|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
1-619 |
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: 1213.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 1 MYDLLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHK 80
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 81 ILTGRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNN 160
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 161 AGVSeDAKLLVILNDNDMSISPPVGALNRHLARLMSGRFYAAARAGVERVLS----VAPPVLELARKLEEHAKGMVVPAT 236
Cdd:COG1154 161 AGHL-KKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKklpgIGPPLYELARRAKEGLKGLVVPGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 237 LFEEFGFNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKPSATPAKKTY 316
Cdd:COG1154 240 LFEELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 317 TQVFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYD 396
Cdd:COG1154 320 TDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 397 QLIHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPNPTAVRYPRGSGT 476
Cdd:COG1154 400 QVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGNGP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 477 GVATVKEFTALPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFVKPIDAALVRELAETHD 551
Cdd:COG1154 480 GVELPAELEPLPIGKGEVLR-----EGKDVAILAFGTMVAEALEAAERLaaegiSATVVDARFVKPLDEELILELAREHD 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504537595 552 YLVTVEEGCLMGGAGSACVEALMESGVIRPVLQLGLPDQFIDHGDPAKLLSQCGLDSAGIAKSIRERF 619
Cdd:COG1154 555 LVVTVEEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELL 622
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-619 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 1104.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 1 MYDLLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHK 80
Cdd:PRK05444 3 KYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 81 ILTGRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQL-NGDDRFSIAVIGDGAMTAGMAFEAMN 159
Cdd:PRK05444 83 ILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLkGGEDRKVVAVIGDGALTGGMAFEALN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 160 NAGVSeDAKLLVILNDNDMSISPPVGALNRHLARLMSGrfyaaaragvervlsvappvlelarkleehakgmvvpaTLFE 239
Cdd:PRK05444 163 NAGDL-KSDLIVILNDNEMSISPNVGALSNYLARLRSS--------------------------------------TLFE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 240 EFGFNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKP-SATPAKKTYTQ 318
Cdd:PRK05444 204 ELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPkSSKPGKPSYTK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 319 VFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYDQL 398
Cdd:PRK05444 284 VFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 399 IHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPN-PTAVRYPRGSGTG 477
Cdd:PRK05444 364 IHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDgPIAIRYPRGNGVG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 478 VAtVKEFTALPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADELD-ATVANMRFVKPIDAALVRELAETHDYLVTV 556
Cdd:PRK05444 444 VE-LPELEPLPIGKGEVLR-----EGEDVAILAFGTMLAEALKAAERLAsATVVDARFVKPLDEELLLELAAKHDLVVTV 517
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504537595 557 EEGCLMGGAGSACVEALMESGVIRPVLQLGLPDQFIDHGDPAKLLSQCGLDSAGIAKSIRERF 619
Cdd:PRK05444 518 EEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
5-616 |
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: 889.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 5 LKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILTG 84
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 85 RRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGvS 164
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAG-D 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 165 EDAKLLVILNDNDMSISPPVGALNRHLARLMSGRFYAAARAGVERVLSVAPPVLE-LARKLEEHAKGMVVPATLFEEFGF 243
Cdd:TIGR00204 160 LKTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNyLAKRTEESMKGLVVPGTFFEELGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 244 NYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKPSATPAKKTYTQVFGEW 323
Cdd:TIGR00204 240 NYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSALPSYSKIFSDT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 324 LCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYDQLIHDVA 403
Cdd:TIGR00204 320 LCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVC 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 404 LQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQ-QPNPTAVRYPRGSGTGVATVK 482
Cdd:TIGR00204 400 IQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHyDDGPIAVRYPRGNAVGVELTP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 483 EFTALPIGKGEVRRRssqpeGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFVKPIDAALVRELAETHDYLVTVE 557
Cdd:TIGR00204 480 EPEKLPIGKSEVLRK-----GEKILILGFGTLVPEALEVAESLnekgiEATVVDARFVKPLDEELILEIAASHEKLVTVE 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 504537595 558 EGCLMGGAGSACVEALMESGVIRPVLQLGLPDQFIDHGDPAKLLSQCGLDSAGIAKSIR 616
Cdd:TIGR00204 555 ENAIMGGAGSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKIL 613
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
5-277 |
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: 541.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 5 LKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILTG 84
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 85 RRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGvS 164
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAG-H 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 165 EDAKLLVILNDNDMSISPPVGALNRHLARLMSGRFYAAARAGVERVLS--VAPPVLELARKLEEHAKGMVVPATLFEEFG 242
Cdd:pfam13292 160 LKKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLKpkIGPPLYELARRAKESLKGLVVPGTLFEELG 239
|
250 260 270
....*....|....*....|....*....|....*
gi 504537595 243 FNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVT 277
Cdd:pfam13292 240 FKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
41-283 |
5.61e-126 |
|
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: 369.57 E-value: 5.61e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 41 GGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILTGRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTS 120
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 121 ISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGVsEDAKLLVILNDNDMSISPPVGalnrhlarlmsgrfy 200
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGY-LKSNMIVILNDNEMSISPNVG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 201 aaaragvervlsvappvlelarkleehakgmvVPATLFEEFGFNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKG 280
Cdd:cd02007 145 --------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKG 192
|
...
gi 504537595 281 QGY 283
Cdd:cd02007 193 KGY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
312-477 |
4.61e-50 |
|
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: 169.97 E-value: 4.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 312 AKKTYTQVFGEWLCDEAerdsrvvgitpamregsgmvefekrfkdryYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFL 391
Cdd:smart00861 1 KKIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 392 QRAYDQLIHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPNPTAVRYP 471
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
....*.
gi 504537595 472 RGSGTG 477
Cdd:smart00861 131 RKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
1-619 |
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: 1213.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 1 MYDLLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHK 80
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 81 ILTGRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNN 160
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 161 AGVSeDAKLLVILNDNDMSISPPVGALNRHLARLMSGRFYAAARAGVERVLS----VAPPVLELARKLEEHAKGMVVPAT 236
Cdd:COG1154 161 AGHL-KKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKklpgIGPPLYELARRAKEGLKGLVVPGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 237 LFEEFGFNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKPSATPAKKTY 316
Cdd:COG1154 240 LFEELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 317 TQVFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYD 396
Cdd:COG1154 320 TDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 397 QLIHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPNPTAVRYPRGSGT 476
Cdd:COG1154 400 QVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGNGP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 477 GVATVKEFTALPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFVKPIDAALVRELAETHD 551
Cdd:COG1154 480 GVELPAELEPLPIGKGEVLR-----EGKDVAILAFGTMVAEALEAAERLaaegiSATVVDARFVKPLDEELILELAREHD 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504537595 552 YLVTVEEGCLMGGAGSACVEALMESGVIRPVLQLGLPDQFIDHGDPAKLLSQCGLDSAGIAKSIRERF 619
Cdd:COG1154 555 LVVTVEEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELL 622
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-619 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 1104.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 1 MYDLLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHK 80
Cdd:PRK05444 3 KYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 81 ILTGRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQL-NGDDRFSIAVIGDGAMTAGMAFEAMN 159
Cdd:PRK05444 83 ILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLkGGEDRKVVAVIGDGALTGGMAFEALN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 160 NAGVSeDAKLLVILNDNDMSISPPVGALNRHLARLMSGrfyaaaragvervlsvappvlelarkleehakgmvvpaTLFE 239
Cdd:PRK05444 163 NAGDL-KSDLIVILNDNEMSISPNVGALSNYLARLRSS--------------------------------------TLFE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 240 EFGFNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKP-SATPAKKTYTQ 318
Cdd:PRK05444 204 ELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPkSSKPGKPSYTK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 319 VFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYDQL 398
Cdd:PRK05444 284 VFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 399 IHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPN-PTAVRYPRGSGTG 477
Cdd:PRK05444 364 IHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDgPIAIRYPRGNGVG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 478 VAtVKEFTALPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADELD-ATVANMRFVKPIDAALVRELAETHDYLVTV 556
Cdd:PRK05444 444 VE-LPELEPLPIGKGEVLR-----EGEDVAILAFGTMLAEALKAAERLAsATVVDARFVKPLDEELLLELAAKHDLVVTV 517
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504537595 557 EEGCLMGGAGSACVEALMESGVIRPVLQLGLPDQFIDHGDPAKLLSQCGLDSAGIAKSIRERF 619
Cdd:PRK05444 518 EEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
5-616 |
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: 889.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 5 LKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILTG 84
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 85 RRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGvS 164
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAG-D 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 165 EDAKLLVILNDNDMSISPPVGALNRHLARLMSGRFYAAARAGVERVLSVAPPVLE-LARKLEEHAKGMVVPATLFEEFGF 243
Cdd:TIGR00204 160 LKTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNyLAKRTEESMKGLVVPGTFFEELGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 244 NYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKPSATPAKKTYTQVFGEW 323
Cdd:TIGR00204 240 NYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSALPSYSKIFSDT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 324 LCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYDQLIHDVA 403
Cdd:TIGR00204 320 LCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVC 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 404 LQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQ-QPNPTAVRYPRGSGTGVATVK 482
Cdd:TIGR00204 400 IQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHyDDGPIAVRYPRGNAVGVELTP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 483 EFTALPIGKGEVRRRssqpeGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFVKPIDAALVRELAETHDYLVTVE 557
Cdd:TIGR00204 480 EPEKLPIGKSEVLRK-----GEKILILGFGTLVPEALEVAESLnekgiEATVVDARFVKPLDEELILEIAASHEKLVTVE 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 504537595 558 EGCLMGGAGSACVEALMESGVIRPVLQLGLPDQFIDHGDPAKLLSQCGLDSAGIAKSIR 616
Cdd:TIGR00204 555 ENAIMGGAGSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKIL 613
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
3-617 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 803.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 3 DLLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKIL 82
Cdd:PRK12571 7 PLLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCYPHKIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 83 TGRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAG 162
Cdd:PRK12571 87 TGRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYEALNNAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 163 vSEDAKLLVILNDNDMSISPPVGALNRHLARLMSGRFYAAARAGVERVLSVAP-PVLELARKLEEHAKGMVVPATLFEEF 241
Cdd:PRK12571 167 -AADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIAKGVEERLPgPLRDGARRARELVTGMIGGGTLFEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 242 GFNYIGPIDGHDLDSLIPTLQNIRE-LRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKPSATPAKKTYTQVF 320
Cdd:PRK12571 246 GFTYVGPIDGHDMEALLSVLRAARArADGPVLVHVVTEKGRGYAPAEADEDKYHAVGKFDVVTGLQKKSAPSAPSYTSVF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 321 GEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYDQLIH 400
Cdd:PRK12571 326 GEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQRGYDQLLH 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 401 DVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPN-PTAVRYPRGSGTGVA 479
Cdd:PRK12571 406 DVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDgPIAVRFPRGEGVGVE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 480 TVKEFTALPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADELDA-----TVANMRFVKPIDAALVRELAETHDYLV 554
Cdd:PRK12571 486 IPAEGTILGIGKGRVPR-----EGPDVAILSVGAHLHECLDAADLLEAegisvTVADPRFVKPLDEALTDLLVRHHIVVI 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504537595 555 TVEEGClMGGAGSACVEALMESGVI---RPVLQLGLPDQFIDHGDPAKLLSQCGLDSAGIAKSIRE 617
Cdd:PRK12571 561 VEEQGA-MGGFGAHVLHHLADTGLLdggLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTG 625
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
4-615 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 677.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 4 LLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILT 83
Cdd:PLN02582 33 LLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQSYPHKILT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 84 GRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGV 163
Cdd:PLN02582 113 GRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAGY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 164 SeDAKLLVILNDN-DMSI--------SPPVGALNRHLARLMSGRFYAAAR---AGVERvlSVAPPVLELARKLEEHAKGM 231
Cdd:PLN02582 193 L-DSDMIVILNDNkQVSLptatldgpAPPVGALSSALSRLQSSRPLRELRevaKGVTK--QIGGPMHELAAKVDEYARGM 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 232 V--VPATLFEEFGFNYIGPIDGHDLDSLIPTLQNIRELR--GPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKP 307
Cdd:PLN02582 270 IsgSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKttGPVLIHVVTEKGRGYPYAERAADKYHGVVKFDPATGKQF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 308 SATPAKKTYTQVFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIY 387
Cdd:PLN02582 350 KVKAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIY 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 388 STFLQRAYDQLIHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQ-QPNPT 466
Cdd:PLN02582 430 SSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAiDDRPS 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 467 AVRYPRGSGTGVATVKEFTALPI--GKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADELD-----ATVANMRFVKPID 539
Cdd:PLN02582 510 CFRYPRGNGIGVQLPPNNKGIPIevGKGRILL-----EGERVALLGYGTAVQSCLAAASLLErhglsATVADARFCKPLD 584
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504537595 540 AALVRELAETHDYLVTVEEGCLmGGAGSACVEALMESGVIRPVLQ---LGLPDQFIDHGDPAKLLSQCGLDSAGIAKSI 615
Cdd:PLN02582 585 RALIRSLAKSHEVLITVEEGSI-GGFGSHVAQFMALDGLLDGKLKwrpLVLPDRYIDHGAPADQLAEAGLTPSHIAATV 662
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
4-598 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 550.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 4 LLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILT 83
Cdd:PLN02234 66 LLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 84 GRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGV 163
Cdd:PLN02234 146 GRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGY 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 164 SeDAKLLVILNDNDM---------SISPPVGALNRHLARLMSGRFYAAARAgvervlsvappvlelarkleehakgmvvp 234
Cdd:PLN02234 226 L-HSNMIVILNDNKQvslptanldGPTQPVGALSCALSRLQSNCGMIRETS----------------------------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 235 ATLFEEFGFNYIGPIDGHDLDSLIPTLQNIRELR--GPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKPSATPA 312
Cdd:PLN02234 276 STLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQFKNISK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 313 KKTYTQVFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQ 392
Cdd:PLN02234 356 TQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQ 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 393 RAYDQLIHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQ-QPNPTAVRYP 471
Cdd:PLN02234 436 RAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAiDDRPSCFRYH 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 472 RGSGTGVATVKEFTALP--IGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADELDA-----TVANMRFVKPIDAALVR 544
Cdd:PLN02234 516 RGNGIGVSLPPGNKGVPlqIGRGRILR-----DGERVALLGYGSAVQRCLEAASMLSErglkiTVADARFCKPLDVALIR 590
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 504537595 545 ELAETHDYLVTVEEGCLmGGAGSACVEALMESGVIRPvlQLGLPDQFIDHGDPA 598
Cdd:PLN02234 591 SLAKSHEVLITVEEGSI-GGFGSHVVQFLALDGLLDG--KLKVYRTWITNGSTS 641
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
5-277 |
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: 541.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 5 LKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILTG 84
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 85 RRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGvS 164
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAG-H 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 165 EDAKLLVILNDNDMSISPPVGALNRHLARLMSGRFYAAARAGVERVLS--VAPPVLELARKLEEHAKGMVVPATLFEEFG 242
Cdd:pfam13292 160 LKKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLKpkIGPPLYELARRAKESLKGLVVPGTLFEELG 239
|
250 260 270
....*....|....*....|....*....|....*
gi 504537595 243 FNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVT 277
Cdd:pfam13292 240 FKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
4-615 |
5.03e-168 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 491.83 E-value: 5.03e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 4 LLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILT 83
Cdd:PRK12315 2 YLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKMLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 84 GRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGv 163
Cdd:PRK12315 82 GRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAA- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 164 SEDAKLLVILNDNDMSISPPVGALNRHLARLmsgrfyaaaragvervlsvappvlelaRKLEEHAkgmvvPATLFEEFGF 243
Cdd:PRK12315 161 ELKSNLIIIVNDNQMSIAENHGGLYKNLKEL---------------------------RDTNGQS-----ENNLFKAMGL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 244 NYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGiKPSATPAKKTYTQVFGEW 323
Cdd:PRK12315 209 DYRYVEDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKGYQPAEENKEAFHWHMPFDLETG-QSKVPASGESYSSVTLDY 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 324 LCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYDQLIHDVA 403
Cdd:PRK12315 288 LLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQRAYDQLSHDLA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 404 LQNLPVVFAIDRAGLVGADgATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTAL-QQPNPTAVRYPRGS-GTGVATV 481
Cdd:PRK12315 368 INNNPAVMIVFGGSISGND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALtQHEHPVAIRVPEHGvESGPTVD 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 482 KEFTALpigKGEVRRRssqpeGKRVAILAFGTM------VAPSLAAADELDATVANMRFVKPIDAALVRELAETHDYLVT 555
Cdd:PRK12315 447 TDYSTL---KYEVTKA-----GEKVAILALGDFyelgekVAKKLKEELGIDATLINPKFITGLDEELLEKLKEDHELVVT 518
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 556 VEEGCLMGGAGSACVEALMESGVirPVLQLGLPDQFIDHGDPAKLLSQCGLDSAGIAKSI 615
Cdd:PRK12315 519 LEDGILDGGFGEKIARYYGNSDM--KVLNYGAKKEFNDRVPVEELYKRNHLTPEQIVEDI 576
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
4-614 |
2.17e-135 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 412.19 E-value: 2.17e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 4 LLKTIDDPADLRRLDRRQLQPLADELRAfVLDSV--SKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKI 81
Cdd:PLN02225 78 ILDSIETPLQLKNLSVKELKLLADEIRT-ELHSVlwKKTQKSMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAHKV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 82 LTGRRDQMHTlRQYDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNA 161
Cdd:PLN02225 157 LTRRWSAIPS-RQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGKRDRVVAVIDNATITAGQAYEAMSNA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 162 GVSeDAKLLVILNDNDMSISP--------PVGALNRHLARLMSGRFYAAARAGVERVLS-VAPPVLELARKLEEHAKGMV 232
Cdd:PLN02225 236 GYL-DSNMIVILNDSRHSLHPnmeegskaSISALSSIMSKIQSSKIFRKFRELAKAMTKrIGKGMYEWAAKVDEYARGMV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 233 VP--ATLFEEFGFNYIGPIDGHDLDSLIPTLQNIREL--RGPQFLHVVTKKGQGyklaeadpvlyhgpgkfnpAEGIKPS 308
Cdd:PLN02225 315 GPtgSTLFEELGLYYIGPVDGHNIEDLVCVLREVSSLdsMGPVLVHVITEENRD-------------------AETGKNI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 309 ATPAKKTYTQVFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYS 388
Cdd:PLN02225 376 MVKDRRTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPS 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 389 TFLQRAYDQLIHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPN-PTA 467
Cdd:PLN02225 456 AFLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDrPVC 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 468 VRYPRGSGTGVATVKEfTALPIgkgEVRRRSSQPEGKRVAILAFGTMV-----APSLAAADELDATVANMRFVKPIDAAL 542
Cdd:PLN02225 536 FRFPRGSIVNMNYLVP-TGLPI---EIGRGRVLVEGQDVALLGYGAMVqnclhAHSLLSKLGLNVTVADARFCKPLDIKL 611
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504537595 543 VRELAETHDYLVTVEEGCLmGGAGSACVEALMESGVI------RPVLqlgLPDQFIDHGDPAKLLSQCGLDSAGIAKS 614
Cdd:PLN02225 612 VRDLCQNHKFLITVEEGCV-GGFGSHVAQFIALDGQLdgnikwRPIV---LPDGYIEEASPREQLALAGLTGHHIAAT 685
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
41-283 |
5.61e-126 |
|
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: 369.57 E-value: 5.61e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 41 GGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILTGRRDQMHTLRQYDGISGFPRRSESEYDTFGTAHSSTS 120
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 121 ISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGVsEDAKLLVILNDNDMSISPPVGalnrhlarlmsgrfy 200
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGY-LKSNMIVILNDNEMSISPNVG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 201 aaaragvervlsvappvlelarkleehakgmvVPATLFEEFGFNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKG 280
Cdd:cd02007 145 --------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKG 192
|
...
gi 504537595 281 QGY 283
Cdd:cd02007 193 KGY 195
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
313-617 |
1.39e-84 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 267.34 E-value: 1.39e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 313 KKTYTQVFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFL- 391
Cdd:COG3958 3 KKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 392 QRAYDQLIHDVALQNLPV-VFAIDrAGL-VGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPNPTAVR 469
Cdd:COG3958 83 GRAYEQIRNDIAYPNLNVkIVGSH-AGLsYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 470 YPRGsgtGVATV-KEFTALPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFVKPIDAALV 543
Cdd:COG3958 162 LGRG---AVPVVyDEDYEFEIGKARVLR-----EGKDVTIIATGIMVAEALEAAELLakegiSARVINMHTIKPLDEEAI 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504537595 544 RELAETHDYLVTVEEGCLMGGAGSACVEALMESGVIrPVLQLGLPDQFIDHGDPAKLLSQCGLDSAGIAKSIRE 617
Cdd:COG3958 234 LKAARKTGAVVTAEEHSIIGGLGSAVAEVLAENYPV-PLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKE 306
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
318-472 |
2.81e-76 |
|
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: 240.04 E-value: 2.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 318 QVFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFLQRAYDQ 397
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504537595 398 LIHDVALQNLPVVFAIDRAGL-VGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPNPTAVRYPR 472
Cdd:cd07033 81 IRHDVALQNLPVKFVGTHAGIsVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
312-473 |
2.43e-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: 175.05 E-value: 2.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 312 AKKTYTQVFGEWLCDEAERDSRVVGITPAMREGSGMVEFEKRFKD---RYYDVGIAEQHAVTFAGGLATEG--LKPVVAI 386
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 387 YSTFLQRAYDQLIHDVALQNLPVVFAIDRAGL-VGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQ--P 463
Cdd:pfam02779 81 FSDFLNRADDAIRHGAALGKLPVPFVVTRDPIgVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRdgR 160
|
170
....*....|
gi 504537595 464 NPTAVRYPRG 473
Cdd:pfam02779 161 KPVVLRLPRQ 170
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
312-477 |
4.61e-50 |
|
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: 169.97 E-value: 4.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 312 AKKTYTQVFGEWLCDEAerdsrvvgitpamregsgmvefekrfkdryYDVGIAEQHAVTFAGGLATEGLKPVVAIYSTFL 391
Cdd:smart00861 1 KKIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 392 QRAYDQLIHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPNPTAVRYP 471
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
....*.
gi 504537595 472 RGSGTG 477
Cdd:smart00861 131 RKSLYR 136
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
318-472 |
1.03e-33 |
|
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: 125.92 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 318 QVFGEWLCDEAerdsRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIY-STFLQRAYD 396
Cdd:cd06586 1 AAFAEVLTAWG----VRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTsGTGLLNAIN 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504537595 397 QLIhDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLH---TALQQPNPTAVRYPR 472
Cdd:cd06586 77 GLA-DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHairTAYASQGPVVVRLPR 154
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
490-611 |
4.65e-30 |
|
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: 114.62 E-value: 4.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 490 GKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFVKPIDAALVRELAETHDYLVTVEEGCLMGG 564
Cdd:pfam02780 1 GKAEILR-----EGDDVTIVAYGSMVEEALEAAELLakegiSAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGG 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 504537595 565 AGSACVEALMES---GVIRPVLQLGLPDqFIDHGDPAKLLSQCGLDSAGI 611
Cdd:pfam02780 76 FGSEVAAALAEEafdGLDAPVLRVGGPD-FPEPGSADELEKLYGLTPEKI 124
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
15-617 |
3.37e-29 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 122.55 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 15 RRLDRRQLQPLADELRAFVLDSVSKTG-GH----LSS-NLGTVELTIALHYVFNTPN----DRIVWDVGHQT---YPHKI 81
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANsGHpgmpMGAaDIAYVLWTRFLRHDPKNPKwpnrDRFVLSAGHGSmllYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 82 LTG---RRDQMHTLRQYDGI-SGFPrrsesEYdtFGTAHSSTS-------ISAALGMAIGS----QLNGDDRFSI----- 141
Cdd:PRK05899 81 LAGydlSIDDLKNFRQLGSKtPGHP-----EY--GHTPGVETTtgplgqgLANAVGMALAEkylaALFNRPGLDIvdhyt 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 142 -AVIGDGAMTAGMAFEAMNNAGVSEDAKLLVILNDNDMSISPPVgalnrhlarlmSGRFYA--AARagvervlsvappvl 218
Cdd:PRK05899 154 yVLCGDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPT-----------EGWFTEdvKKR-------------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 219 elarkleehakgmvvpatlFEEFGFNYIgPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVlYHGpgK 298
Cdd:PRK05899 209 -------------------FEAYGWHVI-EVDGHDVEAIDAAIEEAKASTKPTLIIAKTIIGKGAPNKEGTHK-VHG--A 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 299 FNPAEGIKPsatpAKK----TYTQVFGEWLCDEAERDSRVVG----ITPA-MREGSGMVEF-EKRFKDRYYDVGIAEQHA 368
Cdd:PRK05899 266 PLGAEEIAA----AKKelgwDYRKASGKALNALAKALPELVGgsadLAGSnNTKIKGSKDFaPEDYSGRYIHYGVREFAM 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 369 VTFAGGLATEG-LKPVVAIYSTFLQRAYDQlIHDVALQNLPVVFAIDRAGL-VGADGATHAGAYDLAFMRCIPNMTIMAA 446
Cdd:PRK05899 342 AAIANGLALHGgFIPFGGTFLVFSDYARNA-IRLAALMKLPVIYVFTHDSIgVGEDGPTHQPVEQLASLRAIPNLTVIRP 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 447 SDENECRQMLHTALQQPN-PTAVRYPRgSGTGVATVKEFTALPIGKGEVRRRSSQpegkrVAILAFGTMVAPSLAAADEL 525
Cdd:PRK05899 421 ADANETAAAWKYALERKDgPSALVLTR-QNLPVLERTAQEEGVAKGGYVLRDDPD-----VILIATGSEVHLALEAADEL 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 526 DA-----TVANMRFVKPIDA--ALVRE--LAETHDYLVTVEEGCLMGGAgsacvealmeSGVIRPVLQLGLpDQFIDHGD 596
Cdd:PRK05899 495 EAegikvRVVSMPSTELFDEqdAAYKEsvLPAAVTARVAVEAGVADGWY----------KYVGLDGKVLGI-DTFGASAP 563
|
650 660
....*....|....*....|.
gi 504537595 597 PAKLLSQCGLDSAGIAKSIRE 617
Cdd:PRK05899 564 ADELFKEFGFTVENIVAAAKE 584
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
350-575 |
7.57e-24 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 103.52 E-value: 7.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 350 FEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAI-YSTFLQRAYDQLIHDVA--------LQNLPVVFaidRA--GL 418
Cdd:PTZ00182 76 LDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFmFADFIFPAFDQIVNEAAkyrymsggQFDCPIVI---RGpnGA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 419 VGADGATHAGAYDLAFMRCiPNMTIMAASDENECRQMLHTALQQPNPTAVRYPR---GSGTGVATVKEFTaLPIGKGEVR 495
Cdd:PTZ00182 153 VGHGGAYHSQSFEAYFAHV-PGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKllyRESVEVVPEADYT-LPLGKAKVV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 496 RrssqpEGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFVKPIDA-ALVRELAETHDyLVTVEEGCLMGGAGSAC 569
Cdd:PTZ00182 231 R-----EGKDVTIVGYGSQVHVALKAAEELakegiSCEVIDLRSLRPWDReTIVKSVKKTGR-CVIVHEAPPTCGIGAEI 304
|
....*.
gi 504537595 570 VEALME 575
Cdd:PTZ00182 305 AAQIME 310
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
315-577 |
2.42e-19 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 89.40 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 315 TYTQVFGEWLCDEAERDSRV------VG-ITPAMREGSGMVEfekRF-KDRYYDVGIAEqHAvtFAG---GLATEGLKPV 383
Cdd:PRK09212 5 TVREALRDAMQEEMERDPKVflmgeeVGeYQGAYKVTQGLLE---QFgPKRVIDTPITE-HG--FAGlavGAAFAGLRPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 384 VAIYS-TFLQRAYDQLIHDVALQN--------LPVVFaidRA--GLVGADGATHAGAYDlAFMRCIPNMTIMAASDENEC 452
Cdd:PRK09212 79 VEFMTfNFSMQAIDQIVNSAAKTNymsggqlkCPIVF---RGpnGAAARVAAQHSQCYA-AWYSHIPGLKVVAPYFAADC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 453 RQMLHTALQQPNPTA-VRYPRGSGTGVATVKEFTALPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADEL-----D 526
Cdd:PRK09212 155 KGLLKTAIRDPNPVIfLENEILYGHSHEVPEEEESIPIGKAAILR-----EGSDVTIVTFSIQVKLALEAAELLekegiS 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 504537595 527 ATVANMRFVKPIDAALVRELAETHDYLVTVEEGCLMGGAGSACVEALMESG 577
Cdd:PRK09212 230 VEVIDLRTLRPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEA 280
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
324-575 |
3.50e-19 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 89.49 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 324 LCDEAERDSRVVGITPAMREGSGMVE-----FEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAIYS-TFLQRAYDQ 397
Cdd:PLN02683 37 LDEEMSADPKVFIMGEEVGEYQGAYKitkglLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTfNFSMQAIDH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 398 LIHDVALQN--------LPVVFAIDRAGLVGAdGATHAGAYDLAFMRCiPNMTIMAASDENECRQMLHTALQQPNPT--- 466
Cdd:PLN02683 117 IINSAAKTNymsagqisVPIVFRGPNGAAAGV-GAQHSQCFAAWYSSV-PGLKVLAPYSSEDARGLLKAAIRDPDPVvfl 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 467 ------AVRYPRgsgTGVATVKEFTaLPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFV 535
Cdd:PLN02683 195 enellyGESFPV---SAEVLDSSFV-LPIGKAKIER-----EGKDVTIVAFSKMVGYALKAAEILakegiSAEVINLRSI 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 504537595 536 KPIDAALVRELAETHDYLVTVEEGCLMGGAGSACVEALME 575
Cdd:PLN02683 266 RPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVE 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
27-295 |
4.89e-16 |
|
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: 78.31 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 27 DELRAFVLDSVSKTG-GHLSSNLGTVELTIAL-----HYVFNTPN----DRIVWDVGHQT---YPHKILTG--RRDQMHT 91
Cdd:cd02012 1 NRIRRLSIDMVQKAGsGHPGGSLSAADILAVLyfkvlKYDPADPKwpnrDRFVLSKGHASpalYAVLALAGylPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 92 LRQYDGI-SGFPrrsesEYDTFGTAHSSTS-----ISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGVSE 165
Cdd:cd02012 81 FRQLGSRlPGHP-----EYGLTPGVEVTTGslgqgLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 166 DAKLLVILNDNDMSIsppvgalnrhlarlmSGRfyaaaragVERVLSVAPpvleLARKleehakgmvvpatlFEEFGFNY 245
Cdd:cd02012 156 LDNLIAIVDSNRIQI---------------DGP--------TDDILFTED----LAKK--------------FEAFGWNV 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 504537595 246 IgPIDGHDLDSLIPTLQNIRELRG-PQFLHVVTKKGQGYKLAEaDPVLYHG 295
Cdd:cd02012 195 I-EVDGHDVEEILAALEEAKKSKGkPTLIIAKTIKGKGVPFME-NTAKWHG 243
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
349-577 |
1.52e-13 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 73.03 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 349 EFEKRfkdRYYDVGIAEQhavTFAG---GLATEGLKPVVAiYSTF---LQrAYDQLIHDVALQNL--------PVVFAid 414
Cdd:PRK11892 185 EFGAR---RVIDTPITEH---GFAGigvGAAFAGLKPIVE-FMTFnfaMQ-AIDQIINSAAKTLYmsggqmgcPIVFR-- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 415 raGLVGAD---GATHAGAYDlAFMRCIPNMTIMAASDENECRQMLHTALQQPNPTA-----VRYprGSGTGVATVKEFTa 486
Cdd:PRK11892 255 --GPNGAAarvAAQHSQDYA-AWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPVIfleneILY--GQSFDVPKLDDFV- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 487 LPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFVKPIDAALVRELAETHDYLVTVEEGCL 561
Cdd:PRK11892 329 LPIGKARIHR-----EGKDVTIVSFSIGMTYALKAAEELakegiDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEEGWP 403
|
250
....*....|....*.
gi 504537595 562 MGGAGSACVEALMESG 577
Cdd:PRK11892 404 QSGVGAEIAARVMEQA 419
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
15-303 |
1.31e-09 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 59.32 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 15 RRLDRRQLQPLADELRAFVLDSVSKTG-GHLSSNLGTVELTIALHY-VFN-TPN-------DRIVWDVGHQT---YPHKI 81
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGsGHPGGSLSAADILAALYFkVMNiDPKnpdwpdrDRFILSKGHAApalYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 82 LTGR--RDQMHTLRQYDGI-SGFPrrseseyDTFGTA---HSSTS----ISAALGMAIGSQLNGDDRFSIAVIGDGAMTA 151
Cdd:COG3959 81 EKGYfpKEELATFRKLGSRlQGHP-------DMKKTPgveMSTGSlgqgLSVAVGMALAAKLDGKDYRVYVLLGDGELQE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 152 GMAFEAMNNAgvsedAK-----LLVILNDNDMSIsppvgalnrhlarlmSGRfyaaaragVERVLSVAPpvleLARKlee 226
Cdd:COG3959 154 GQVWEAAMAA-----AHykldnLIAIVDRNGLQI---------------DGP--------TEDVMSLEP----LAEK--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 227 hakgmvvpatlFEEFGFNYIgPIDGHDLDSLIPTLQNIRELRG-PQF--LHvvTKKGQGYKLAEADPvLYHGpGKFNPAE 303
Cdd:COG3959 199 -----------WEAFGWHVI-EVDGHDIEALLAALDEAKAVKGkPTViiAH--TVKGKGVSFMENRP-KWHG-KAPNDEE 262
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
324-465 |
2.83e-09 |
|
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: 56.33 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 324 LCDEAERDSRVV--GITPAMREGS-----GMveFEKRFKDRYYDVGIAEQHAVTFAGGLATEGLKPVVAI-YSTFLQRAY 395
Cdd:cd07036 7 LDEEMERDPRVVvlGEDVGDYGGVfkvtkGL--LDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFALPAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 396 DQLIHDVA--------LQNLPVVFaidRA--GLVGADGATHAGAYDlAFMRCIPNMTIMAASDENECRQMLHTALQQPNP 465
Cdd:cd07036 85 DQIVNEAAklrymsggQFKVPIVI---RGpnGGGIGGGAQHSQSLE-AWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
326-576 |
2.08e-08 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 56.29 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 326 DEAERDSRVVGITPAMREGSGMVEFEKRFKDRY-----YDVGIAEQHAVTFAGGLATEGLKPVV-AIYSTFLQRAYDQLI 399
Cdd:CHL00144 16 EEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYgdlrvLDTPIAENSFTGMAIGAAMTGLRPIVeGMNMGFLLLAFNQIS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 400 HDVALQ--------NLPVVfaIDRAGLVGAD-GATHAGAYDlAFMRCIPNMTIMAASDENECRQMLHTALQQPNPT---- 466
Cdd:CHL00144 96 NNAGMLhytsggnfTIPIV--IRGPGGVGRQlGAEHSQRLE-SYFQSVPGLQIVACSTPYNAKGLLKSAIRSNNPViffe 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 467 -AVRYprgsgtgvaTVKEFTA-----LPIGKGEVRRrssqpEGKRVAILAFGTMVAPSLAAADEL-----DATVANMRFV 535
Cdd:CHL00144 173 hVLLY---------NLKEEIPdneylLPLEKAEVVR-----PGNDITILTYSRMRHHVLQAVKVLvekgyDPEIIDLISL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 504537595 536 KPID-AALVRELAETHDYLVtVEEGCLMGGAGSACVEALMES 576
Cdd:CHL00144 239 KPLDlGTISKSVKKTHKVLI-VEECMKTGGIGAELIAQINEH 279
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
23-180 |
3.44e-07 |
|
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: 52.77 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 23 QPLADELRAFVLDSVSKTG-GHLSSNLGTVELTIAL--HYVFNTPN-------DRIVWDVGHQT---YPHKILTGRRDQM 89
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANsGHPGAPMGMAPIAEVLfkRFLKHNPNdpkwinrDRFVLSNGHGSmllYSLLHLTGYDLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 90 HTLRQYDGI-SGFPRRSESEYDT---FGTAHSSTSISAALGMAIG-----SQLNGD-----DRFSIAVIGDGAMTAGMAF 155
Cdd:pfam00456 83 EDLKSFRQLgSKTPGHPEFGHTAgveVTTGPLGQGIANAVGMAIAernlaATYNRPgfdivDHYTYVFLGDGCLMEGVSS 162
|
170 180
....*....|....*....|....*
gi 504537595 156 EAMNNAGVSEDAKLLVILNDNDMSI 180
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQISI 187
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
119-184 |
3.56e-07 |
|
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: 52.45 E-value: 3.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504537595 119 TSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGVsEDAKLLVILNDNDMSISPPV 184
Cdd:COG1071 131 GQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAV-WKLPVVFVCENNGYAISTPV 195
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
119-184 |
1.70e-06 |
|
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: 50.19 E-value: 1.70e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504537595 119 TSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGVsEDAKLLVILNDNDMSISPPV 184
Cdd:cd02000 108 GQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAAL-WKLPVIFVCENNGYAISTPT 172
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
52-277 |
2.69e-06 |
|
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: 48.02 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 52 ELTIALHYVFNtPNDRIVWDVGHQTYPHkiltgrrdqMHTLRQYDGisgfprrseseyDTFGTAHSSTSISAALGMAIGS 131
Cdd:cd00568 1 RVLAALRAALP-EDAIVVNDAGNSAYWA---------YRYLPLRRG------------RRFLTSTGFGAMGYGLPAAIGA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 132 QLNGDDRFSIAVIGDGAMtaGMAFEAMNNAgVSEDAKLLVILNDNDMSISPpvgalnrhlaRLMSGRFYAAARAGVERvl 211
Cdd:cd00568 59 ALAAPDRPVVCIAGDGGF--MMTGQELATA-VRYGLPVIVVVFNNGGYGTI----------RMHQEAFYGGRVSGTDL-- 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504537595 212 svappvlelarkleehakGMVVPATLFEEFGFNYIGPIDGHDLDsliPTLQNIRELRGPQFLHVVT 277
Cdd:cd00568 124 ------------------SNPDFAALAEAYGAKGVRVEDPEDLE---AALAEALAAGGPALIEVKT 168
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
354-468 |
5.12e-04 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 43.12 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 354 FKDRYYDVGIAEQHAVTFAGGLATEG-LKPVVAIYSTFLQRAYDQlIHDVALQNLPV--VFAIDRAGLvGADGATHAGAY 430
Cdd:PTZ00089 401 PEGRYIRFGVREHAMCAIMNGIAAHGgFIPFGATFLNFYGYALGA-VRLAALSHHPViyVATHDSIGL-GEDGPTHQPVE 478
|
90 100 110
....*....|....*....|....*....|....*....
gi 504537595 431 DLAFMRCIPNMTIMAASDENECRQMLHTALQQPN-PTAV 468
Cdd:PTZ00089 479 TLALLRATPNLLVIRPADGTETSGAYALALANAKtPTIL 517
|
|
| PLN02790 |
PLN02790 |
transketolase |
362-535 |
5.15e-04 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 43.09 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 362 GIAEQHAVTFAGGLA--TEGLKPVVAiysTFLQRAyDQLIHDV---ALQNLPVVFAI--DRAGLvGADGATHAGAYDLAF 434
Cdd:PLN02790 398 GVREHGMGAICNGIAlhSSGLIPYCA---TFFVFT-DYMRAAMrlsALSEAGVIYVMthDSIGL-GEDGPTHQPIEHLAS 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 435 MRCIPNMTIMAASDENECRQMLHTALQQPN-PTAVRYPRGSgtgVATVKEFTALPIGKGE-VRRRSSQPEGKRVAILAFG 512
Cdd:PLN02790 473 LRAMPNILMLRPADGNETAGAYKVAVTNRKrPTVLALSRQK---VPNLPGTSIEGVEKGGyVISDNSSGNKPDLILIGTG 549
|
170 180
....*....|....*....|...
gi 504537595 513 TMVAPSLAAADELDATVANMRFV 535
Cdd:PLN02790 550 SELEIAAKAAKELRKEGKKVRVV 572
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
112-223 |
6.57e-04 |
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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: 41.11 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504537595 112 FGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGA-MTAGMafEAMNNAgVSEDAKLLVILNDND---MS---ISPPV 184
Cdd:cd02008 44 LNAIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTfFHSGI--LGLINA-VYNKANITVVILDNRttaMTggqPHPGT 120
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90 100 110 120
....*....|....*....|....*....|....*....|
gi 504537595 185 GALNRHLARLMSgrFYAAARA-GVERVLSVAPPVLELARK 223
Cdd:cd02008 121 GKTLTEPTTVID--IEALVRAiGVKRVVVVDPYDLKAIRE 158
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| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
109-184 |
7.76e-03 |
|
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: 38.85 E-value: 7.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504537595 109 YDTFGTAHSSTSISAalGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGVSEDAKLLVILNdNDMSISPPV 184
Cdd:pfam00676 97 YGGNGILGAQVPLGA--GIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCEN-NQYGISTPA 169
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