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNN 160
Cdd:pfam00676 73 LYGRVAKGKGGSMH----GYYGAKGNRfYGGNGILGAQVPLGA--GIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNF 146
|
90 100
....*....|....*....|
gi 759930713 161 AGAMDTDLLVILNDNDMSIS 180
Cdd:pfam00676 147 AALWKLPVIFVCENNQYGIS 166
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
119-175 |
2.62e-04 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 41.80 E-value: 2.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 759930713 119 TSIGAALGMAVAAKTLGVDRKSVAIIGDGA--MTaGQAFEalnNAGAMDTDLLVILNDN 175
Cdd:pfam02775 28 GTMGYGLPAAIGAKLARPDRPVVAIAGDGGfqMN-LQELA---TAVRYNLPITVVVLNN 82
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
101-175 |
2.65e-04 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 43.55 E-value: 2.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759930713 101 FPKREESEYDTFGVGHSSTSIGAalGMAVAAKTLGVDRKSVAIIGDGAMTAGQAFEALNNAGAMDTDLLVILNDN 175
Cdd:PLN02269 126 FYKKDANFYGGHGIVGAQVPLGA--GLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIFVCENN 198
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
120-175 |
3.90e-04 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 41.81 E-value: 3.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 759930713 120 SIGAALGMAVAAKTLGVDRKSVAIIGDG-AMTAGQafeALNNAGAMDTDLLVILNDN 175
Cdd:cd02002 50 GLGWGLPAAVGAALANPDRKVVAIIGDGsFMYTIQ---ALWTAARYGLPVTVVILNN 103
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
487-562 |
7.63e-04 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 42.21 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 487 LPIGKGVVRRRGKQVAILAFGSMVH-----PALAAAEALDATVADMRFVKPLDAELIRE-LAQTHELvVTVEENVVMGGA 560
Cdd:PRK11892 329 LPIGKARIHREGKDVTIVSFSIGMTyalkaAEELAKEGIDAEVIDLRTIRPMDTETIVEsVKKTNRL-VTVEEGWPQSGV 407
|
..
gi 759930713 561 GS 562
Cdd:PRK11892 408 GA 409
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
63-175 |
5.54e-03 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 39.76 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759930713 63 TPHDR-LVWDVG-HQTYPHKILTGRRERmhTMRQHNGLAgfpkreeseydtfgvghsstSIGAALGMAVAAKTLGVDRKS 140
Cdd:COG0028 376 LPDDAiVVTDVGqHQMWAARYLRFRRPR--RFLTSGGLG--------------------TMGYGLPAAIGAKLARPDRPV 433
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 759930713 141 VAIIGDGA--MTaGQAFEAlnnagAMDTDL---LVILNDN 175
Cdd:COG0028 434 VAITGDGGfqMN-LQELAT-----AVRYGLpvkVVVLNNG 467
|
|
| |
