|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
5-626 |
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: 925.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 5 LLARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLIT 84
Cdd:COG1154 4 LLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHKILT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 85 GRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRpDTFAVAVVGDGALPSGIVFEAMNNAG 164
Cdd:COG1154 84 GRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGE-DRKVVAVIGDGALTGGMAFEALNNAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 165 GLKRPFLLILNDNKMSICPRVGGLANYLDRIRMAPTYNDLNRRVKDWIRRLPLVGGFAERTMQTVKDAVKASVNGGMLFE 244
Cdd:COG1154 163 HLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPGIGPPLYELARRAKEGLKGLVVPGTLFE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 245 ELGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVLTDKGRGFAPAEADPVKFHAPQPFQKVekaggTVSVAPLKANAP 324
Cdd:COG1154 243 ELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPE-----TGEPKKSKSSAP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 325 SskaFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTFL 404
Cdd:COG1154 318 S---YTDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 405 QRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHNGPVSIRYP 484
Cdd:COG1154 395 QRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 485 K-TALEVVERLHPPRIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILrRDHGLRVGVVNARFVKPLDEAVILQTLTES 563
Cdd:COG1154 475 RgNGPGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERL-AAEGISATVVDARFVKPLDEELILELAREH 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503329994 564 PFVITVEEGCLMGGFGAAVLELANAHRIDTRhVTRLGLPDRFIMHAERDEQLAEVGLDVEGLV 626
Cdd:COG1154 554 DLVVTVEEGVLAGGFGSAVLEFLADAGLDVP-VLRLGLPDRFIEHGSRAELLAELGLDAEGIA 615
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-626 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 815.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 1 MTSALLARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPH 80
Cdd:PRK05444 2 PKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 81 KLITGRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRPDTFAVAVVGDGALPSGIVFEAM 160
Cdd:PRK05444 82 KILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 161 NNAGGLKRPFLLILNDNKMSICPRVGGLANYLDRIRMaptyndlnrrvkdwirrlplvggfaertmqtvkdavkasvngG 240
Cdd:PRK05444 162 NNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRS------------------------------------------S 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 241 MLFEELGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVLTDKGRGFAPAEADPVKFHAPQPFQKVEKAggtvsvaPLK 320
Cdd:PRK05444 200 TLFEELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGE-------QPK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 321 ANAPSSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIY 400
Cdd:PRK05444 273 SSKPGKPSYTKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIY 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 401 STFLQRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHN-GPV 479
Cdd:PRK05444 353 STFLQRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDdGPI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 480 SIRYPKTALEVVERLHPPRIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILRrdhglRVGVVNARFVKPLDEAVILQT 559
Cdd:PRK05444 433 AIRYPRGNGVGVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA-----SATVVDARFVKPLDEELLLEL 507
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503329994 560 LTESPFVITVEEGCLMGGFGAAVLELANAHRIDTrHVTRLGLPDRFIMHAERDEQLAEVGLDVEGLV 626
Cdd:PRK05444 508 AAKHDLVVTVEEGAIMGGFGSAVLEFLADHGLDV-PVLNLGLPDEFIDHGSREELLAELGLDAEGIA 573
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
6-625 |
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: 636.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 6 LARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLITG 85
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 86 RASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRpDTFAVAVVGDGALPSGIVFEAMNNAGG 165
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGA-DRKTVCVIGDGAITAGMAFEALNHAGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 166 LKRPFLLILNDNKMSICPRVGGLANYLDRIRMAPTYNDLNRRVKDWIRRLPLVGGFaerTMQTVKDAVKASVNGGMLFEE 245
Cdd:TIGR00204 160 LKTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNY---LAKRTEESMKGLVVPGTFFEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 246 LGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVLTDKGRGFAPAEADPVKFHAPQPFQkvekaggtVSVAPLKANAPS 325
Cdd:TIGR00204 237 LGFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFD--------LSTGCLPKSKSA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 326 SKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTFLQ 405
Cdd:TIGR00204 309 LPSYSKIFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 406 RSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHN-GPVSIRYP 484
Cdd:TIGR00204 389 RAYDQVVHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDdGPIAVRYP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 485 K---TALEVVERLHPprIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILrRDHGLRVGVVNARFVKPLDEAVILQTLT 561
Cdd:TIGR00204 469 RgnaVGVELTPEPEK--LPIGKSEVLRKGEKILILGFGTLVPEALEVAESL-NEKGIEATVVDARFVKPLDEELILEIAA 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503329994 562 ESPFVITVEEGCLMGGFGAAVLELANAHRIDTRhVTRLGLPDRFIMHAERDEQLAEVGLDVEGL 625
Cdd:TIGR00204 546 SHEKLVTVEENAIMGGAGSAVLEFLMDQNKLVP-VKRLGIPDFFIPHGTQEEVLAELGLDTAGM 608
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
6-282 |
6.71e-137 |
|
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: 401.79 E-value: 6.71e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 6 LARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLITG 85
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 86 RASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRPDTfAVAVVGDGALPSGIVFEAMNNAGG 165
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRK-VVAVIGDGALTGGMAFEALNNAGH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 166 LKRPFLLILNDNKMSICPRVGGLANYLDRIRMAPTYNDLNRRVKDWIRrlPLVGGFAERTMQTVKDAVKASVNGGMLFEE 245
Cdd:pfam13292 160 LKKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLK--PKIGPPLYELARRAKESLKGLVVPGTLFEE 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 503329994 246 LGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVLT 282
Cdd:pfam13292 238 LGFKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
42-288 |
1.88e-92 |
|
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: 284.44 E-value: 1.88e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 42 SAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLITGRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCA 121
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 122 ASTALGLKLGDELMGrPDTFAVAVVGDGALPSGIVFEAMNNAGGLKRPFLLILNDNKMSICPRVGglanyldrirmapty 201
Cdd:cd02007 81 ISAALGMAVARDLKG-KKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 202 ndlnrrvkdwirrlplvggfaertmqtvkdavkasvNGGMLFEELGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVL 281
Cdd:cd02007 145 ------------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVV 188
|
....*..
gi 503329994 282 TDKGRGF 288
Cdd:cd02007 189 TKKGKGY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
363-488 |
2.32e-40 |
|
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: 144.17 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 363 IRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTFLQRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGT 442
Cdd:smart00861 9 FGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSI 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 503329994 443 YDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHNGPVSIRYPKTAL 488
Cdd:smart00861 89 EDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKSL 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
5-626 |
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: 925.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 5 LLARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLIT 84
Cdd:COG1154 4 LLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHKILT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 85 GRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRpDTFAVAVVGDGALPSGIVFEAMNNAG 164
Cdd:COG1154 84 GRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGE-DRKVVAVIGDGALTGGMAFEALNNAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 165 GLKRPFLLILNDNKMSICPRVGGLANYLDRIRMAPTYNDLNRRVKDWIRRLPLVGGFAERTMQTVKDAVKASVNGGMLFE 244
Cdd:COG1154 163 HLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPGIGPPLYELARRAKEGLKGLVVPGTLFE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 245 ELGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVLTDKGRGFAPAEADPVKFHAPQPFQKVekaggTVSVAPLKANAP 324
Cdd:COG1154 243 ELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPE-----TGEPKKSKSSAP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 325 SskaFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTFL 404
Cdd:COG1154 318 S---YTDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 405 QRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHNGPVSIRYP 484
Cdd:COG1154 395 QRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 485 K-TALEVVERLHPPRIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILrRDHGLRVGVVNARFVKPLDEAVILQTLTES 563
Cdd:COG1154 475 RgNGPGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERL-AAEGISATVVDARFVKPLDEELILELAREH 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503329994 564 PFVITVEEGCLMGGFGAAVLELANAHRIDTRhVTRLGLPDRFIMHAERDEQLAEVGLDVEGLV 626
Cdd:COG1154 554 DLVVTVEEGVLAGGFGSAVLEFLADAGLDVP-VLRLGLPDRFIEHGSRAELLAELGLDAEGIA 615
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-626 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 815.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 1 MTSALLARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPH 80
Cdd:PRK05444 2 PKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 81 KLITGRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRPDTFAVAVVGDGALPSGIVFEAM 160
Cdd:PRK05444 82 KILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 161 NNAGGLKRPFLLILNDNKMSICPRVGGLANYLDRIRMaptyndlnrrvkdwirrlplvggfaertmqtvkdavkasvngG 240
Cdd:PRK05444 162 NNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRS------------------------------------------S 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 241 MLFEELGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVLTDKGRGFAPAEADPVKFHAPQPFQKVEKAggtvsvaPLK 320
Cdd:PRK05444 200 TLFEELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGE-------QPK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 321 ANAPSSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIY 400
Cdd:PRK05444 273 SSKPGKPSYTKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIY 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 401 STFLQRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHN-GPV 479
Cdd:PRK05444 353 STFLQRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDdGPI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 480 SIRYPKTALEVVERLHPPRIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILRrdhglRVGVVNARFVKPLDEAVILQT 559
Cdd:PRK05444 433 AIRYPRGNGVGVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA-----SATVVDARFVKPLDEELLLEL 507
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503329994 560 LTESPFVITVEEGCLMGGFGAAVLELANAHRIDTrHVTRLGLPDRFIMHAERDEQLAEVGLDVEGLV 626
Cdd:PRK05444 508 AAKHDLVVTVEEGAIMGGFGSAVLEFLADHGLDV-PVLNLGLPDEFIDHGSREELLAELGLDAEGIA 573
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
6-625 |
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: 636.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 6 LARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLITG 85
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 86 RASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRpDTFAVAVVGDGALPSGIVFEAMNNAGG 165
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGA-DRKTVCVIGDGAITAGMAFEALNHAGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 166 LKRPFLLILNDNKMSICPRVGGLANYLDRIRMAPTYNDLNRRVKDWIRRLPLVGGFaerTMQTVKDAVKASVNGGMLFEE 245
Cdd:TIGR00204 160 LKTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNY---LAKRTEESMKGLVVPGTFFEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 246 LGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVLTDKGRGFAPAEADPVKFHAPQPFQkvekaggtVSVAPLKANAPS 325
Cdd:TIGR00204 237 LGFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFD--------LSTGCLPKSKSA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 326 SKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTFLQ 405
Cdd:TIGR00204 309 LPSYSKIFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 406 RSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHN-GPVSIRYP 484
Cdd:TIGR00204 389 RAYDQVVHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDdGPIAVRYP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 485 K---TALEVVERLHPprIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILrRDHGLRVGVVNARFVKPLDEAVILQTLT 561
Cdd:TIGR00204 469 RgnaVGVELTPEPEK--LPIGKSEVLRKGEKILILGFGTLVPEALEVAESL-NEKGIEATVVDARFVKPLDEELILEIAA 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503329994 562 ESPFVITVEEGCLMGGFGAAVLELANAHRIDTRhVTRLGLPDRFIMHAERDEQLAEVGLDVEGL 625
Cdd:TIGR00204 546 SHEKLVTVEENAIMGGAGSAVLEFLMDQNKLVP-VKRLGIPDFFIPHGTQEEVLAELGLDTAGM 608
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-626 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 604.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 5 LLARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLIT 84
Cdd:PRK12571 8 LLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCYPHKILT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 85 GRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELmGRPDTFAVAVVGDGALPSGIVFEAMNNAG 164
Cdd:PRK12571 88 GRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARAL-GQPDGDVVAVIGDGSLTAGMAYEALNNAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 165 GLKRPFLLILNDNKMSICPRVGGLANYLDRIRMAPTYNDLNRRVKDWIRRLPlvgGFAERTMQTVKDAVKASVNGGMLFE 244
Cdd:PRK12571 167 AADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIAKGVEERLP---GPLRDGARRARELVTGMIGGGTLFE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 245 ELGFTYLGPIDGHHLPTLRAYLQKVK-KLNGPVLLHVLTDKGRGFAPAEADPVKFHApqpFQKVEKAGGTvsvaPLKAnA 323
Cdd:PRK12571 244 ELGFTYVGPIDGHDMEALLSVLRAARaRADGPVLVHVVTEKGRGYAPAEADEDKYHA---VGKFDVVTGL----QKKS-A 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 324 PSSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTF 403
Cdd:PRK12571 316 PSAPSYTSVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 404 LQRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHN-GPVSIR 482
Cdd:PRK12571 396 LQRGYDQLLHDVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDdGPIAVR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 483 YPKTALEVVERLHPPRI-ELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILRRDhGLRVGVVNARFVKPLDEAVILQTLT 561
Cdd:PRK12571 476 FPRGEGVGVEIPAEGTIlGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAE-GISVTVADPRFVKPLDEALTDLLVR 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503329994 562 ESPFVITVEEGClMGGFGAAVLE-LANAHRIDTRHVTR-LGLPDRFIMHAERDEQLAEVGLDVEGLV 626
Cdd:PRK12571 555 HHIVVIVEEQGA-MGGFGAHVLHhLADTGLLDGGLKLRtLGLPDRFIDHASREEMYAEAGLTAPDIA 620
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
5-620 |
1.01e-149 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 449.74 E-value: 1.01e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 5 LLARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLIT 84
Cdd:PLN02582 33 LLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQSYPHKILT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 85 GRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRPDTfAVAVVGDGALPSGIVFEAMNNAG 164
Cdd:PLN02582 113 GRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKNN-VVAVIGDGAMTAGQAYEAMNNAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 165 GLKRPFLLILNDNK-MSI--------CPRVGGLANYLDRIRMAPTYNDLNRRVKDWIRRLplvGGFAERTMQTVKDAVKA 235
Cdd:PLN02582 192 YLDSDMIVILNDNKqVSLptatldgpAPPVGALSSALSRLQSSRPLRELREVAKGVTKQI---GGPMHELAAKVDEYARG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 236 --SVNGGMLFEELGFTYLGPIDGHHLPTLRAYLQKVK--KLNGPVLLHVLTDKGRGFAPAEADPVKFHApqpFQKVEKAG 311
Cdd:PLN02582 269 miSGSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKstKTTGPVLIHVVTEKGRGYPYAERAADKYHG---VVKFDPAT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 312 GTVSVAPLKanapsSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKA 391
Cdd:PLN02582 346 GKQFKVKAK-----TQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 392 GARPVVDIYSTFLQRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEV------ 465
Cdd:PLN02582 421 GLKPFCAIYSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELfhmvat 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 466 AAMIDfglshNGPVSIRYPKTALEVVERlhPPR-----IELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILRRdHGLRV 540
Cdd:PLN02582 501 AAAID-----DRPSCFRYPRGNGIGVQL--PPNnkgipIEVGKGRILLEGERVALLGYGTAVQSCLAAASLLER-HGLSA 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 541 GVVNARFVKPLDEAVILQTLTESPFVITVEEGCLmGGFGAAVLE-LANAHRIDTRHVTR-LGLPDRFIMHAERDEQLAEV 618
Cdd:PLN02582 573 TVADARFCKPLDRALIRSLAKSHEVLITVEEGSI-GGFGSHVAQfMALDGLLDGKLKWRpLVLPDRYIDHGAPADQLAEA 651
|
..
gi 503329994 619 GL 620
Cdd:PLN02582 652 GL 653
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
6-282 |
6.71e-137 |
|
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: 401.79 E-value: 6.71e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 6 LARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLITG 85
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 86 RASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRPDTfAVAVVGDGALPSGIVFEAMNNAGG 165
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRK-VVAVIGDGALTGGMAFEALNNAGH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 166 LKRPFLLILNDNKMSICPRVGGLANYLDRIRMAPTYNDLNRRVKDWIRrlPLVGGFAERTMQTVKDAVKASVNGGMLFEE 245
Cdd:pfam13292 160 LKKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLK--PKIGPPLYELARRAKESLKGLVVPGTLFEE 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 503329994 246 LGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVLT 282
Cdd:pfam13292 238 LGFKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-582 |
9.91e-128 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 389.75 E-value: 9.91e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 5 LLARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLIT 84
Cdd:PRK12315 2 YLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKMLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 85 GRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRPDTFaVAVVGDGALPSGIVFEAMNNAG 164
Cdd:PRK12315 82 GRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNI-IAVIGDGSLSGGLALEGLNNAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 165 GLKRPFLLILNDNKMSICPRVGGLANYLDRIRmaptynDLNRRVKDwirrlplvggfaertmqtvkdavkasvNggmLFE 244
Cdd:PRK12315 161 ELKSNLIIIVNDNQMSIAENHGGLYKNLKELR------DTNGQSEN---------------------------N---LFK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 245 ELGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVLTDKGRGFAPAEADPVKFHAPQPFqkVEKAGGTVSVAPlkanap 324
Cdd:PRK12315 205 AMGLDYRYVEDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKGYQPAEENKEAFHWHMPF--DLETGQSKVPAS------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 325 sSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTFL 404
Cdd:PRK12315 277 -GESYSSVTLDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 405 QRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDgPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLS-HNGPVSIRY 483
Cdd:PRK12315 356 QRAYDQLSHDLAINNNPAVMIVFGGSISGND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTqHEHPVAIRV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 484 PKTALEVVERLHPPRIELgKAEVLDRQPDGTFLVFGAQVPTALRAAEILRRDHGLRVGVVNARFVKPLDEAVILQTLTES 563
Cdd:PRK12315 435 PEHGVESGPTVDTDYSTL-KYEVTKAGEKVAILALGDFYELGEKVAKKLKEELGIDATLINPKFITGLDEELLEKLKEDH 513
|
570
....*....|....*....
gi 503329994 564 PFVITVEEGCLMGGFGAAV 582
Cdd:PRK12315 514 ELVVTLEDGILDGGFGEKI 532
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
3-609 |
5.71e-124 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 382.14 E-value: 5.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 3 SALLARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKL 82
Cdd:PLN02234 64 TPLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 83 ITGRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRPDTfAVAVVGDGALPSGIVFEAMNN 162
Cdd:PLN02234 144 LTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNS-VVSVIGDGAMTAGQAYEAMNN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 163 AGGLKRPFLLILNDNKMSICPRVGglanyLDrirmAPTyndlnrrvkdwirrlPLVGGFAERTMQTVKDAVKASVNGGML 242
Cdd:PLN02234 223 AGYLHSNMIVILNDNKQVSLPTAN-----LD----GPT---------------QPVGALSCALSRLQSNCGMIRETSSTL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 243 FEELGFTYLGPIDGHHLPTLRAYLQKVK--KLNGPVLLHVLTDKGRGFAPAEADPVKFHAPQPFQKvekaggtvSVAPLK 320
Cdd:PLN02234 279 FEELGFHYVGPVDGHNIDDLVSILETLKstKTIGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDP--------ETGKQF 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 321 ANAPSSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIY 400
Cdd:PLN02234 351 KNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIY 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 401 STFLQRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLS-HNGPV 479
Cdd:PLN02234 431 SSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAiDDRPS 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 480 SIRYPKTALEVVERlhPP-----RIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILrRDHGLRVGVVNARFVKPLDEA 554
Cdd:PLN02234 511 CFRYHRGNGIGVSL--PPgnkgvPLQIGRGRILRDGERVALLGYGSAVQRCLEAASML-SERGLKITVADARFCKPLDVA 587
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 503329994 555 VILQTLTESPFVITVEEGCLmGGFGAAVLELAnahRIDTRHVTRLGLPDRFIMHA 609
Cdd:PLN02234 588 LIRSLAKSHEVLITVEEGSI-GGFGSHVVQFL---ALDGLLDGKLKVYRTWITNG 638
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
3-620 |
1.37e-96 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 312.42 E-value: 1.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 3 SALLARIAAPADLHTLTEAQLDQLACEMREELIRVVSRRSAH-FASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHK 81
Cdd:PLN02225 76 TPILDSIETPLQLKNLSVKELKLLADEIRTELHSVLWKKTQKsMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAHK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 82 LITGRASQLETiRSKGGLMGYPNPAESDFDLFMTGHAGCAASTALGLKLGDELMGRPDTfAVAVVGDGALPSGIVFEAMN 161
Cdd:PLN02225 156 VLTRRWSAIPS-RQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGKRDR-VVAVIDNATITAGQAYEAMS 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 162 NAGGLKRPFLLILNDNKMSICPR--------VGGLANYLDRIRMAPTYNDLNRRVKDWIRRlplVGGFAERTMQTVKDAV 233
Cdd:PLN02225 234 NAGYLDSNMIVILNDSRHSLHPNmeegskasISALSSIMSKIQSSKIFRKFRELAKAMTKR---IGKGMYEWAAKVDEYA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 234 KASV--NGGMLFEELGFTYLGPIDGHHLPTLRAYLQKVKKLN--GPVLLHVLTDKGRGFAPAEADPVKfhapqpfqkvek 309
Cdd:PLN02225 311 RGMVgpTGSTLFEELGLYYIGPVDGHNIEDLVCVLREVSSLDsmGPVLVHVITEENRDAETGKNIMVK------------ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 310 aggtvsvaplkanapSSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMA 389
Cdd:PLN02225 379 ---------------DRRTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLS 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 390 KAGARPVVDIYSTFLQRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMI 469
Cdd:PLN02225 444 SGGLKPFCIIPSAFLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMV 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 470 -DFGLSHNGPVSIRYPKTALEVVERLHPP--RIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILRRdHGLRVGVVNAR 546
Cdd:PLN02225 524 aTAAYVTDRPVCFRFPRGSIVNMNYLVPTglPIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSK-LGLNVTVADAR 602
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503329994 547 FVKPLDEAVILQTLTESPFVITVEEGCLmGGFGAAVLE-LANAHRIDTRHVTR-LGLPDRFIMHAERDEQLAEVGL 620
Cdd:PLN02225 603 FCKPLDIKLVRDLCQNHKFLITVEEGCV-GGFGSHVAQfIALDGQLDGNIKWRpIVLPDGYIEEASPREQLALAGL 677
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
42-288 |
1.88e-92 |
|
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: 284.44 E-value: 1.88e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 42 SAHFASNLGVVELCLALHLEFDFTRDRLIWDTGHQVYPHKLITGRASQLETIRSKGGLMGYPNPAESDFDLFMTGHAGCA 121
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 122 ASTALGLKLGDELMGrPDTFAVAVVGDGALPSGIVFEAMNNAGGLKRPFLLILNDNKMSICPRVGglanyldrirmapty 201
Cdd:cd02007 81 ISAALGMAVARDLKG-KKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 202 ndlnrrvkdwirrlplvggfaertmqtvkdavkasvNGGMLFEELGFTYLGPIDGHHLPTLRAYLQKVKKLNGPVLLHVL 281
Cdd:cd02007 145 ------------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVV 188
|
....*..
gi 503329994 282 TDKGRGF 288
Cdd:cd02007 189 TKKGKGY 195
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
331-626 |
6.32e-76 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 245.77 E-value: 6.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 331 DAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTFL-QRSYD 409
Cdd:COG3958 8 DAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLtGRAYE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 410 QIFQEVSLQNLPV-LFTLDrAGL-VGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHNGPVSIRYPKTA 487
Cdd:COG3958 88 QIRNDIAYPNLNVkIVGSH-AGLsYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRLGRGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 488 levVERLHPP--RIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILRRDhGLRVGVVNARFVKPLDEAVILQTLTESPF 565
Cdd:COG3958 167 ---VPVVYDEdyEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKE-GISARVINMHTIKPLDEEAILKAARKTGA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503329994 566 VITVEEGCLMGGFGAAVLELAnAHRIDTRhVTRLGLPDRFIMHAERDEQLAEVGLDVEGLV 626
Cdd:COG3958 243 VVTAEEHSIIGGLGSAVAEVL-AENYPVP-LRRIGVPDRFGESGSPEELLEKYGLDAEGIV 301
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
331-485 |
2.82e-63 |
|
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: 206.91 E-value: 2.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 331 DAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTFLQRSYDQ 410
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503329994 411 IFQEVSLQNLPVLFTLDRAGL-VGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHNGPVSIRYPK 485
Cdd:cd07033 81 IRHDVALQNLPVKFVGTHAGIsVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
363-488 |
2.32e-40 |
|
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: 144.17 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 363 IRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIYSTFLQRSYDQIFQEVSLQNLPVLFTLDRAGLVGSDGPTHHGT 442
Cdd:smart00861 9 FGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSI 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 503329994 443 YDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHNGPVSIRYPKTAL 488
Cdd:smart00861 89 EDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKSL 134
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
325-488 |
1.44e-35 |
|
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: 132.29 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 325 SSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQ---KIRDTYPERFFDVGICESHAVAFAAGMAKAGA--RPVVDI 399
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVtkgLLHPQGAGRVIDTGIAEQAMVGFANGMALHGPllPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 400 YSTFLQRSYDQIFQEVSLQNLPVLFTLDRAGL-VGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHNG- 477
Cdd:pfam02779 81 FSDFLNRADDAIRHGAALGKLPVPFVVTRDPIgVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|..
gi 503329994 478 -PVSIRYPKTAL 488
Cdd:pfam02779 161 kPVVLRLPRQLL 172
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
502-625 |
5.12e-28 |
|
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: 108.84 E-value: 5.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 502 GKAEVLDRQPDGTFLVFGAQVPTALRAAEILRRDhGLRVGVVNARFVKPLDEAVILQTLTESPFVITVEEGCLMGGFGAA 581
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKE-GISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 503329994 582 VLELANAHRIDTRH--VTRLGLPDrFIMHAERDEQLAEVGLDVEGL 625
Cdd:pfam02780 80 VAAALAEEAFDGLDapVLRVGGPD-FPEPGSADELEKLYGLTPEKI 124
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
315-580 |
5.69e-24 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 103.91 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 315 SVAPLKANAPSSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKI----RDTY-PERFFDVGICESHAVAFAAGMA 389
Cdd:PTZ00182 23 SSSTESKGATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCtkglLDKYgPDRVFDTPITEQGFAGFAIGAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 390 KAGARPVVDI-YSTFLQRSYDQIFQEV--------SLQNLPVLFtldRA--GLVGSDGPTHHGTYDiAWMRIFPHMVVMA 458
Cdd:PTZ00182 103 MNGLRPIAEFmFADFIFPAFDQIVNEAakyrymsgGQFDCPIVI---RGpnGAVGHGGAYHSQSFE-AYFAHVPGLKVVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 459 PGDGGEVAAMIDFGLSHNGPVSIRYPKTALEVVERLHPP---RIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILRRD 535
Cdd:PTZ00182 179 PSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEadyTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKE 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 503329994 536 hGLRVGVVNARFVKPLDEAVILQTLTESPFVITVEEGCLMGGFGA 580
Cdd:PTZ00182 259 -GISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGA 302
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
331-582 |
9.15e-22 |
|
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: 96.62 E-value: 9.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 331 DAVSSALFEAMARDPRVSVL-------------TAamcegnKLQkirDTY-PERFFDVGICESHAVAFAAGMAKAGARPV 396
Cdd:COG0022 8 EAINEALREEMERDPRVFVMgedvgkyggvfgvTK------GLQ---EKFgPDRVFDTPISEAGIVGAAIGAALAGLRPV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 397 VDI-YSTFLQRSYDQIFQEVS--------LQNLPVLF-TLDRAGlvGSDGPTHHGTYdIAWMRIFPHMVVMAPGDGGEVA 466
Cdd:COG0022 79 VEIqFADFIYPAFDQIVNQAAklrymsggQFKVPMVIrTPYGGG--IGAGAQHSQSL-EAWFAHIPGLKVVAPSTPYDAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 467 AMIDFGLSHNGPVSIRYPKtAL-----EVVERlhPPRIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILrRDHGLRVG 541
Cdd:COG0022 156 GLLKAAIRDDDPVIFLEHK-RLyrlkgEVPEE--DYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEEL-AEEGISAE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 503329994 542 VVNARFVKPLDEAVILQTLTESPFVITVEEGCLMGGFGAAV 582
Cdd:COG0022 232 VIDLRTLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEI 272
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
125-626 |
5.82e-21 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 97.13 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 125 ALGLKLGDELMGRPDTFAV-----AVVGDGALPSGIVFEAMNNAGGLKrpfL----LILNDNKMSICPRVGG--LANYLD 193
Cdd:PRK05899 131 ALAEKYLAALFNRPGLDIVdhytyVLCGDGDLMEGISHEACSLAGHLK---LgnliVIYDDNRISIDGPTEGwfTEDVKK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 194 RirmaptyndlnrrvkdwirrlplvggfaertmqtvkdavkasvnggmlFEELGFTYLgPIDGHHLPTLRAYLQKVKKLN 273
Cdd:PRK05899 208 R------------------------------------------------FEAYGWHVI-EVDGHDVEAIDAAIEEAKAST 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 274 GPVLLHVLTDKGRGfAPAEADPVKFH-APQPFQKVEKAggtvsvapLKA-NAPSSKAFTDAVSsALFEAMAR------DP 345
Cdd:PRK05899 239 KPTLIIAKTIIGKG-APNKEGTHKVHgAPLGAEEIAAA--------KKElGWDYRKASGKALN-ALAKALPElvggsaDL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 346 RVSVLTAAMCEGNKLqkiRDTYPERFFDVGICESHAVAFAAGMAKAGA-RPVVDIYSTFLQRSYDQIfqEVS-LQNLPVL 423
Cdd:PRK05899 309 AGSNNTKIKGSKDFA---PEDYSGRYIHYGVREFAMAAIANGLALHGGfIPFGGTFLVFSDYARNAI--RLAaLMKLPVI 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 424 FTLDRAGL-VGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGL-SHNGPVSIRYPKTALEVVERLHP-PRIE 500
Cdd:PRK05899 384 YVFTHDSIgVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGPSALVLTRQNLPVLERTAQeEGVA 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 501 LGkAEVLDRQPDGTFLVFGAQVPTALRAAEILRRDhGLRVGVVNARFVKPLDEAVilQTLTESPF------VITVEEGCL 574
Cdd:PRK05899 464 KG-GYVLRDDPDVILIATGSEVHLALEAADELEAE-GIKVRVVSMPSTELFDEQD--AAYKESVLpaavtaRVAVEAGVA 539
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 503329994 575 MGGfgaavlelanaHRIDTRHVTRLGLpDRFIMHAERDEQLAEVGLDVEGLV 626
Cdd:PRK05899 540 DGW-----------YKYVGLDGKVLGI-DTFGASAPADELFKEFGFTVENIV 579
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
336-485 |
5.23e-20 |
|
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: 87.02 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 336 ALFEAMARDPRVSVLTAAMCEGNKLQKIRDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDIY-STFLQRSYDQIFqE 414
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTsGTGLLNAINGLA-D 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503329994 415 VSLQNLPVLFTLDRAGLVGSDGPTHHGTYDIAWMRIFPHMVVMAPgDGGEVAAMIDFGL----SHNGPVSIRYPK 485
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSP-SPAELPAGIDHAIrtayASQGPVVVRLPR 154
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
331-592 |
1.18e-19 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 90.55 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 331 DAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIR----DTY-PERFFDVGICESHAVAFAAGMAKAGARPVVDIYS-TFL 404
Cdd:PRK09212 8 EALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTqgllEQFgPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFMTfNFS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 405 QRSYDQIFQEVSLQN--------LPVLFtldRA--GLVGSDGPTHHGTYDiAWMRIFPHMVVMAPGDGGEVAAMIDFGLS 474
Cdd:PRK09212 88 MQAIDQIVNSAAKTNymsggqlkCPIVF---RGpnGAAARVAAQHSQCYA-AWYSHIPGLKVVAPYFAADCKGLLKTAIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 475 HNGPV-----SIRYpKTALEVVERLHPprIELGKAEVLDRQPDGTFLVFGAQVPTALRAAEILRRDhGLRVGVVNARFVK 549
Cdd:PRK09212 164 DPNPViflenEILY-GHSHEVPEEEES--IPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKE-GISVEVIDLRTLR 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 503329994 550 PLDEAVILQTLTESPFVITVEEGCLMGGFGAAVLELANAHRID 592
Cdd:PRK09212 240 PLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMKEAFD 282
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
313-582 |
3.37e-18 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 86.80 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 313 TVSVAPLKANAPSSKAFTDAVSSALFEAMARDPRVSVLTAAMCEGNKLQKIR----DTY-PERFFDVGICESHAVAFAAG 387
Cdd:PLN02683 13 AAAAARGYASAAKEMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITkgllQKYgPDRVLDTPITEAGFTGIGVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 388 MAKAGARPVVDIYS-TFLQRSYDQIFQEVSLQN--------LPVLFTLDRAGLVGSdGPTHHGTYdIAWMRIFPHMVVMA 458
Cdd:PLN02683 93 AAYAGLKPVVEFMTfNFSMQAIDHIINSAAKTNymsagqisVPIVFRGPNGAAAGV-GAQHSQCF-AAWYSSVPGLKVLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 459 PGDGGEVAAMIDFGLSHNGPVSI---------RYPKTAlEVVERLHPprIELGKAEVLDRQPDGTFLVFGAQVPTALRAA 529
Cdd:PLN02683 171 PYSSEDARGLLKAAIRDPDPVVFlenellygeSFPVSA-EVLDSSFV--LPIGKAKIEREGKDVTIVAFSKMVGYALKAA 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 503329994 530 EILRRDhGLRVGVVNARFVKPLDEAVILQTLTESPFVITVEEGCLMGGFGAAV 582
Cdd:PLN02683 248 EILAKE-GISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEI 299
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
331-479 |
1.53e-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: 60.18 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 331 DAVSSALFEAMARDPRVSVL--TAAMCEG-NKLQK-IRDTY-PERFFDVGICESHAVAFAAGMAKAGARPVVDI-YSTFL 404
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLgeDVGDYGGvFKVTKgLLDKFgPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 405 QRSYDQIFQEVS--------LQNLPVLFtldRA--GLVGSDGPTHHGTYDiAWMRIFPHMVVMAPGDGGEVAAMIDFGLS 474
Cdd:cd07036 81 LPAFDQIVNEAAklrymsggQFKVPIVI---RGpnGGGIGGGAQHSQSLE-AWFAHIPGLKVVAPSTPYDAKGLLKAAIR 156
|
....*
gi 503329994 475 HNGPV 479
Cdd:cd07036 157 DDDPV 161
|
|
| PLN02790 |
PLN02790 |
transketolase |
364-543 |
4.41e-08 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 56.18 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 364 RDTYPERFFDVGICESHAVAFAAGMA--KAGARPvvdIYSTFLQRS-YDQIFQEVS-LQNLPVLF--TLDRAGLvGSDGP 437
Cdd:PLN02790 387 KDTPEERNVRFGVREHGMGAICNGIAlhSSGLIP---YCATFFVFTdYMRAAMRLSaLSEAGVIYvmTHDSIGL-GEDGP 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 438 THHGTYDIAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHN-GPVSIRYPKTALEVVERLHPPRIELG----KAEVLDRQPD 512
Cdd:PLN02790 463 THQPIEHLASLRAMPNILMLRPADGNETAGAYKVAVTNRkRPTVLALSRQKVPNLPGTSIEGVEKGgyviSDNSSGNKPD 542
|
170 180 190
....*....|....*....|....*....|.
gi 503329994 513 GTFLVFGAQVPTALRAAEILRRDhGLRVGVV 543
Cdd:PLN02790 543 LILIGTGSELEIAAKAAKELRKE-GKKVRVV 572
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
356-540 |
2.68e-06 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 50.44 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 356 EGNKLQKirDTYPERFFDVGICESHAVAFAAGMAKAGARPVVDiySTFLQrSYDQIFQEV---SLQNLPVL--FTLDRAG 430
Cdd:PTZ00089 392 EANDFTK--ASPEGRYIRFGVREHAMCAIMNGIAAHGGFIPFG--ATFLN-FYGYALGAVrlaALSHHPVIyvATHDSIG 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 431 LvGSDGPTHHGTYDIAWMRIFPHMVVMAPGDGGEVAA--MIDF---------GLSHNGPVSIryPKTALEVVERlhppri 499
Cdd:PTZ00089 467 L-GEDGPTHQPVETLALLRATPNLLVIRPADGTETSGayALALanaktptilCLSRQNTPPL--PGSSIEGVLK------ 537
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503329994 500 elgKAEVLDRQPDGTFLVF---GAQVPTALRAAEILRRDHGLRV 540
Cdd:PTZ00089 538 ---GAYIVVDFTNSPQLILvasGSEVSLCVEAAKALSKELNVRV 578
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
289-580 |
8.54e-06 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 48.76 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 289 APAEADPVKFHAPQPFQKVEKAGGTVSVAPLKANAPSSKAFTDAVSS----ALFEAMA----RDPRVSVLTAAMCEGNKL 360
Cdd:PRK11892 96 EAAAAAPAAAAAAAAKKAAPAPAAPAAPAAEVAADPDIPAGTEMVTMtvreALRDAMAeemrRDEDVFVMGEEVAEYQGA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 361 QKIR----DTY-PERFFDVGICEsHAVA-FAAGMAKAGARPVVDiYSTF---LQrSYDQIFQEVSLQNL--------PVL 423
Cdd:PRK11892 176 YKVTqgllQEFgARRVIDTPITE-HGFAgIGVGAAFAGLKPIVE-FMTFnfaMQ-AIDQIINSAAKTLYmsggqmgcPIV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 424 FtldR-----AGLVGSDgptHHGTYDiAWMRIFPHMVVMAPGDGGEVAAMIDFGLSHNGPV-----SIRYPKTaLEVver 493
Cdd:PRK11892 253 F---RgpngaAARVAAQ---HSQDYA-AWYSHIPGLKVVAPYSAADAKGLLKAAIRDPNPViflenEILYGQS-FDV--- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 494 lhpPRIE-----LGKAEVLDRQPDGTFLVFGAQVPTALRAAEILRRDhGLRVGVVNARFVKPLDEAVILQTLTESPFVIT 568
Cdd:PRK11892 322 ---PKLDdfvlpIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKE-GIDAEVIDLRTIRPMDTETIVESVKKTNRLVT 397
|
330
....*....|..
gi 503329994 569 VEEGCLMGGFGA 580
Cdd:PRK11892 398 VEEGWPQSGVGA 409
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
94-177 |
4.42e-04 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 43.16 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503329994 94 RSKGGLMGYPNPAESdfdlFMTGHAGCAASTALGLKLG-DELMGRPDTFAVAVVGDGALPSGIVFEAMNNAGGLKRPFLL 172
Cdd:PLN02269 118 RGKGGSMHFYKKDAN----FYGGHGIVGAQVPLGAGLAfAQKYNKEENVAFALYGDGAANQGQLFEALNIAALWDLPVIF 193
|
....*
gi 503329994 173 ILNDN 177
Cdd:PLN02269 194 VCENN 198
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
121-181 |
2.54e-03 |
|
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: 40.56 E-value: 2.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503329994 121 AASTALGLKLGDElmgrpDTFAVAVVGDGALPSGIVFEAMNNAGGLKRPFLLILNDNKMSI 181
Cdd:cd02000 113 AAGAALALKYRGE-----DRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCENNGYAI 168
|
|
| |
