|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
48-719 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 1405.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 48 QVKKRSRTVQASLS--ESGEYYTQRPPTPILDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELT 125
Cdd:PLN02582 4 LRSNRPSGVCASLSpeESAEYPSQRPPTPLLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 126 VALHYVFNAPQDRILWDVGHQSYPHKILTGRREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLK 205
Cdd:PLN02582 84 VALHYVFNAPQDKILWDVGHQSYPHKILTGRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 206 GRNNNVIAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNRQVSLPTATLDGPVPPVGALSSALSRLQSNRPLRELREV 285
Cdd:PLN02582 164 GKKNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLPTATLDGPAPPVGALSSALSRLQSSRPLRELREV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 286 AKGVTKQIGGPMHELAAKVDEYARGMISGSGSTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKTTGPVLIHVVTEKGR 365
Cdd:PLN02582 244 AKGVTKQIGGPMHELAAKVDEYARGMISGSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKTTGPVLIHVVTEKGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 366 GYPYAERAADKYHGVAKFDPATGKQFKGSAKTQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDV 445
Cdd:PLN02582 324 GYPYAERAADKYHGVVKFDPATGKQFKVKAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 446 GIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNM 525
Cdd:PLN02582 404 GIAEQHAVTFAAGLACEGLKPFCAIYSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNM 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 526 VVMAPSDEAELFHIVATAAAIDDRPSCFRYPRGNGIGVELPAGNKGIPLEVGKGRILVEGERVALLGYGSAVQNCLAAAS 605
Cdd:PLN02582 484 VVMAPSDEAELFHMVATAAAIDDRPSCFRYPRGNGIGVQLPPNNKGIPIEVGKGRILLEGERVALLGYGTAVQSCLAAAS 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 606 VLESRGLQVTVADARFCKPLDRALIRSLAKSHEVLVTVEEGSIGGFGSHVVQFMALDGLLDGKLKWRPIVLPDRYIDHGS 685
Cdd:PLN02582 564 LLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEGSIGGFGSHVAQFMALDGLLDGKLKWRPLVLPDRYIDHGA 643
|
650 660 670
....*....|....*....|....*....|....
gi 2165115855 686 PADQLAEAGLTPSHIAATVFNILGQTREALEVMT 719
Cdd:PLN02582 644 PADQLAEAGLTPSHIAATVLNVLGQTREALQIMS 677
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
72-709 |
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: 1039.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 72 PTPILDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHK 151
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 152 ILTGRREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNN 231
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 232 AGYLDSDMIVILNDN-RQVSlptatldgpvPPVGALSSALSRLQSNRPLRELREVAKGVTKQ---IGGPMHELAAKVDEY 307
Cdd:COG1154 161 AGHLKKDLIVILNDNeMSIS----------PNVGALSNYLARLRTSPTYNKLREEVKKLLKKlpgIGPPLYELARRAKEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 308 ARGMISGSgsTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKttGPVLIHVVTEKGRGYPYAERAADKYHGVAKFDPAT 387
Cdd:COG1154 231 LKGLVVPG--TLFEELGFKYIGPIDGHDLDALVETLRNAKDLK--GPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPET 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 388 GKQFKGSAKTQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPF 467
Cdd:COG1154 307 GEPKKSKSSAPSYTDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 468 CAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAId 547
Cdd:COG1154 387 VAIYSTFLQRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 548 DRPSCFRYPRGNGIGVELPAgnKGIPLEVGKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDR 627
Cdd:COG1154 466 DGPTAIRYPRGNGPGVELPA--ELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDE 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 628 ALIRSLAKSHEVLVTVEEGSI-GGFGSHVVQFMALDGLLdgkLKWRPIVLPDRYIDHGSPADQLAEAGLTPSHIAATVFN 706
Cdd:COG1154 544 ELILELAREHDLVVTVEEGVLaGGFGSAVLEFLADAGLD---VPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILE 620
|
...
gi 2165115855 707 ILG 709
Cdd:COG1154 621 LLG 623
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
76-709 |
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: 735.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 76 LDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHKILTG 155
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 156 RREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGYL 235
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 236 DSDMIVILNDNrQVSLPtatldgpvPPVGALSSALSRLQSNRPLRELREVAKGVTKQIGGPMHELAAKVDEYARGMISGS 315
Cdd:TIGR00204 161 KTDMIVILNDN-EMSIS--------ENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYLAKRTEESMKGLVVPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 316 gsTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKttGPVLIHVVTEKGRGYPYAERAADKYHGVAKFDPATGKQFKGSA 395
Cdd:TIGR00204 232 --TFFEELGFNYIGPVDGHDLLELIETLKNAKKLK--GPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 396 KTQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFM 475
Cdd:TIGR00204 308 ALPSYSKIFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 476 QRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAIDDRPSCFRY 555
Cdd:TIGR00204 388 QRAYDQVVHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRY 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 556 PRGNGIGVELPAGNKGIPLevGKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDRALIRSLAK 635
Cdd:TIGR00204 468 PRGNAVGVELTPEPEKLPI--GKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAA 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2165115855 636 SHEVLVTVEEGSI-GGFGSHVVQFMALDGLLDGKLKwrpIVLPDRYIDHGSPADQLAEAGLTPSHIAATVFNILG 709
Cdd:TIGR00204 546 SHEKLVTVEENAImGGAGSAVLEFLMDQNKLVPVKR---LGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
76-361 |
4.26e-164 |
|
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: 473.05 E-value: 4.26e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 76 LDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHKILTG 155
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 156 RREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGYL 235
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 236 DSDMIVILNDN-RQVSlptatldgpvPPVGALSSALSRLQSNRPLRELREVAKGVTK-QIGGPMHELAAKVDEYARGMIs 313
Cdd:pfam13292 161 KKDLIVILNDNeMSIS----------PNVGALSNYLSRLRTSPTYNRLKEEVKKLLKpKIGPPLYELARRAKESLKGLV- 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2165115855 314 gSGSTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKttGPVLIHVVT 361
Cdd:pfam13292 230 -VPGTLFEELGFKYIGPIDGHDLDALVKVLENAKDLK--GPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
112-367 |
7.67e-123 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 364.56 E-value: 7.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 112 GGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHKILTGRREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTT 191
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 192 ISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNRQVSLPTAtldgpvppvgalssals 271
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNV----------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 272 rlqsnrplrelrevakgvtkqiggpmhelaakvdeyargmisGSGSTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKt 351
Cdd:cd02007 144 ------------------------------------------GTPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLK- 180
|
250
....*....|....*.
gi 2165115855 352 tGPVLIHVVTEKGRGY 367
Cdd:cd02007 181 -GPVLLHVVTKKGKGY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
443-562 |
2.47e-46 |
|
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: 161.11 E-value: 2.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 443 FDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACL 522
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2165115855 523 PNMVVMAPSDEAELFHIVATAAAiDDRPSCFRYPRGNGIG 562
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
48-719 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 1405.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 48 QVKKRSRTVQASLS--ESGEYYTQRPPTPILDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELT 125
Cdd:PLN02582 4 LRSNRPSGVCASLSpeESAEYPSQRPPTPLLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 126 VALHYVFNAPQDRILWDVGHQSYPHKILTGRREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLK 205
Cdd:PLN02582 84 VALHYVFNAPQDKILWDVGHQSYPHKILTGRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 206 GRNNNVIAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNRQVSLPTATLDGPVPPVGALSSALSRLQSNRPLRELREV 285
Cdd:PLN02582 164 GKKNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLPTATLDGPAPPVGALSSALSRLQSSRPLRELREV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 286 AKGVTKQIGGPMHELAAKVDEYARGMISGSGSTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKTTGPVLIHVVTEKGR 365
Cdd:PLN02582 244 AKGVTKQIGGPMHELAAKVDEYARGMISGSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKTTGPVLIHVVTEKGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 366 GYPYAERAADKYHGVAKFDPATGKQFKGSAKTQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDV 445
Cdd:PLN02582 324 GYPYAERAADKYHGVVKFDPATGKQFKVKAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 446 GIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNM 525
Cdd:PLN02582 404 GIAEQHAVTFAAGLACEGLKPFCAIYSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNM 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 526 VVMAPSDEAELFHIVATAAAIDDRPSCFRYPRGNGIGVELPAGNKGIPLEVGKGRILVEGERVALLGYGSAVQNCLAAAS 605
Cdd:PLN02582 484 VVMAPSDEAELFHMVATAAAIDDRPSCFRYPRGNGIGVQLPPNNKGIPIEVGKGRILLEGERVALLGYGTAVQSCLAAAS 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 606 VLESRGLQVTVADARFCKPLDRALIRSLAKSHEVLVTVEEGSIGGFGSHVVQFMALDGLLDGKLKWRPIVLPDRYIDHGS 685
Cdd:PLN02582 564 LLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEGSIGGFGSHVAQFMALDGLLDGKLKWRPLVLPDRYIDHGA 643
|
650 660 670
....*....|....*....|....*....|....
gi 2165115855 686 PADQLAEAGLTPSHIAATVFNILGQTREALEVMT 719
Cdd:PLN02582 644 PADQLAEAGLTPSHIAATVLNVLGQTREALQIMS 677
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
72-709 |
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: 1039.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 72 PTPILDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHK 151
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 152 ILTGRREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNN 231
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 232 AGYLDSDMIVILNDN-RQVSlptatldgpvPPVGALSSALSRLQSNRPLRELREVAKGVTKQ---IGGPMHELAAKVDEY 307
Cdd:COG1154 161 AGHLKKDLIVILNDNeMSIS----------PNVGALSNYLARLRTSPTYNKLREEVKKLLKKlpgIGPPLYELARRAKEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 308 ARGMISGSgsTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKttGPVLIHVVTEKGRGYPYAERAADKYHGVAKFDPAT 387
Cdd:COG1154 231 LKGLVVPG--TLFEELGFKYIGPIDGHDLDALVETLRNAKDLK--GPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPET 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 388 GKQFKGSAKTQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPF 467
Cdd:COG1154 307 GEPKKSKSSAPSYTDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 468 CAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAId 547
Cdd:COG1154 387 VAIYSTFLQRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 548 DRPSCFRYPRGNGIGVELPAgnKGIPLEVGKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDR 627
Cdd:COG1154 466 DGPTAIRYPRGNGPGVELPA--ELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDE 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 628 ALIRSLAKSHEVLVTVEEGSI-GGFGSHVVQFMALDGLLdgkLKWRPIVLPDRYIDHGSPADQLAEAGLTPSHIAATVFN 706
Cdd:COG1154 544 ELILELAREHDLVVTVEEGVLaGGFGSAVLEFLADAGLD---VPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILE 620
|
...
gi 2165115855 707 ILG 709
Cdd:COG1154 621 LLG 623
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
1-687 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 1027.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 1 MALCAYAFPGILNRTVAVASdaSKPTPLFSewihgtdlqfqfhqkltqvKKRSRTVQASLSESGEYYTQRPPTPILDTIN 80
Cdd:PLN02234 13 MALSVFAFPSYINRNPSLKY--LKPSSMSS-------------------TKYSKVRATTFSEKGEYYSNRPPTPLLDTIN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 81 YPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHKILTGRREKM 160
Cdd:PLN02234 72 HPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTGRRGKM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 161 STLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGYLDSDMI 240
Cdd:PLN02234 152 KTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 241 VILNDNRQVSLPTATLDGPVPPVGALSSALSRLQSNRplrelrevakgvtkqiggpmhelaakvdeyarGMISGSGSTLF 320
Cdd:PLN02234 232 VILNDNKQVSLPTANLDGPTQPVGALSCALSRLQSNC--------------------------------GMIRETSSTLF 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 321 EELGLYYIGPVDGHNIDDLISILKEVRSTKTTGPVLIHVVTEKGRGYPYAERAADKYHGVAKFDPATGKQFKGSAKTQSY 400
Cdd:PLN02234 280 EELGFHYVGPVDGHNIDDLVSILETLKSTKTIGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQFKNISKTQSY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 401 TTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYD 480
Cdd:PLN02234 360 TSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 481 QVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAIDDRPSCFRYPRGNG 560
Cdd:PLN02234 440 QVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNG 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 561 IGVELPAGNKGIPLEVGKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDRALIRSLAKSHEVL 640
Cdd:PLN02234 520 IGVSLPPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVL 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2165115855 641 VTVEEGSIGGFGSHVVQFMALDGLLDGKLKwrpivLPDRYIDHGSPA 687
Cdd:PLN02234 600 ITVEEGSIGGFGSHVVQFLALDGLLDGKLK-----VYRTWITNGSTS 641
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
70-704 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 959.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 70 RPPTPILDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYP 149
Cdd:PRK05444 1 IPKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 150 HKILTGRREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKG-RNNNVIAVIGDGAMTAGQAYEA 228
Cdd:PRK05444 81 HKILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGgEDRKVVAVIGDGALTGGMAFEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 229 MNNAGYLDSDMIVILNDN-RQVSlptatldgpvPPVGALSSALSRLQSnrplrelrevakgvtkqiggpmhelaakvdey 307
Cdd:PRK05444 161 LNNAGDLKSDLIVILNDNeMSIS----------PNVGALSNYLARLRS-------------------------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 308 argmisgsgSTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKttGPVLIHVVTEKGRGYPYAERAADKYHGVAKFDPAT 387
Cdd:PRK05444 199 ---------STLFEELGFNYIGPIDGHDLDALIETLKNAKDLK--GPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPET 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 388 GKQFKGS-AKTQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKP 466
Cdd:PRK05444 268 GEQPKSSkPGKPSYTKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 467 FCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAI 546
Cdd:PRK05444 348 VVAIYSTFLQRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAY 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 547 DDRPSCFRYPRGNGIGVELPAGNkgiPLEVGKGRILVEGERVALLGYGSAVQNCLAAASVLESrglqVTVADARFCKPLD 626
Cdd:PRK05444 428 DDGPIAIRYPRGNGVGVELPELE---PLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLD 500
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2165115855 627 RALIRSLAKSHEVLVTVEEGSI-GGFGSHVVQFMALDGLLDgklKWRPIVLPDRYIDHGSPADQLAEAGLTPSHIAATV 704
Cdd:PRK05444 501 EELLLELAAKHDLVVTVEEGAImGGFGSAVLEFLADHGLDV---PVLNLGLPDEFIDHGSREELLAELGLDAEGIARRI 576
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
68-719 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 883.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 68 TQRPPTPILDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQS 147
Cdd:PRK12571 1 TPRPKTPLLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 148 YPHKILTGRREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYE 227
Cdd:PRK12571 81 YPHKILTGRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 228 AMNNAGYLDSDMIVILNDN-RQVSlptatldgpvPPVGALSSALSRLQSNRPLRELREVAKGVTKQIGGPMHELAAKVDE 306
Cdd:PRK12571 161 ALNNAGAADRRLIVILNDNeMSIA----------PPVGALAAYLSTLRSSDPFARLRAIAKGVEERLPGPLRDGARRARE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 307 YARGMISGSgsTLFEELGLYYIGPVDGHNIDDLISILKEVRStKTTGPVLIHVVTEKGRGYPYAERAADKYHGVAKFDPA 386
Cdd:PRK12571 231 LVTGMIGGG--TLFEELGFTYVGPIDGHDMEALLSVLRAARA-RADGPVLVHVVTEKGRGYAPAEADEDKYHAVGKFDVV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 387 TGKQFKGSAKTQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKP 466
Cdd:PRK12571 308 TGLQKKSAPSAPSYTSVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 467 FCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAI 546
Cdd:PRK12571 388 FCAVYSTFLQRGYDQLLHDVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 547 DDRPSCFRYPRGNGIGVELPAgnKGIPLEVGKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLD 626
Cdd:PRK12571 468 DDGPIAVRFPRGEGVGVEIPA--EGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 627 RALIRSLAKSHEVLVTVEEGSIGGFGSHVVQFMALDGLLDGKLKWRPIVLPDRYIDHGSPADQLAEAGLTPSHIAATVFN 706
Cdd:PRK12571 546 EALTDLLVRHHIVVIVEEQGAMGGFGAHVLHHLADTGLLDGGLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTG 625
|
650
....*....|...
gi 2165115855 707 ILGQTREALEVMT 719
Cdd:PRK12571 626 ALARLSGVPERET 638
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
48-719 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 743.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 48 QVKKRSRtVQASLSESGEYYTQRPPTPILDTINYPIHMKNLSLKELKQLADELRSDtIFNV--SKTGGHLGSSLGVVELT 125
Cdd:PLN02225 52 ECSNRAR-VCCSLPNTDEYCDEKFETPILDSIETPLQLKNLSVKELKLLADEIRTE-LHSVlwKKTQKSMNPSFAAIELT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 126 VALHYVFNAPQDRILWDVGHQSYPHKILTGRREKMSTlRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLK 205
Cdd:PLN02225 130 LALHYVFRAPVDNILWDAVEQTYAHKVLTRRWSAIPS-RQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 206 GRNNNVIAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNRQvSLPTATLDGPVPPVGALSSALSRLQSNRPLRELREV 285
Cdd:PLN02225 209 GKRDRVVAVIDNATITAGQAYEAMSNAGYLDSNMIVILNDSRH-SLHPNMEEGSKASISALSSIMSKIQSSKIFRKFREL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 286 AKGVTKQIGGPMHELAAKVDEYARGMISGSGSTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKTTGPVLIHVVTEKGR 365
Cdd:PLN02225 288 AKAMTKRIGKGMYEWAAKVDEYARGMVGPTGSTLFEELGLYYIGPVDGHNIEDLVCVLREVSSLDSMGPVLVHVITEENR 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 366 gypyaeraadkyhgvakfDPATGKQFKGSAKtQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDV 445
Cdd:PLN02225 368 ------------------DAETGKNIMVKDR-RTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 446 GIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNM 525
Cdd:PLN02225 429 GMAEQHAVTFSAGLSSGGLKPFCIIPSAFLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNM 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 526 VVMAPSDEAELFHIVATAAAIDDRPSCFRYPRGNGIGVE--LPAgnkGIPLEVGKGRILVEGERVALLGYGSAVQNCLAA 603
Cdd:PLN02225 509 IAMAPADEDELVNMVATAAYVTDRPVCFRFPRGSIVNMNylVPT---GLPIEIGRGRVLVEGQDVALLGYGAMVQNCLHA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 604 ASVLESRGLQVTVADARFCKPLDRALIRSLAKSHEVLVTVEEGSIGGFGSHVVQFMALDGLLDGKLKWRPIVLPDRYIDH 683
Cdd:PLN02225 586 HSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITVEEGCVGGFGSHVAQFIALDGQLDGNIKWRPIVLPDGYIEE 665
|
650 660 670
....*....|....*....|....*....|....*.
gi 2165115855 684 GSPADQLAEAGLTPSHIAATVFNILGQTREALEVMT 719
Cdd:PLN02225 666 ASPREQLALAGLTGHHIAATALSLLGRTREALLLMS 701
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
76-709 |
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: 735.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 76 LDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHKILTG 155
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 156 RREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGYL 235
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 236 DSDMIVILNDNrQVSLPtatldgpvPPVGALSSALSRLQSNRPLRELREVAKGVTKQIGGPMHELAAKVDEYARGMISGS 315
Cdd:TIGR00204 161 KTDMIVILNDN-EMSIS--------ENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYLAKRTEESMKGLVVPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 316 gsTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKttGPVLIHVVTEKGRGYPYAERAADKYHGVAKFDPATGKQFKGSA 395
Cdd:TIGR00204 232 --TFFEELGFNYIGPVDGHDLLELIETLKNAKKLK--GPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 396 KTQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFM 475
Cdd:TIGR00204 308 ALPSYSKIFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 476 QRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAIDDRPSCFRY 555
Cdd:TIGR00204 388 QRAYDQVVHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRY 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 556 PRGNGIGVELPAGNKGIPLevGKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDRALIRSLAK 635
Cdd:TIGR00204 468 PRGNAVGVELTPEPEKLPI--GKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAA 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2165115855 636 SHEVLVTVEEGSI-GGFGSHVVQFMALDGLLDGKLKwrpIVLPDRYIDHGSPADQLAEAGLTPSHIAATVFNILG 709
Cdd:TIGR00204 546 SHEKLVTVEENAImGGAGSAVLEFLMDQNKLVPVKR---LGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
76-361 |
4.26e-164 |
|
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: 473.05 E-value: 4.26e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 76 LDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHKILTG 155
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 156 RREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGYL 235
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 236 DSDMIVILNDN-RQVSlptatldgpvPPVGALSSALSRLQSNRPLRELREVAKGVTK-QIGGPMHELAAKVDEYARGMIs 313
Cdd:pfam13292 161 KKDLIVILNDNeMSIS----------PNVGALSNYLSRLRTSPTYNRLKEEVKKLLKpKIGPPLYELARRAKESLKGLV- 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2165115855 314 gSGSTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKttGPVLIHVVT 361
Cdd:pfam13292 230 -VPGTLFEELGFKYIGPIDGHDLDALVKVLENAKDLK--GPVLLHVVT 274
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
74-709 |
7.74e-156 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 463.71 E-value: 7.74e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 74 PILDTINYPIHMKNLSLKELKQLADELRSDTIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHKIL 153
Cdd:PRK12315 1 MYLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 154 TGRREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAG 233
Cdd:PRK12315 81 TGRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 234 YLDSDMIVILNDNrQVSLPTAtldgpvppVGALSSALsrlqsnrplRELREvAKGVTKqiggpmhelaakvdeyargmis 313
Cdd:PRK12315 161 ELKSNLIIIVNDN-QMSIAEN--------HGGLYKNL---------KELRD-TNGQSE---------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 314 gsgSTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKTtgPVLIHVVTEKGRGYPYAERAADKYHGVAKFDPATGKQfKG 393
Cdd:PRK12315 200 ---NNLFKAMGLDYRYVEDGNDIESLIEAFKEVKDIDH--PIVLHIHTLKGKGYQPAEENKEAFHWHMPFDLETGQS-KV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 394 SAKTQSYTTYFAEALIAEAEADKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSS 473
Cdd:PRK12315 274 PASGESYSSVTLDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNST 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 474 FMQRAYDQVVHDVDLQKLPVRFaMDRAGLVGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAIDDRPSCF 553
Cdd:PRK12315 354 FLQRAYDQLSHDLAINNNPAVM-IVFGGSISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 554 RYPRGNGIGVELPAGNKGIPlevgKGRILVEGERVALLGYGSAVQNCLAAASVL-ESRGLQVTVADARFCKPLDRALIRS 632
Cdd:PRK12315 433 RVPEHGVESGPTVDTDYSTL----KYEVTKAGEKVAILALGDFYELGEKVAKKLkEELGIDATLINPKFITGLDEELLEK 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 633 LAKSHEVLVTVEEGSI-GGFGSHVVQFMaldGLLDGKlkwrpiVL----PDRYIDHGSPADQLAEAGLTPSHIAATVFNI 707
Cdd:PRK12315 509 LKEDHELVVTLEDGILdGGFGEKIARYY---GNSDMK------VLnygaKKEFNDRVPVEELYKRNHLTPEQIVEDILSV 579
|
..
gi 2165115855 708 LG 709
Cdd:PRK12315 580 LK 581
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
112-367 |
7.67e-123 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 364.56 E-value: 7.67e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 112 GGHLGSSLGVVELTVALHYVFNAPQDRILWDVGHQSYPHKILTGRREKMSTLRQTNGLAGFTKRSESEYDCFGTGHSSTT 191
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 192 ISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNRQVSLPTAtldgpvppvgalssals 271
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNV----------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 272 rlqsnrplrelrevakgvtkqiggpmhelaakvdeyargmisGSGSTLFEELGLYYIGPVDGHNIDDLISILKEVRSTKt 351
Cdd:cd02007 144 ------------------------------------------GTPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLK- 180
|
250
....*....|....*.
gi 2165115855 352 tGPVLIHVVTEKGRGY 367
Cdd:cd02007 181 -GPVLLHVVTKKGKGY 195
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
415-704 |
9.92e-69 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 227.66 E-value: 9.92e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 415 DKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSF-MQRAYDQVVHDVDLQKLPV 493
Cdd:COG3958 21 DPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFlTGRAYEQIRNDIAYPNLNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 494 RFAMDRAGL-VGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAIDDrPSCFRYPRGNgigveLPAG-NKG 571
Cdd:COG3958 101 KIVGSHAGLsYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDG-PVYLRLGRGA-----VPVVyDED 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 572 IPLEVGKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDRALIRSLAKSHEVLVTVEEGSI-GG 650
Cdd:COG3958 175 YEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGAVVTAEEHSIiGG 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2165115855 651 FGSHVVQFMAldGLLDGKLkwRPIVLPDRYIDHGSPADQLAEAGLTPSHIAATV 704
Cdd:COG3958 255 LGSAVAEVLA--ENYPVPL--RRIGVPDRFGESGSPEELLEKYGLDAEGIVAAA 304
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
415-557 |
1.05e-65 |
|
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: 214.23 E-value: 1.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 415 DKDIVAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVR 494
Cdd:cd07033 14 DPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQIRHDVALQNLPVK 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2165115855 495 FAMDRAGL-VGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAIDDrPSCFRYPR 557
Cdd:cd07033 94 FVGTHAGIsVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDG-PVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
415-559 |
2.57e-48 |
|
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: 167.73 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 415 DKDIVAIHAAMGGGTGMNLFLRRFPT---RCFDVGIAEQHAVTFAAGLACEG--LKPFCAIYSSFMQRAYDQVVHDVDLQ 489
Cdd:pfam02779 20 DPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEATFSDFLNRADDAIRHGAALG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2165115855 490 KLPVRFAMDRAGL-VGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAIDDR-PSCFRYPRGN 559
Cdd:pfam02779 100 KLPVPFVVTRDPIgVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGRkPVVLRLPRQL 171
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
443-562 |
2.47e-46 |
|
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: 161.11 E-value: 2.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 443 FDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACL 522
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2165115855 523 PNMVVMAPSDEAELFHIVATAAAiDDRPSCFRYPRGNGIG 562
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSLYR 136
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
577-700 |
9.04e-38 |
|
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: 136.57 E-value: 9.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 577 GKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDRALIRSLAKSHEVLVTVEEGS-IGGFGSHV 655
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVpRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2165115855 656 VQFMALDGLLDGKLKWRPIVLPDrYIDHGSPADQLAEAGLTPSHI 700
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPD-FPEPGSADELEKLYGLTPEKI 124
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
89-704 |
4.95e-35 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 140.65 E-value: 4.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 89 SLKELKQLADELRSDTIFNVSKTG-GHLGSSLGVVELTVAL-----HYVFNAPQ----DRILWDVGHQS---YPHKILTG 155
Cdd:PRK05899 4 DMELLQLLANAIRVLSIDAVQKANsGHPGMPMGAADIAYVLwtrflRHDPKNPKwpnrDRFVLSAGHGSmllYSLLHLAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 156 ---RREKMSTLRQTNglagftkrseS------EYdcfgtGHSS----TT------ISAGLGMAV-GRDLKGRNNNVIAVI 215
Cdd:PRK05899 84 ydlSIDDLKNFRQLG----------SktpghpEY-----GHTPgvetTTgplgqgLANAVGMALaEKYLAALFNRPGLDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 216 ---------GDGAMTAGQAYEAMNNAGYLD-SDMIVILNDNRqvslptATLDGPVppvgalssalsrlqsnrplrelrev 285
Cdd:PRK05899 149 vdhytyvlcGDGDLMEGISHEACSLAGHLKlGNLIVIYDDNR------ISIDGPT------------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 286 akgvtkqiggpmhELAAKVDEYARgmisgsgstlFEELGLYYIgPVDGHNIDDLISILKEVRstKTTGPVLIHVVTEKGR 365
Cdd:PRK05899 198 -------------EGWFTEDVKKR----------FEAYGWHVI-EVDGHDVEAIDAAIEEAK--ASTKPTLIIAKTIIGK 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 366 GYPYAERAAdKYHG-------VAK------FDP--ATGKQFKGSAKTQSyttyfaealiaeaeadkDIVAIHAAMGGGTG 430
Cdd:PRK05899 252 GAPNKEGTH-KVHGaplgaeeIAAakkelgWDYrkASGKALNALAKALP-----------------ELVGGSADLAGSNN 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 431 MNLF------LRRFPTRCFDVGIAEQHAVTFAAGLACEG-LKPFCAIYSSFMQRAYDQVvHDVDLQKLPVRFAMDRAGL- 502
Cdd:PRK05899 314 TKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGgFIPFGGTFLVFSDYARNAI-RLAALMKLPVIYVFTHDSIg 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 503 VGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAIDDRPSCFRYPRGNgigveLP--AGNKGIPLEVGKGR 580
Cdd:PRK05899 393 VGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQN-----LPvlERTAQEEGVAKGGY 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 581 ILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDR---ALIRS-LAKSHEVLVTVEEGSIGGFGSHVv 656
Cdd:PRK05899 468 VLRDDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEqdaAYKESvLPAAVTARVAVEAGVADGWYKYV- 546
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2165115855 657 qfmaldgLLDGKlkwrpIVLPDRYIDHGSPADQLAEAGLTPSHIAATV 704
Cdd:PRK05899 547 -------GLDGK-----VLGIDTFGASAPADELFKEFGFTVENIVAAA 582
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
432-653 |
1.28e-22 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 100.06 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 432 NLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAI-YSSFMQRAYDQVVHDV--------DLQKLPVRFamdRA-- 500
Cdd:PTZ00182 74 GLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFmFADFIFPAFDQIVNEAakyrymsgGQFDCPIVI---RGpn 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 501 GLVGADGPTHCGAFDVTFMAClPNMVVMAPSDEAElfhivatA-----AAI-DDRPSCFRYPRG-NGIGVEL-PAGNKGI 572
Cdd:PTZ00182 151 GAVGHGGAYHSQSFEAYFAHV-PGLKVVAPSDPED-------AkgllkAAIrDPNPVVFFEPKLlYRESVEVvPEADYTL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 573 PLevGKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDR-ALIRSLAKSHEVLVTVEEGSIGGF 651
Cdd:PTZ00182 223 PL--GKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDReTIVKSVKKTGRCVIVHEAPPTCGI 300
|
..
gi 2165115855 652 GS 653
Cdd:PTZ00182 301 GA 302
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
419-557 |
8.98e-19 |
|
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: 83.55 E-value: 8.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 419 VAIHAAMGGGTGMNLFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSS-FMQRAYDQVVhDVDLQKLPVRFAM 497
Cdd:cd06586 14 HVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGtGLLNAINGLA-DAAAEHLPVVFLI 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2165115855 498 DRAGLVGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHI--VATAAAIDDRPSCFRYPR 557
Cdd:cd06586 93 GARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIdhAIRTAYASQGPVVVRLPR 154
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
86-381 |
8.21e-18 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 84.36 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 86 KNLSLKELKQLADELRSDTIFNVSKTG-GHLGSSLGVVELTVALHY-VFN----APQ----DRILWDVGHQS---YPHKI 152
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGsGHPGGSLSAADILAALYFkVMNidpkNPDwpdrDRFILSKGHAApalYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 153 LTGR--REKMSTLRQTNGLAGftkrseseydcfgtGHSSTT---------------ISAGLGMAVGRDLKGRNNNVIAVI 215
Cdd:COG3959 81 EKGYfpKEELATFRKLGSRLQ--------------GHPDMKktpgvemstgslgqgLSVAVGMALAAKLDGKDYRVYVLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 216 GDGAMTAGQAYEAMNNAGY--LDSdMIVILNDNRQvslptatldgpvppvgalssalsrlqsnrplrelrevakgvtkQI 293
Cdd:COG3959 147 GDGELQEGQVWEAAMAAAHykLDN-LIAIVDRNGL-------------------------------------------QI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 294 GGPMHE------LAAKvdeyargmisgsgstlFEELGLYYIgPVDGHNIDDLISILKEVRSTKtTGPVLIHVVTEKGRGY 367
Cdd:COG3959 183 DGPTEDvmslepLAEK----------------WEAFGWHVI-EVDGHDIEALLAALDEAKAVK-GKPTVIIAHTVKGKGV 244
|
330
....*....|....
gi 2165115855 368 PYAERAAdKYHGVA 381
Cdd:COG3959 245 SFMENRP-KWHGKA 257
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
98-379 |
5.80e-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: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 98 DELRSDTIFNVSKTG-GHLGSSLGVVELTVAL-----HYVFNAPQ----DRILWDVGHQS---YPHKILTG--RREKMST 162
Cdd:cd02012 1 NRIRRLSIDMVQKAGsGHPGGSLSAADILAVLyfkvlKYDPADPKwpnrDRFVLSKGHASpalYAVLALAGylPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 163 LRQTNG-LAGFTKRSESEYDCFGTG---HSsttISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGY--LD 236
Cdd:cd02012 81 FRQLGSrLPGHPEYGLTPGVEVTTGslgQG---LSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHykLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 237 sDMIVILNDNRQvslptaTLDGPVPpvgalssalsrlqsnrplrelrEVAkgvtkqiggPMHELAAKvdeyargmisgsg 316
Cdd:cd02012 158 -NLIAIVDSNRI------QIDGPTD----------------------DIL---------FTEDLAKK------------- 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2165115855 317 stlFEELGLYYIgPVDGHNIDDLISILKEVRSTKtTGPVLIHVVTEKGRGYPYAErAADKYHG 379
Cdd:cd02012 187 ---FEAFGWNVI-EVDGHDVEEILAALEEAKKSK-GKPTLIIAKTIKGKGVPFME-NTAKWHG 243
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
435-664 |
5.94e-16 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 79.77 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 435 LRRF-PTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYS-SFMQRAYDQVVHDVDLQ--------KLPVRF--AMDRAGL 502
Cdd:PRK09212 45 LEQFgPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFMTfNFSMQAIDQIVNSAAKTnymsggqlKCPIVFrgPNGAAAR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 503 VGADgptHCGAFDVTFmACLPNMVVMAPSDEAELFHIVATAAAiDDRPSCF-RYPRGNGIGVELPAGNKGIPLevGKGRI 581
Cdd:PRK09212 125 VAAQ---HSQCYAAWY-SHIPGLKVVAPYFAADCKGLLKTAIR-DPNPVIFlENEILYGHSHEVPEEEESIPI--GKAAI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 582 LVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDR-ALIRSLAKSHEvLVTVEEG-SIGGFGS---HVV 656
Cdd:PRK09212 198 LREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTeTIIESVKKTNR-LVVVEEGwPFAGVGAeiaALI 276
|
....*...
gi 2165115855 657 QFMALDGL 664
Cdd:PRK09212 277 MKEAFDYL 284
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
433-646 |
5.53e-12 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 67.92 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 433 LFLRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYS-SFMQRAYDQVVHDVDLQ--------KLPVRFAMDRAGLV 503
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTfNFSMQAIDHIINSAAKTnymsagqiSVPIVFRGPNGAAA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 504 GAdGPTHCGAFDVTFMAClPNMVVMAPSDeAELFHIVATAAAIDDRPSCF---RYPRGNGIGVELPAGNKGIPLEVGKGR 580
Cdd:PLN02683 147 GV-GAQHSQCFAAWYSSV-PGLKVLAPYS-SEDARGLLKAAIRDPDPVVFlenELLYGESFPVSAEVLDSSFVLPIGKAK 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2165115855 581 ILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDRALIRSLAKSHEVLVTVEEG 646
Cdd:PLN02683 224 IEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEG 289
|
|
| PLN02790 |
PLN02790 |
transketolase |
446-616 |
6.15e-09 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 59.26 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 446 GIAEQHAVTFAAGLA--CEGLKPFCA---IYSSFMQRAydqvVHDVDLQKLPVRFAM--DRAGLvGADGPTHCGAFDVTF 518
Cdd:PLN02790 398 GVREHGMGAICNGIAlhSSGLIPYCAtffVFTDYMRAA----MRLSALSEAGVIYVMthDSIGL-GEDGPTHQPIEHLAS 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 519 MACLPNMVVMAPSDEAElfhivaTAAAID------DRPSCFRYPRGNGIGVELPAGNKgipleVGKGRILVEGER----- 587
Cdd:PLN02790 473 LRAMPNILMLRPADGNE------TAGAYKvavtnrKRPTVLALSRQKVPNLPGTSIEG-----VEKGGYVISDNSsgnkp 541
|
170 180 190
....*....|....*....|....*....|
gi 2165115855 588 -VALLGYGSAVQNCLAAASVLESRGLQVTV 616
Cdd:PLN02790 542 dLILIGTGSELEIAAKAAKELRKEGKKVRV 571
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
574-656 |
5.96e-08 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 55.69 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 574 LEVGKGRILVEGERVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDRA-LIRSLAKSHEvLVTVEEG-SIGGF 651
Cdd:PRK11892 329 LPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTEtIVESVKKTNR-LVTVEEGwPQSGV 407
|
....*
gi 2165115855 652 GSHVV 656
Cdd:PRK11892 408 GAEIA 412
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
439-553 |
7.50e-08 |
|
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: 52.48 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 439 PTRCFDVGIAEQHAVTFAAGLACEGLKPFCAI-YSSFMQRAYDQVVHDV--------DLQKLP--VRFAMdraGLVGADG 507
Cdd:cd07036 43 PDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFALPAFDQIVNEAaklrymsgGQFKVPivIRGPN---GGGIGGG 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2165115855 508 PTHCGAFDVTFMAClPNMVVMAPSDEAELFHIVaTAAAIDDRPSCF 553
Cdd:cd07036 120 AQHSQSLEAWFAHI-PGLKVVAPSTPYDAKGLL-KAAIRDDDPVIF 163
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
113-616 |
1.15e-07 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 55.07 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 113 GHLGSSLGVVELTVAL-HYVFN--------APQDRILWDVGHQS---YPHKILTGRREKMSTL---RQTNGL------AG 171
Cdd:PTZ00089 27 GHPGAPMGMAPIAHILwSEVMKynpkdprwINRDRFVLSNGHASallYSMLHLTGYDLSMEDLknfRQLGSRtpghpeRH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 172 FTKRSESEYDCFGTGhssttISAGLGMAVG-RDLKGR---------NNNVIAVIGDGAMTAGQAYEAMNNAGYLDSDMIV 241
Cdd:PTZ00089 107 ITPGVEVTTGPLGQG-----IANAVGLAIAeKHLAAKfnrpghpifDNYVYVICGDGCLQEGVSQEALSLAGHLGLEKLI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 242 ILNDNRQVslptaTLDGPVppvgALS---SALSRLQS-----------NRPLRELREV---AKGVTKQ---------IG- 294
Cdd:PTZ00089 182 VLYDDNKI-----TIDGNT----DLSfteDVEKKYEAygwhvievdngNTDFDGLRKAieeAKKSKGKpkliivkttIGy 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 295 GPMHELAAKVdeyargmisgSGSTLFEElglyyigpvdghniddlisilkEVRSTKTT---GPVLIHVVTEKGRGYpYAE 371
Cdd:PTZ00089 253 GSSKAGTEKV----------HGAPLGDE----------------------DIAQVKELfglDPEKKFHVSEEVRQF-FEQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 372 RAADKYHGVAKFD----------PATG----KQFKGS------AKTQSYTTYFAEALIAEAEAD--KDIVAIHAAMGGG- 428
Cdd:PTZ00089 300 HVEKKKENYEAWKkrfakytaafPKEAqaieRRFKGElppgweKKLPKYTTNDKAIATRKASENvlNPLFQILPELIGGs 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 429 ---TGMNL--------FLRRFPT-RCFDVGIAEQHAVTFAAGLACEG-LKPFCAIYSSFMQRAYDqVVHDVDLQKLPVRF 495
Cdd:PTZ00089 380 adlTPSNLtrpkeandFTKASPEgRYIRFGVREHAMCAIMNGIAAHGgFIPFGATFLNFYGYALG-AVRLAALSHHPVIY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 496 AM--DRAGLvGADGPTHCGAFDVTFMACLPNMVVMAPSDEAELFHIVATAAAIDDRPSCFRYPRGNgigveLPAGNKGIP 573
Cdd:PTZ00089 459 VAthDSIGL-GEDGPTHQPVETLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQN-----TPPLPGSSI 532
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2165115855 574 LEVGKGR-ILVEGE---RVALLGYGSAVQNCLAAASVLESrGLQVTV 616
Cdd:PTZ00089 533 EGVLKGAyIVVDFTnspQLILVASGSEVSLCVEAAKALSK-ELNVRV 578
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
184-247 |
4.71e-05 |
|
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: 45.95 E-value: 4.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2165115855 184 GTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNR 247
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCENNG 165
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
153-246 |
1.47e-04 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 44.70 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 153 LTGRREKMStlRQTNGLAGFTKRSESEYDcfGTGHSSTTISAGLGMAVGRDLKGRNNNVIAVIGDGAMTAGQAYEAMNNA 232
Cdd:PLN02269 109 LMGRKDGCS--RGKGGSMHFYKKDANFYG--GHGIVGAQVPLGAGLAFAQKYNKEENVAFALYGDGAANQGQLFEALNIA 184
|
90
....*....|....
gi 2165115855 233 GYLDSDMIVILNDN 246
Cdd:PLN02269 185 ALWDLPVIFVCENN 198
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
192-247 |
3.10e-04 |
|
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: 43.59 E-value: 3.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2165115855 192 ISAGLGMAVgrDLKGRNNNVIAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNR 247
Cdd:COG1071 135 HAVGAALAA--KLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNG 188
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
110-261 |
6.53e-04 |
|
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.
Pssm-ID: 238975 [Multi-domain] Cd Length: 386 Bit Score: 42.68 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 110 KTGGHLGSSLGVVEL-TVALHYVFNAPQDRILWDV----GHQS---YPHKILTGR--REKMSTLRQTNGLAGFtkrseSE 179
Cdd:cd02017 28 GIGGHIATFASAATLyEVGFNHFFRARGEGGGGDLvyfqGHASpgiYARAFLEGRltEEQLDNFRQEVGGGGL-----SS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 180 YdcfgtgHSST---------TISAGLG--MAV----------GRDLK-GRNNNVIAVIGDGAMTAGQAYEAMNNAGY--L 235
Cdd:cd02017 103 Y------PHPWlmpdfwefpTVSMGLGpiQAIyqarfnryleDRGLKdTSDQKVWAFLGDGEMDEPESLGAIGLAARekL 176
|
170 180
....*....|....*....|....*.
gi 2165115855 236 DsDMIVILNDNRQvslptaTLDGPVP 261
Cdd:cd02017 177 D-NLIFVVNCNLQ------RLDGPVR 195
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
441-666 |
1.69e-03 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 41.26 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 441 RCFDVGIAEQHAVTFAAGLACEGLKPFC-AIYSSFMQRAYDQVVHDVDLQ--------KLPVrfAMDRAGLVGAD-GPTH 510
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAMTGLRPIVeGMNMGFLLLAFNQISNNAGMLhytsggnfTIPI--VIRGPGGVGRQlGAEH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 511 CGAFDVTFMAcLPNMVVMA---PSDEAELFhivaTAAAIDDRPSCF-RYPRGNGIGVELPAGNKGIPLEvgKGRILVEGE 586
Cdd:CHL00144 130 SQRLESYFQS-VPGLQIVAcstPYNAKGLL----KSAIRSNNPVIFfEHVLLYNLKEEIPDNEYLLPLE--KAEVVRPGN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 587 RVALLGYGSAVQNCLAAASVLESRGLQVTVADARFCKPLDRALI-RSLAKSHEVLVTVEEGSIGGFGShVVQFMALDGLL 665
Cdd:CHL00144 203 DITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTIsKSVKKTHKVLIVEECMKTGGIGA-ELIAQINEHLF 281
|
.
gi 2165115855 666 D 666
Cdd:CHL00144 282 D 282
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
172-361 |
3.26e-03 |
|
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: 39.16 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 172 FTKRSESEYDCFGTGHSSTTISAGLGMAVGRdlkgRNNNVIAVIGDGAMtaGQAYEAMNNAGYLDSDMIVILNDNRQvsl 251
Cdd:cd00568 32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAA----PDRPVVCIAGDGGF--MMTGQELATAVRYGLPVIVVVFNNGG--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165115855 252 ptatldgpvppvgalssalsrLQSNRPLRELREVAKGVTKQIGGPmhELAAkvdeYARGMisgsgstlfeelGLYYIGPV 331
Cdd:cd00568 103 ---------------------YGTIRMHQEAFYGGRVSGTDLSNP--DFAA----LAEAY------------GAKGVRVE 143
|
170 180 190
....*....|....*....|....*....|
gi 2165115855 332 DghnIDDLISILKEVRSTKttGPVLIHVVT 361
Cdd:cd00568 144 D---PEDLEAALAEALAAG--GPALIEVKT 168
|
|
| |
