|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
6-629 |
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: 1090.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 6 KTPLLDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPHK 85
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 86 ILTGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNN 165
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 166 AGALDARLIVILNDNDMSIAPPTGAMSAYLARLASGRTYMGFRDLGKKLTAYL---GKNIDRAITRAVEHARGYVTGGTM 242
Cdd:COG1154 161 AGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLpgiGPPLYELARRAKEGLKGLVVPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 243 FEEMGFYHIGPIDGHSFDHLLPVLRNVRDNGrGPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVITGAQARVKPNAPSY 322
Cdd:COG1154 241 FEELGFKYIGPIDGHDLDALVETLRNAKDLK-GPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 323 TSVFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYD 402
Cdd:COG1154 320 TDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 403 QVVHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDgGPISFRYPRGEG 482
Cdd:COG1154 400 QVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYD-GPTAIRYPRGNG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 483 VGVDMPARGEILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVIT 562
Cdd:COG1154 479 PGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVT 558
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517308034 563 VEEGSI-GGFGSHVMHFLATEGLLdngLKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKALG 629
Cdd:COG1154 559 VEEGVLaGGFGSAVLEFLADAGLD---VPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-628 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 1008.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 5 PKTPLLDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPH 84
Cdd:PRK05444 2 PKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 85 KILTGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADL-DKSDRRVIAVIGDGAMSAGMAYEAL 163
Cdd:PRK05444 82 KILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLkGGEDRKVVAVIGDGALTGGMAFEAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 164 NNAGALDARLIVILNDNDMSIAPPTGAMSAYLARLASGrtymgfrdlgkkltaylgknidraitravehargyvtggTMF 243
Cdd:PRK05444 162 NNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRSS---------------------------------------TLF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 244 EEMGFYHIGPIDGHSFDHLLPVLRNVRDNGrGPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVITGAQARV-KPNAPSY 322
Cdd:PRK05444 203 EELGFNYIGPIDGHDLDALIETLKNAKDLK-GPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKSsKPGKPSY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 323 TSVFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYD 402
Cdd:PRK05444 282 TKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 403 QVVHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISFRYPRGEG 482
Cdd:PRK05444 362 QVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 483 VGVDMPArGEILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAglstTVADARFAKPLDHDLIRQLARHHEMVIT 562
Cdd:PRK05444 442 VGVELPE-LEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLASA----TVVDARFVKPLDEELLLELAAKHDLVVT 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517308034 563 VEEGSI-GGFGSHVMHFLATEGLLDnglKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKAL 628
Cdd:PRK05444 517 VEEGAImGGFGSAVLEFLADHGLDV---PVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
16-629 |
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: 758.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 16 PADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPHKILTGRRDRIR 95
Cdd:TIGR00204 7 PQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTGRREKFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 96 TLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGALDARLIV 175
Cdd:TIGR00204 87 TLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDLKTDMIV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 176 ILNDNDMSIAPPTGAMSAYLARLASGRTYMGFRDLGKKLTAYLGKNIDRAITRAVEHARGYVTGGTMFEEMGFYHIGPID 255
Cdd:TIGR00204 167 ILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYLAKRTEESMKGLVVPGTFFEELGFNYIGPVD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 256 GHSFDHLLPVLRNVRDNgRGPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVITGAQARVKPNAPSYTSVFAEALVQEAA 335
Cdd:TIGR00204 247 GHDLLELIETLKNAKKL-KGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSALPSYSKIFSDTLCELAK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 336 LDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYDQVVHDVAIQGLPV 415
Cdd:TIGR00204 326 KDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVCIQKLPV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 416 RFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISFRYPRGEGVGVDMPARGEILQ 495
Cdd:TIGR00204 406 LFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVGVELTPEPEKLP 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 496 IGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVITVEEGSI-GGFGSH 574
Cdd:TIGR00204 486 IGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVEENAImGGAGSA 565
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 517308034 575 VMHFLATEGLLdngLKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKALG 629
Cdd:TIGR00204 566 VLEFLMDQNKL---VPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
10-283 |
3.15e-176 |
|
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: 501.17 E-value: 3.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 10 LDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPHKILTG 89
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 90 RRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGAL 169
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 170 DARLIVILNDNDMSIAPPTGAMSAYLARLASGRTYMGFRDLGKK-LTAYLGKNIDRAITRAVEHARGYVTGGTMFEEMGF 248
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKlLKPKIGPPLYELARRAKESLKGLVVPGTLFEELGF 240
|
250 260 270
....*....|....*....|....*....|....*
gi 517308034 249 YHIGPIDGHSFDHLLPVLRNVRDNGrGPVLIHVVT 283
Cdd:pfam13292 241 KYIGPIDGHDLDALVKVLENAKDLK-GPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
46-289 |
5.37e-114 |
|
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: 339.14 E-value: 5.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 46 GGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPHKILTGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTS 125
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 126 ISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGALDARLIVILNDNDMSIAPPTGamsaylarlasgrtym 205
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 206 gfrdlgkkltaylgknidraitravehargyvTGGTMFEEMGFYHIGPIDGHSFDHLLPVLRNVRDnGRGPVLIHVVTQK 285
Cdd:cd02007 145 --------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKD-LKGPVLLHVVTKK 191
|
....
gi 517308034 286 GKGY 289
Cdd:cd02007 192 GKGY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
365-484 |
1.59e-39 |
|
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: 141.47 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 365 FDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYDQVVHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTL 444
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 517308034 445 PGFVVMAAADEAELKHMVRTAVAYDgGPISFRYPRGEGVG 484
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIRDD-GPVVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
6-629 |
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: 1090.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 6 KTPLLDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPHK 85
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 86 ILTGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNN 165
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 166 AGALDARLIVILNDNDMSIAPPTGAMSAYLARLASGRTYMGFRDLGKKLTAYL---GKNIDRAITRAVEHARGYVTGGTM 242
Cdd:COG1154 161 AGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLpgiGPPLYELARRAKEGLKGLVVPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 243 FEEMGFYHIGPIDGHSFDHLLPVLRNVRDNGrGPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVITGAQARVKPNAPSY 322
Cdd:COG1154 241 FEELGFKYIGPIDGHDLDALVETLRNAKDLK-GPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 323 TSVFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYD 402
Cdd:COG1154 320 TDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 403 QVVHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDgGPISFRYPRGEG 482
Cdd:COG1154 400 QVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYD-GPTAIRYPRGNG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 483 VGVDMPARGEILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVIT 562
Cdd:COG1154 479 PGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVT 558
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517308034 563 VEEGSI-GGFGSHVMHFLATEGLLdngLKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKALG 629
Cdd:COG1154 559 VEEGVLaGGFGSAVLEFLADAGLD---VPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-628 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 1008.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 5 PKTPLLDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPH 84
Cdd:PRK05444 2 PKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 85 KILTGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADL-DKSDRRVIAVIGDGAMSAGMAYEAL 163
Cdd:PRK05444 82 KILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLkGGEDRKVVAVIGDGALTGGMAFEAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 164 NNAGALDARLIVILNDNDMSIAPPTGAMSAYLARLASGrtymgfrdlgkkltaylgknidraitravehargyvtggTMF 243
Cdd:PRK05444 162 NNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRSS---------------------------------------TLF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 244 EEMGFYHIGPIDGHSFDHLLPVLRNVRDNGrGPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVITGAQARV-KPNAPSY 322
Cdd:PRK05444 203 EELGFNYIGPIDGHDLDALIETLKNAKDLK-GPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKSsKPGKPSY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 323 TSVFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYD 402
Cdd:PRK05444 282 TKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 403 QVVHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISFRYPRGEG 482
Cdd:PRK05444 362 QVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 483 VGVDMPArGEILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAglstTVADARFAKPLDHDLIRQLARHHEMVIT 562
Cdd:PRK05444 442 VGVELPE-LEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLASA----TVVDARFVKPLDEELLLELAAKHDLVVT 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517308034 563 VEEGSI-GGFGSHVMHFLATEGLLDnglKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKAL 628
Cdd:PRK05444 517 VEEGAImGGFGSAVLEFLADHGLDV---PVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-634 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 971.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 5 PKTPLLDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPH 84
Cdd:PRK12571 4 PKTPLLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCYPH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 85 KILTGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALN 164
Cdd:PRK12571 84 KILTGRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYEALN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 165 NAGALDARLIVILNDNDMSIAPPTGAMSAYLARLASGRTYMGFRDLGKKLTAYLGKNIDRAITRAVEHARGYVTGGTMFE 244
Cdd:PRK12571 164 NAGAADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIAKGVEERLPGPLRDGARRARELVTGMIGGGTLFE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 245 EMGFYHIGPIDGHSFDHLLPVLRNVRDNGRGPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVITGAQARVKPNAPSYTS 324
Cdd:PRK12571 244 ELGFTYVGPIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEADEDKYHAVGKFDVVTGLQKKSAPSAPSYTS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 325 VFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYDQV 404
Cdd:PRK12571 324 VFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQRGYDQL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 405 VHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISFRYPRGEGVG 484
Cdd:PRK12571 404 LHDVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 485 VDMPARGEILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVITVE 564
Cdd:PRK12571 484 VEIPAEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHIVVIVEE 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 565 EGSIGGFGSHVMHFLATEGLLDNGLKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKALGRGVAV 634
Cdd:PRK12571 564 QGAMGGFGAHVLHHLADTGLLDGGLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALARLSGV 633
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
2-630 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 819.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 2 TQLPKTPLLDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQC 81
Cdd:PLN02582 26 SQRPPTPLLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 82 YPHKILTGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYE 161
Cdd:PLN02582 106 YPHKILTGRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 162 ALNNAGALDARLIVILNDN-DMSI--------APPTGAMSAYLARLASGRTYMGFRDLGKKLTAYLGKNIDRAITRAVEH 232
Cdd:PLN02582 186 AMNNAGYLDSDMIVILNDNkQVSLptatldgpAPPVGALSSALSRLQSSRPLRELREVAKGVTKQIGGPMHELAAKVDEY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 233 ARGYV--TGGTMFEEMGFYHIGPIDGHSFDHLLPVLRNVRDNGR-GPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVIT 309
Cdd:PLN02582 266 ARGMIsgSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKTtGPVLIHVVTEKGRGYPYAERAADKYHGVVKFDPAT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 310 GAQARVKPNAPSYTSVFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPF 389
Cdd:PLN02582 346 GKQFKVKAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPF 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 390 AALYSTFLQRAYDQVVHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYD 469
Cdd:PLN02582 426 CAIYSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAID 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 470 GGPISFRYPRGEGVGVDMPA--RGEILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDH 547
Cdd:PLN02582 506 DRPSCFRYPRGNGIGVQLPPnnKGIPIEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDR 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 548 DLIRQLARHHEMVITVEEGSIGGFGSHVMHFLATEGLLDNGLKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKA 627
Cdd:PLN02582 586 ALIRSLAKSHEVLITVEEGSIGGFGSHVAQFMALDGLLDGKLKWRPLVLPDRYIDHGAPADQLAEAGLTPSHIAATVLNV 665
|
...
gi 517308034 628 LGR 630
Cdd:PLN02582 666 LGQ 668
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
16-629 |
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: 758.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 16 PADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPHKILTGRRDRIR 95
Cdd:TIGR00204 7 PQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTGRREKFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 96 TLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGALDARLIV 175
Cdd:TIGR00204 87 TLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDLKTDMIV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 176 ILNDNDMSIAPPTGAMSAYLARLASGRTYMGFRDLGKKLTAYLGKNIDRAITRAVEHARGYVTGGTMFEEMGFYHIGPID 255
Cdd:TIGR00204 167 ILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYLAKRTEESMKGLVVPGTFFEELGFNYIGPVD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 256 GHSFDHLLPVLRNVRDNgRGPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVITGAQARVKPNAPSYTSVFAEALVQEAA 335
Cdd:TIGR00204 247 GHDLLELIETLKNAKKL-KGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSALPSYSKIFSDTLCELAK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 336 LDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYDQVVHDVAIQGLPV 415
Cdd:TIGR00204 326 KDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVCIQKLPV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 416 RFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISFRYPRGEGVGVDMPARGEILQ 495
Cdd:TIGR00204 406 LFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVGVELTPEPEKLP 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 496 IGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVITVEEGSI-GGFGSH 574
Cdd:TIGR00204 486 IGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVEENAImGGAGSA 565
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 517308034 575 VMHFLATEGLLdngLKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKALG 629
Cdd:TIGR00204 566 VLEFLMDQNKL---VPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
5-606 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 646.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 5 PKTPLLDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPH 84
Cdd:PLN02234 62 PPTPLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPH 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 85 KILTGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALN 164
Cdd:PLN02234 142 KILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 165 NAGALDARLIVILNDNDM---------SIAPPTGAMSAYLARLASGRTYMgfrdlgkkltaylgknidraitravehaRG 235
Cdd:PLN02234 222 NAGYLHSNMIVILNDNKQvslptanldGPTQPVGALSCALSRLQSNCGMI----------------------------RE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 236 yvTGGTMFEEMGFYHIGPIDGHSFDHLLPVLRNVRDNGR-GPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVITGAQAR 314
Cdd:PLN02234 274 --TSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQFK 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 315 VKPNAPSYTSVFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYS 394
Cdd:PLN02234 352 NISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 395 TFLQRAYDQVVHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPIS 474
Cdd:PLN02234 432 SFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSC 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 475 FRYPRGEGVGVDMPA--RGEILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQ 552
Cdd:PLN02234 512 FRYHRGNGIGVSLPPgnKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRS 591
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 517308034 553 LARHHEMVITVEEGSIGGFGSHVMHFLATEGLLDNGLKLrslvmPDIWMEQAKP 606
Cdd:PLN02234 592 LAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKV-----YRTWITNGST 640
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
10-283 |
3.15e-176 |
|
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: 501.17 E-value: 3.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 10 LDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPHKILTG 89
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 90 RRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGAL 169
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 170 DARLIVILNDNDMSIAPPTGAMSAYLARLASGRTYMGFRDLGKK-LTAYLGKNIDRAITRAVEHARGYVTGGTMFEEMGF 248
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKlLKPKIGPPLYELARRAKESLKGLVVPGTLFEELGF 240
|
250 260 270
....*....|....*....|....*....|....*
gi 517308034 249 YHIGPIDGHSFDHLLPVLRNVRDNGrGPVLIHVVT 283
Cdd:pfam13292 241 KYIGPIDGHDLDALVKVLENAKDLK-GPVLLHVVT 274
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
6-630 |
2.63e-172 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 507.33 E-value: 2.63e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 6 KTPLLDQVIYPADLRKLEDRDLPQLAREVRDEMIDAV-SRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPH 84
Cdd:PLN02225 75 ETPILDSIETPLQLKNLSVKELKLLADEIRTELHSVLwKKTQKSMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 85 KILTGRRDRIRTlRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALN 164
Cdd:PLN02225 155 KVLTRRWSAIPS-RQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGKRDRVVAVIDNATITAGQAYEAMS 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 165 NAGALDARLIVILNDNDMSIAP--------PTGAMSAYLARLASGRTYMGFRDLGKKLTAYLGKNIDRAITRAVEHARGY 236
Cdd:PLN02225 234 NAGYLDSNMIVILNDSRHSLHPnmeegskaSISALSSIMSKIQSSKIFRKFRELAKAMTKRIGKGMYEWAAKVDEYARGM 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 237 V--TGGTMFEEMGFYHIGPIDGHSFDHLLPVLRNVRD-NGRGPVLIHVVTQKGKgyppaeaaadkyhgvnkfDVITGAQA 313
Cdd:PLN02225 314 VgpTGSTLFEELGLYYIGPVDGHNIEDLVCVLREVSSlDSMGPVLVHVITEENR------------------DAETGKNI 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 314 RVKpNAPSYTSVFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALY 393
Cdd:PLN02225 376 MVK-DRRTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIP 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 394 STFLQRAYDQVVHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPI 473
Cdd:PLN02225 455 SAFLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDRPV 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 474 SFRYPRGEGVGVD-MPARGEILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQ 552
Cdd:PLN02225 535 CFRFPRGSIVNMNyLVPTGLPIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRD 614
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517308034 553 LARHHEMVITVEEGSIGGFGSHVMHFLATEGLLDNGLKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKALGR 630
Cdd:PLN02225 615 LCQNHKFLITVEEGCVGGFGSHVAQFIALDGQLDGNIKWRPIVLPDGYIEEASPREQLALAGLTGHHIAATALSLLGR 692
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
8-590 |
1.08e-154 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 457.93 E-value: 1.08e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 8 PLLDQVIYPADLRKLEDRDLPQLAREVRDEMIDAVSRTGGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPHKIL 87
Cdd:PRK12315 1 MYLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 88 TGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAG 167
Cdd:PRK12315 81 TGRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 168 ALDARLIVILNDNDMSIAPPTGAMsaylarlasgrtYMGFRDLgkkltaylgknidRAITRAVEHargyvtggTMFEEMG 247
Cdd:PRK12315 161 ELKSNLIIIVNDNQMSIAENHGGL------------YKNLKEL-------------RDTNGQSEN--------NLFKAMG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 248 FYHIGPIDGHSFDHLLPVLRNVRDNGRgPVLIHVVTQKGKGYPPAEAAADKYHGVNKFDVITGaQARVKPNAPSYTSVFA 327
Cdd:PRK12315 208 LDYRYVEDGNDIESLIEAFKEVKDIDH-PIVLHIHTLKGKGYQPAEENKEAFHWHMPFDLETG-QSKVPASGESYSSVTL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 328 EALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYDQVVHD 407
Cdd:PRK12315 286 DYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQRAYDQLSHD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 408 VAIQGLPVRFPIdRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISFRYPrgegvGVDM 487
Cdd:PRK12315 366 LAINNNPAVMIV-FGGSISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAIRVP-----EHGV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 488 PARGEILQ---IGKGRIVKEGTKVALLSFGTRLADCLLAAEDL-DAAGLSTTVADARFAKPLDHDLIRQLARHHEMVITV 563
Cdd:PRK12315 440 ESGPTVDTdysTLKYEVTKAGEKVAILALGDFYELGEKVAKKLkEELGIDATLINPKFITGLDEELLEKLKEDHELVVTL 519
|
570 580 590
....*....|....*....|....*....|
gi 517308034 564 EEGSI-GGFGSHVMHFLATEGL--LDNGLK 590
Cdd:PRK12315 520 EDGILdGGFGEKIARYYGNSDMkvLNYGAK 549
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
46-289 |
5.37e-114 |
|
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: 339.14 E-value: 5.37e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 46 GGHLGAGLGVVELTIAIHSVFDTPDDRLIFDVGHQCYPHKILTGRRDRIRTLRQEDGLSGFTRRAESEYDPFGAAHSSTS 125
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 126 ISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGALDARLIVILNDNDMSIAPPTGamsaylarlasgrtym 205
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 206 gfrdlgkkltaylgknidraitravehargyvTGGTMFEEMGFYHIGPIDGHSFDHLLPVLRNVRDnGRGPVLIHVVTQK 285
Cdd:cd02007 145 --------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKD-LKGPVLLHVVTKK 191
|
....
gi 517308034 286 GKGY 289
Cdd:cd02007 192 GKGY 195
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
325-628 |
1.68e-68 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 225.35 E-value: 1.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 325 VFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFL-QRAYDQ 403
Cdd:COG3958 9 AFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLtGRAYEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 404 VVHDVAIQGLPVR-FPIDrAGF-VGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDgGPISFRYPRGE 481
Cdd:COG3958 89 IRNDIAYPNLNVKiVGSH-AGLsYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHD-GPVYLRLGRGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 482 gvgvdMPA---RGEILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHE 558
Cdd:COG3958 167 -----VPVvydEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTG 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517308034 559 MVITVEEGSI-GGFGSHVMHFLATEglldNGLKLRSLVMPDIWMEQAKPEAMNAHAGLDRAGIVSTVFKAL 628
Cdd:COG3958 242 AVVTAEEHSIiGGLGSAVAEVLAEN----YPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
325-479 |
2.25e-64 |
|
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: 208.84 E-value: 2.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 325 VFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYDQV 404
Cdd:cd07033 2 AFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517308034 405 VHDVAIQGLPVRFPIDRAGF-VGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDgGPISFRYPR 479
Cdd:cd07033 82 RHDVALQNLPVKFVGTHAGIsVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYD-GPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
319-481 |
1.54e-44 |
|
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: 156.56 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 319 APSYTSVFAEALVQEAALDDKIVGITAAMPNGTGLDKLAEAFPS---RCFDVGIAEQHAVTFAAGLAAEG--YKPFAALY 393
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEATF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 394 STFLQRAYDQVVHDVAIQGLPVRFPIDRAG-FVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDG-G 471
Cdd:pfam02779 82 SDFLNRADDAIRHGAALGKLPVPFVVTRDPiGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGrK 161
|
170
....*....|
gi 517308034 472 PISFRYPRGE 481
Cdd:pfam02779 162 PVVLRLPRQL 171
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
365-484 |
1.59e-39 |
|
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: 141.47 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 365 FDVGIAEQHAVTFAAGLAAEGYKPFAALYSTFLQRAYDQVVHDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTL 444
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 517308034 445 PGFVVMAAADEAELKHMVRTAVAYDgGPISFRYPRGEGVG 484
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIRDD-GPVVIRLERKSLYR 136
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
126-624 |
5.69e-27 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 115.62 E-value: 5.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 126 ISAGLGMAIAA----------DLDKSDRRVIAVIGDGAMSAGMAYEALNNAG--ALDaRLIVILNDNDMSIAPPT-GAMS 192
Cdd:PRK05899 124 LANAVGMALAEkylaalfnrpGLDIVDHYTYVLCGDGDLMEGISHEACSLAGhlKLG-NLIVIYDDNRISIDGPTeGWFT 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 193 -AYLARlasgrtymgfrdlgkkltaylgknidraitravehargyvtggtmFEEMGFYHIgPIDGHSFDHLLPVLRNVRD 271
Cdd:PRK05899 203 eDVKKR---------------------------------------------FEAYGWHVI-EVDGHDVEAIDAAIEEAKA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 272 NGRgPVLIHVVTQKGKGYPPAEAAAdKYHG--VNKFDVitgAQARVKPNAPsYTSVFAEALVQEAALDDKIVGITA--AM 347
Cdd:PRK05899 237 STK-PTLIIAKTIIGKGAPNKEGTH-KVHGapLGAEEI---AAAKKELGWD-YRKASGKALNALAKALPELVGGSAdlAG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 348 PNGTGLDK----LAEAFPSRCFDVGIAEQHAVTFAAGLAAEG-YKPFAALYSTFLQRAYDQvVHDVAIQGLPVRFPIDRA 422
Cdd:PRK05899 311 SNNTKIKGskdfAPEDYSGRYIHYGVREFAMAAIANGLALHGgFIPFGGTFLVFSDYARNA-IRLAALMKLPVIYVFTHD 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 423 G-FVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISFRYPRG------EGVGVDMPARGeilq 495
Cdd:PRK05899 390 SiGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQnlpvleRTAQEEGVAKG---- 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 496 igkGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDhdliRQLARHHEMV--------ITVEEGS 567
Cdd:PRK05899 466 ---GYVLRDDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFD----EQDAAYKESVlpaavtarVAVEAGV 538
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 517308034 568 IGGFGSHVmhflateglldnGLKLRSLVMpDIWMEQAKPEAMNAHAGLDRAGIVSTV 624
Cdd:PRK05899 539 ADGWYKYV------------GLDGKVLGI-DTFGASAPADELFKEFGFTVENIVAAA 582
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
497-620 |
6.52e-27 |
|
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: 105.76 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 497 GKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVITVEEGS-IGGFGSHV 575
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVpRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 517308034 576 MHFLATEGLLDNGLKLRSLVMPDIWMeQAKPEAMNAHAGLDRAGI 620
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLRVGGPDFPE-PGSADELEKLYGLTPEKI 124
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
356-573 |
4.04e-21 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 95.43 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 356 LAEAF-PSRCFDVGIAEQHAVTFAAGLAAEGYKPFAA-LYSTFLQRAYDQVVHDVAIQ----------GLPVRFPidrAG 423
Cdd:PTZ00182 75 LLDKYgPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEfMFADFIFPAFDQIVNEAAKYrymsggqfdcPIVIRGP---NG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 424 FVGADGPTHAGSFDTtFLTTLPGFVVMAAADEAELKHMVRTAVAyDGGPISFRYPRG-EGVGVDMPARGE-ILQIGKGRI 501
Cdd:PTZ00182 152 AVGHGGAYHSQSFEA-YFAHVPGLKVVAPSDPEDAKGLLKAAIR-DPNPVVFFEPKLlYRESVEVVPEADyTLPLGKAKV 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517308034 502 VKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVITVEEGSI-GGFGS 573
Cdd:PTZ00182 230 VREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPtCGIGA 302
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
356-583 |
3.68e-19 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 89.01 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 356 LAEAF-PSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYS-TFLQRAYDQVVHDVA----IQGLPVRFPIDRAGFVGADG 429
Cdd:PRK09212 44 LLEQFgPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFMTfNFSMQAIDQIVNSAAktnyMSGGQLKCPIVFRGPNGAAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 430 ---PTHAGSFdTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISFRYPRGEGVGVDMPARGEILQIGKGRIVKEGT 506
Cdd:PRK09212 124 rvaAQHSQCY-AAWYSHIPGLKVVAPYFAADCKGLLKTAIRDPNPVIFLENEILYGHSHEVPEEEESIPIGKAAILREGS 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517308034 507 KVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVITVEEG-SIGGFGSHVMHFLATEG 583
Cdd:PRK09212 203 DVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKTNRLVVVEEGwPFAGVGAEIAALIMKEA 280
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
325-479 |
2.91e-18 |
|
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: 82.01 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 325 VFAEALVQEAalddKIVGITAAMPNGTGLDKLAEAFPSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALY-STFLQRAYDQ 403
Cdd:cd06586 2 AFAEVLTAWG----VRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTsGTGLLNAING 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517308034 404 VVhDVAIQGLPVRFPIDRAGFVGADGPTHAGSFDTTFLTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISF--RYPR 479
Cdd:cd06586 78 LA-DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVvvRLPR 154
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
32-301 |
6.03e-17 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 81.01 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 32 REVRDEMIDAVSRTG-GHLGAGLGVVELTIA------IHSVFDtPD----DRLIFDVGHQC---YPHKILTG--RRDRIR 95
Cdd:cd02012 1 NRIRRLSIDMVQKAGsGHPGGSLSAADILAVlyfkvlKYDPAD-PKwpnrDRFVLSKGHASpalYAVLALAGylPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 96 TLRQEDG-LSGFTrraesEYDPFGAAHSSTS-----ISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGA- 168
Cdd:cd02012 80 TFRQLGSrLPGHP-----EYGLTPGVEVTTGslgqgLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHy 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 169 -LDaRLIVILNDNDMSIAPPTGAMSAylarlasgrtymgFRDLGKKLTAYlgknidraitravehargyvtggtmfeemG 247
Cdd:cd02012 155 kLD-NLIAIVDSNRIQIDGPTDDILF-------------TEDLAKKFEAF-----------------------------G 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 517308034 248 FYHIgPIDGHSFDHLLPVLRNVRDNGRGPVLIHVVTQKGKGYPPAEAAAdKYHG 301
Cdd:cd02012 192 WNVI-EVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA-KWHG 243
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
20-302 |
7.15e-15 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 75.11 E-value: 7.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 20 RKLEDRDLPQLAREVRDEMIDAVSRTG-GHLGAGLGVVE-LTIAIHSVF----DTPD----DRLIFDVGHQC---YPHKI 86
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGsGHPGGSLSAADiLAALYFKVMnidpKNPDwpdrDRFILSKGHAApalYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 87 LTGR--RDRIRTLRQEDG-LSGftrraeseydpfgaaHSSTS---------------ISAGLGMAIAADLDKSDRRVIAV 148
Cdd:COG3959 81 EKGYfpKEELATFRKLGSrLQG---------------HPDMKktpgvemstgslgqgLSVAVGMALAAKLDGKDYRVYVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 149 IGDGAMSAGMAYEALNNAGA--LDaRLIVILNDNDMSIAPPTGAMsaylarlasgrtyMGFRDLGKKltaylgknidrai 226
Cdd:COG3959 146 LGDGELQEGQVWEAAMAAAHykLD-NLIAIVDRNGLQIDGPTEDV-------------MSLEPLAEK------------- 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517308034 227 travehargyvtggtmFEEMGFYHIgPIDGHSFDHLLPVLRNVRDNGRGPVLIHVVTQKGKGYPPAEAAAdKYHGV 302
Cdd:COG3959 199 ----------------WEAFGWHVI-EVDGHDIEALLAALDEAKAVKGKPTVIIAHTVKGKGVSFMENRP-KWHGK 256
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
329-566 |
8.82e-13 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 70.23 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 329 ALVQEAALDDKIVGITAAMPNGTGLDKLAEAF-----PSRCFDVGIAEQHAVTFAAGLAAEGYKPFAALYS-TFLQRAYD 402
Cdd:PLN02683 36 ALDEEMSADPKVFIMGEEVGEYQGAYKITKGLlqkygPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTfNFSMQAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 403 QVVHDVAIQ--------GLPVRF--PIDRAGFVGADgptHAGSFdTTFLTTLPGFVVMAAADEAELKHMVRTAVAyDGGP 472
Cdd:PLN02683 116 HIINSAAKTnymsagqiSVPIVFrgPNGAAAGVGAQ---HSQCF-AAWYSSVPGLKVLAPYSSEDARGLLKAAIR-DPDP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 473 ISF-----RYprgegvGVDMPARGEILQ------IGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARF 541
Cdd:PLN02683 191 VVFlenelLY------GESFPVSAEVLDssfvlpIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRS 264
|
250 260
....*....|....*....|....*
gi 517308034 542 AKPLDHDLIRQLARHHEMVITVEEG 566
Cdd:PLN02683 265 IRPLDRDTINASVRKTNRLVTVEEG 289
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
124-283 |
6.64e-09 |
|
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: 57.84 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 124 TSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGALDARLIVILNDNDMSIAPPTGAMSAY--LARLASG 201
Cdd:COG1071 131 GQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAISTPVERQTAVetIADRAAG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 202 rtyMGFRdlgkkltaylGKNID--------RAITRAVEHARgyvtggtmfeemgfyhigpidghsfdhllpvlrnvrdNG 273
Cdd:COG1071 211 ---YGIP----------GVRVDgndvlavyAAVKEAVERAR-------------------------------------AG 240
|
170
....*....|
gi 517308034 274 RGPVLIHVVT 283
Cdd:COG1071 241 EGPTLIEAKT 250
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
493-575 |
7.44e-09 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 58.39 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 493 ILQIGKGRIVKEGTKVALLSFGTRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVITVEEG-SIGGF 571
Cdd:PRK11892 328 VLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEEGwPQSGV 407
|
....
gi 517308034 572 GSHV 575
Cdd:PRK11892 408 GAEI 411
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
328-466 |
9.23e-09 |
|
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132919 [Multi-domain] Cd Length: 167 Bit Score: 55.18 E-value: 9.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 328 EALVQEAALDDKIV--GITAAMPNGTGL--DKLAEAF-PSRCFDVGIAEQHAVTFAAGLAAEGYKPFAAL-YSTFLQRAY 401
Cdd:cd07036 5 EALDEEMERDPRVVvlGEDVGDYGGVFKvtKGLLDKFgPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFALPAF 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517308034 402 DQVVHDVA--------IQGLP--VRFPIdraGFVGADGPTHAGSFDTTFlTTLPGFVVMAAADEAELKHMVRTAV 466
Cdd:cd07036 85 DQIVNEAAklrymsggQFKVPivIRGPN---GGGIGGGAQHSQSLEAWF-AHIPGLKVVAPSTPYDAKGLLKAAI 155
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
47-301 |
5.32e-08 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 55.84 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 47 GHLGAGLGVVELTIAIHS---VFDTPD------DRLIFDVGHQC---YPHKILTGRR---DRIRTLRQEDGLS------G 105
Cdd:PTZ00089 27 GHPGAPMGMAPIAHILWSevmKYNPKDprwinrDRFVLSNGHASallYSMLHLTGYDlsmEDLKNFRQLGSRTpghperH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 106 FTRRAESEYDPFGAAhsstsISAGLGMAIAA----------DLDKSDRRVIAVIGDGAMSAGMAYEALNNAGALD-ARLI 174
Cdd:PTZ00089 107 ITPGVEVTTGPLGQG-----IANAVGLAIAEkhlaakfnrpGHPIFDNYVYVICGDGCLQEGVSQEALSLAGHLGlEKLI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 175 VILNDNDMSIapptgamsaylarlaSGRTYMGF-RDLGKKltaylgknidraitravehargyvtggtmFEEMGFYHIGP 253
Cdd:PTZ00089 182 VLYDDNKITI---------------DGNTDLSFtEDVEKK-----------------------------YEAYGWHVIEV 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 517308034 254 IDGHS-FDHLLPVLRNVRDNGRGPVLIHVVTQKGKGypPAEAAADKYHG 301
Cdd:PTZ00089 218 DNGNTdFDGLRKAIEEAKKSKGKPKLIIVKTTIGYG--SSKAGTEKVHG 264
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
106-283 |
1.13e-06 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 48.79 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 106 FTRRAESEYDPFGAAHSSTSISAGLGMAIAAdldkSDRRVIAVIGDGamSAGMAYEALNNAGALDARLIVILNDNDMSIa 185
Cdd:cd00568 32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAA----PDRPVVCIAGDG--GFMMTGQELATAVRYGLPVIVVVFNNGGYG- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 186 pptgamsaylarlaSGRTYMGFRDLGKKLTAYLGkNIDRAitravehargyvtggTMFEEMGFYHIGPIDGhsfDHLLPV 265
Cdd:cd00568 105 --------------TIRMHQEAFYGGRVSGTDLS-NPDFA---------------ALAEAYGAKGVRVEDP---EDLEAA 151
|
170
....*....|....*...
gi 517308034 266 LRNVRDNGrGPVLIHVVT 283
Cdd:cd00568 152 LAEALAAG-GPALIEVKT 168
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
124-283 |
1.46e-06 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 50.19 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 124 TSISAGLGMAIAADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGALDARLIVILNDNDMSIAPPTGAMSA--YLARLASG 201
Cdd:cd02000 108 GQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCENNGYAISTPTSRQTAgtSIADRAAA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 202 RTYMGFRDLGKKLTAylgknIDRAITRAVEHARgyvtggtmfeemgfyhigpidghsfdhllpvlrnvrdNGRGPVLIHV 281
Cdd:cd02000 188 YGIPGIRVDGNDVLA-----VYEAAKEAVERAR-------------------------------------AGGGPTLIEA 225
|
..
gi 517308034 282 VT 283
Cdd:cd02000 226 VT 227
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
29-184 |
1.77e-06 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 50.46 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 29 QLAREVRDEMIDAVSRTG-GHLGAGLGVVELTIAIHSVFDTPD---------DRLIFDVGHQC---YPHKILTG---RRD 92
Cdd:pfam00456 4 RAVNAIRALAMDAVEKANsGHPGAPMGMAPIAEVLFKRFLKHNpndpkwinrDRFVLSNGHGSmllYSLLHLTGydlSME 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 93 RIRTLRQEDGLS------GFTRRAESEYDPFGAAhsstsISAGLGMAIA----------ADLDKSDRRVIAVIGDGAMSA 156
Cdd:pfam00456 84 DLKSFRQLGSKTpghpefGHTAGVEVTTGPLGQG-----IANAVGMAIAernlaatynrPGFDIVDHYTYVFLGDGCLME 158
|
170 180
....*....|....*....|....*....
gi 517308034 157 GMAYEALNNAGALD-ARLIVILNDNDMSI 184
Cdd:pfam00456 159 GVSSEASSLAGHLGlGNLIVFYDDNQISI 187
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
48-201 |
7.86e-05 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 45.01 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 48 HLGAGLGVVELTIAIHSvfdTPDDRLIfdVGHQCYPHKILTGrrDRIR------TLRQEDGLSG-----FTRRAESEYDP 116
Cdd:pfam00676 27 HLYAGQEAAQVGIAAAL---EPGDYII--PGYRDHGNLLARG--LSLEeifaelYGRVAKGKGGsmhgyYGAKGNRFYGG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 117 FGAAHSSTSISAGLGMAiaADLDKSDRRVIAVIGDGAMSAGMAYEALNNAGALDARLIVILNDND--MSIAPPTGAMSAY 194
Cdd:pfam00676 100 NGILGAQVPLGAGIALA--AKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCENNQygISTPAERASASTT 177
|
....*..
gi 517308034 195 LARLASG 201
Cdd:pfam00676 178 YADRARG 184
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
116-181 |
2.83e-04 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 42.26 E-value: 2.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517308034 116 PFGAAHSSTSISAGLGMAIAADLDKSDRRVIAVIGDGA-MSAGMayEALNNAGALDARLIVILNDND 181
Cdd:cd02008 43 PLNAIDTCTCMGASIGVAIGMAKASEDKKVVAVIGDSTfFHSGI--LGLINAVYNKANITVVILDNR 107
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
363-576 |
3.97e-04 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 42.80 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 363 RCFDVGIAEQHAVTFAAGLAAEGYKPFA-ALYSTFLQRAYDQVVHDVAI----QGLPVRFP--IDRAGFVGAD-GPTHAG 434
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAMTGLRPIVeGMNMGFLLLAFNQISNNAGMlhytSGGNFTIPivIRGPGGVGRQlGAEHSQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 435 SFDTTFlTTLPGFVVMAAADEAELKHMVRTAVAYDGGPISFRYPRGEGVGVDMPARGEILQIGKGRIVKEGTKVALLSFG 514
Cdd:CHL00144 132 RLESYF-QSVPGLQIVACSTPYNAKGLLKSAIRSNNPVIFFEHVLLYNLKEEIPDNEYLLPLEKAEVVRPGNDITILTYS 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517308034 515 TRLADCLLAAEDLDAAGLSTTVADARFAKPLDHDLIRQLARHHEMVITVEEG-SIGGFGSHVM 576
Cdd:CHL00144 211 RMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTHKVLIVEECmKTGGIGAELI 273
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
129-234 |
1.70e-03 |
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Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 39.82 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 129 GLGMAIAADLDKSDRRVIAVIGDGA--MSaGMAYEAL--NNAGAldarLIVILNDN-----DMSIAPPTGAMSAYLARLA 199
Cdd:cd02004 53 GLGYAIAAALARPDKRVVLVEGDGAfgFS-GMELETAvrYNLPI----VVVVGNNGgwyqgLDGQQLSYGLGLPVTTLLP 127
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90 100 110
....*....|....*....|....*....|....*...
gi 517308034 200 SGRTYMGFRDLGKKltAYLGKNID---RAITRAVEHAR 234
Cdd:cd02004 128 DTRYDLVAEAFGGK--GELVTTPEelkPALKRALASGK 163
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| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
129-281 |
2.08e-03 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 39.11 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517308034 129 GLGMAIAADLDKSDRRVIAVIGDGamSAGMAYEALNNAGALDARLIVILNDNDMSiapptgAMSAYLARLASGRTYMGfr 208
Cdd:pfam02775 33 GLPAAIGAKLARPDRPVVAIAGDG--GFQMNLQELATAVRYNLPITVVVLNNGGY------GMTRGQQTPFGGGRYSG-- 102
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517308034 209 dlgkkLTAYLGKNIDraitrAVEHARGY-VTGGTmfeemgfyhigpidGHSFDHLLPVLRNVRDNGrGPVLIHV 281
Cdd:pfam02775 103 -----PSGKILPPVD-----FAKLAEAYgAKGAR--------------VESPEELEEALKEALEHD-GPALIDV 151
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| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
125-181 |
7.53e-03 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 37.90 E-value: 7.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 517308034 125 SISAGLGMAIAADLDKSDRRVIAVIGDGAMSagMAYEALNNAGALDARLI-VILNDND 181
Cdd:cd02014 52 TMGNGLPGAIAAKLAYPDRQVIALSGDGGFA--MLMGDLITAVKYNLPVIvVVFNNSD 107
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