|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
11-628 |
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: 979.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 11 GRLLGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKI 90
Cdd:COG1154 2 TPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 91 LTGRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNI 170
Cdd:COG1154 82 LTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 171 ATAGNPLVIVVNDNGRSYSPTIGGLADHLSSLRLNPGYEKVLDTVKDALGNTPFVGKPMYEVLHAVKKGIKDAVAPQAMF 250
Cdd:COG1154 162 GHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPGIGPPLYELARRAKEGLKGLVVPGTLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 251 EDLGIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVTRKGYGYRPAEDDEaDCLHGPGAFDAETGKLLAVPSVK--WT 328
Cdd:COG1154 242 EELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDP-DKFHGVGPFDPETGEPKKSKSSApsYT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 329 NVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQ 408
Cdd:COG1154 321 DVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 409 VLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVdDGPTILRFPTGTVA 488
Cdd:COG1154 401 VIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIRYPRGNGP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 489 -ADLPAVRR---VGPVDVLAESarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELV-ELASAHRLVV 563
Cdd:COG1154 480 gVELPAELEplpIGKGEVLREG--KDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELIlELAREHDLVV 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033141171 564 TVEDGVRIGGVGSALAQAMRDADVRVPVKDMGVPADWHPHGSRAQILADLRLTAQDVARDVTGWI 628
Cdd:COG1154 558 TVEEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELL 622
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
13-628 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 882.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 13 LLGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILT 92
Cdd:PRK05444 6 LLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPHKILT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 93 GRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRG-EKRSVVAVVGDGALTGGMCWEALNNIA 171
Cdd:PRK05444 86 GRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGgEDRKVVAVIGDGALTGGMAFEALNNAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 172 TAGNPLVIVVNDNGRSYSPTIGGLADHLSSLRLNpgyekvldtvkdalgntpfvgkpmyevlhavkkgikdavapqAMFE 251
Cdd:PRK05444 166 DLKSDLIVILNDNEMSISPNVGALSNYLARLRSS------------------------------------------TLFE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 252 DLGIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVTRKGYGYRPAEDDEADClHGPGAFDAETGKLLAV---PSVKWT 328
Cdd:PRK05444 204 ELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKY-HGVGKFDPETGEQPKSskpGKPSYT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 329 NVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQ 408
Cdd:PRK05444 283 KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 409 VLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPTILRFPTGT-V 487
Cdd:PRK05444 363 VIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNgV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 488 AADLPAVRR--VGPVDVLAESarTDVLLVAVGSFAGLGVEVAARVAEqgygVTVVDPRWVRPVPAELV-ELASAHRLVVT 564
Cdd:PRK05444 443 GVELPELEPlpIGKGEVLREG--EDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLlELAAKHDLVVT 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033141171 565 VEDGVRIGGVGSALAQAMRDADVRVPVKDMGVPADWHPHGSRAQILADLRLTAQDVARDVTGWI 628
Cdd:PRK05444 517 VEEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
14-628 |
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: 582.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 14 LGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILTG 93
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 94 RQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIATA 173
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 174 GNPLVIVVNDNGRSYSPTIGGLADHLSSLRLNPGYEKVLDTVKDALGNTPFVGKPMYEvlhAVKKGIKDAVAPQAMFEDL 253
Cdd:TIGR00204 161 KTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYLAK---RTEESMKGLVVPGTFFEEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 254 GIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVTRKGYGYRPAEDDEADcLHGPGAFDAETGKLL----AVPSvkWTN 329
Cdd:TIGR00204 238 GFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIG-WHGVGPFDLSTGCLPksksALPS--YSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 330 VFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQV 409
Cdd:TIGR00204 315 IFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 410 LLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPTILRFPTGTVAA 489
Cdd:TIGR00204 395 VHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 490 ----DLPAVRRVGPVDVLAESarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELV-ELASAHRLVVT 564
Cdd:TIGR00204 475 veltPEPEKLPIGKSEVLRKG--EKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELIlEIAASHEKLVT 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033141171 565 VEDGVRIGGVGSALAQAMRDADVRVPVKDMGVPADWHPHGSRAQILADLRLTAQDVARDVTGWI 628
Cdd:TIGR00204 553 VEENAIMGGAGSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWL 616
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
14-289 |
1.21e-167 |
|
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: 479.60 E-value: 1.21e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 14 LGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILTG 93
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 94 RQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIATA 173
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 174 GNPLVIVVNDNGRSYSPTIGGLADHLSSLRLNPGYEKVLDTVKDALGntPFVGKPMYEVLHAVKKGIKDAVAPQAMFEDL 253
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLK--PKIGPPLYELARRAKESLKGLVVPGTLFEEL 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1033141171 254 GIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVT 289
Cdd:pfam13292 239 GFKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
50-295 |
4.40e-99 |
|
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: 301.00 E-value: 4.40e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 50 GGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILTGRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTA 129
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 130 LSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIATAGNPLVIVVNDNGRSYSPTIGgladhlsslrlnpgye 209
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 210 kvldtvkdalgntpfvgkpmyevlhavkkgikdavAPQAMFEDLGIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVT 289
Cdd:cd02007 145 -----------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVT 189
|
....*.
gi 1033141171 290 RKGYGY 295
Cdd:cd02007 190 KKGKGY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
370-483 |
1.29e-36 |
|
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: 133.38 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 370 YDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQVLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVV 449
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110
....*....|....*....|....*....|....
gi 1033141171 450 PGLRIAAPRDSATLREELREAIAvDDGPTILRFP 483
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLE 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
11-628 |
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: 979.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 11 GRLLGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKI 90
Cdd:COG1154 2 TPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 91 LTGRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNI 170
Cdd:COG1154 82 LTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 171 ATAGNPLVIVVNDNGRSYSPTIGGLADHLSSLRLNPGYEKVLDTVKDALGNTPFVGKPMYEVLHAVKKGIKDAVAPQAMF 250
Cdd:COG1154 162 GHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPGIGPPLYELARRAKEGLKGLVVPGTLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 251 EDLGIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVTRKGYGYRPAEDDEaDCLHGPGAFDAETGKLLAVPSVK--WT 328
Cdd:COG1154 242 EELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDP-DKFHGVGPFDPETGEPKKSKSSApsYT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 329 NVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQ 408
Cdd:COG1154 321 DVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 409 VLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVdDGPTILRFPTGTVA 488
Cdd:COG1154 401 VIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIRYPRGNGP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 489 -ADLPAVRR---VGPVDVLAESarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELV-ELASAHRLVV 563
Cdd:COG1154 480 gVELPAELEplpIGKGEVLREG--KDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELIlELAREHDLVV 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033141171 564 TVEDGVRIGGVGSALAQAMRDADVRVPVKDMGVPADWHPHGSRAQILADLRLTAQDVARDVTGWI 628
Cdd:COG1154 558 TVEEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELL 622
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
13-628 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 882.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 13 LLGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILT 92
Cdd:PRK05444 6 LLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPHKILT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 93 GRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRG-EKRSVVAVVGDGALTGGMCWEALNNIA 171
Cdd:PRK05444 86 GRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGgEDRKVVAVIGDGALTGGMAFEALNNAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 172 TAGNPLVIVVNDNGRSYSPTIGGLADHLSSLRLNpgyekvldtvkdalgntpfvgkpmyevlhavkkgikdavapqAMFE 251
Cdd:PRK05444 166 DLKSDLIVILNDNEMSISPNVGALSNYLARLRSS------------------------------------------TLFE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 252 DLGIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVTRKGYGYRPAEDDEADClHGPGAFDAETGKLLAV---PSVKWT 328
Cdd:PRK05444 204 ELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKY-HGVGKFDPETGEQPKSskpGKPSYT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 329 NVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQ 408
Cdd:PRK05444 283 KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 409 VLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPTILRFPTGT-V 487
Cdd:PRK05444 363 VIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNgV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 488 AADLPAVRR--VGPVDVLAESarTDVLLVAVGSFAGLGVEVAARVAEqgygVTVVDPRWVRPVPAELV-ELASAHRLVVT 564
Cdd:PRK05444 443 GVELPELEPlpIGKGEVLREG--EDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLlELAAKHDLVVT 516
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033141171 565 VEDGVRIGGVGSALAQAMRDADVRVPVKDMGVPADWHPHGSRAQILADLRLTAQDVARDVTGWI 628
Cdd:PRK05444 517 VEEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
7-640 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 787.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 7 TANHGRLLGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAY 86
Cdd:PRK12571 2 PRPKTPLLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 87 VHKILTGRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEA 166
Cdd:PRK12571 82 PHKILTGRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 167 LNNIATAGNPLVIVVNDNGRSYSPTIGGLADHLSSLRLNPGYEKVLDTVKDALGNTPfvgKPMYEVLHAVKKGIKDAVAP 246
Cdd:PRK12571 162 LNNAGAADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIAKGVEERLP---GPLRDGARRARELVTGMIGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 247 QAMFEDLGIKYVGPVDGHDVPAVEAALRAAK-NFGGPVIVHAVTRKGYGYRPAEDDEaDCLHGPGAFDAETGK-LLAVPS 324
Cdd:PRK12571 239 GTLFEELGFTYVGPIDGHDMEALLSVLRAARaRADGPVLVHVVTEKGRGYAPAEADE-DKYHAVGKFDVVTGLqKKSAPS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 325 VK-WTNVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLN 403
Cdd:PRK12571 318 APsYTSVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 404 RAFDQVLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPTILRFP 483
Cdd:PRK12571 398 RGYDQLLHDVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 484 TGT-VAADLPAVRRVGPVDVLAESAR-TDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELVELASAHRL 561
Cdd:PRK12571 478 RGEgVGVEIPAEGTILGIGKGRVPREgPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHI 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 562 VVTVEDGVRIGGVGSALAQAMRDA---DVRVPVKDMGVPADWHPHGSRAQILADLRLTAQDVARDVTGWISSLDATPVDP 638
Cdd:PRK12571 558 VVIVEEQGAMGGFGAHVLHHLADTgllDGGLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALARLSGVPERE 637
|
..
gi 1033141171 639 AA 640
Cdd:PRK12571 638 TA 639
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
14-628 |
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: 582.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 14 LGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILTG 93
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 94 RQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIATA 173
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 174 GNPLVIVVNDNGRSYSPTIGGLADHLSSLRLNPGYEKVLDTVKDALGNTPFVGKPMYEvlhAVKKGIKDAVAPQAMFEDL 253
Cdd:TIGR00204 161 KTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYLAK---RTEESMKGLVVPGTFFEEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 254 GIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVTRKGYGYRPAEDDEADcLHGPGAFDAETGKLL----AVPSvkWTN 329
Cdd:TIGR00204 238 GFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIG-WHGVGPFDLSTGCLPksksALPS--YSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 330 VFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQV 409
Cdd:TIGR00204 315 IFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 410 LLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPTILRFPTGTVAA 489
Cdd:TIGR00204 395 VHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 490 ----DLPAVRRVGPVDVLAESarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELV-ELASAHRLVVT 564
Cdd:TIGR00204 475 veltPEPEKLPIGKSEVLRKG--EKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELIlEIAASHEKLVT 552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033141171 565 VEDGVRIGGVGSALAQAMRDADVRVPVKDMGVPADWHPHGSRAQILADLRLTAQDVARDVTGWI 628
Cdd:TIGR00204 553 VEENAIMGGAGSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWL 616
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
14-289 |
1.21e-167 |
|
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: 479.60 E-value: 1.21e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 14 LGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILTG 93
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 94 RQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIATA 173
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 174 GNPLVIVVNDNGRSYSPTIGGLADHLSSLRLNPGYEKVLDTVKDALGntPFVGKPMYEVLHAVKKGIKDAVAPQAMFEDL 253
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLK--PKIGPPLYELARRAKESLKGLVVPGTLFEEL 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1033141171 254 GIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVT 289
Cdd:pfam13292 239 GFKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
13-624 |
1.80e-150 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 450.89 E-value: 1.80e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 13 LLGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILT 92
Cdd:PLN02582 33 LLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQSYPHKILT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 93 GRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIAT 172
Cdd:PLN02582 113 GRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAGY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 173 AGNPLVIVVNDNGRSYSPT---------IGGLADHLSSLRLNPGYEKVLDTVKdalGNTPFVGKPMYEVLHAVKKGIKDA 243
Cdd:PLN02582 193 LDSDMIVILNDNKQVSLPTatldgpappVGALSSALSRLQSSRPLRELREVAK---GVTKQIGGPMHELAAKVDEYARGM 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 244 VA--PQAMFEDLGIKYVGPVDGHDVPAVEAALRAAKNFG--GPVIVHAVTRKGYGYrPAEDDEADCLHGPGAFDAETGKL 319
Cdd:PLN02582 270 ISgsGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKttGPVLIHVVTEKGRGY-PYAERAADKYHGVVKFDPATGKQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 320 LAVP--SVKWTNVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAV 397
Cdd:PLN02582 349 FKVKakTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 398 YATFLNRAFDQVLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGP 477
Cdd:PLN02582 429 YSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIDDRP 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 478 TILRFPTGT-VAADLPAVRRVGPVDV-----LAESarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAE 551
Cdd:PLN02582 509 SCFRYPRGNgIGVQLPPNNKGIPIEVgkgriLLEG--ERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRA 586
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033141171 552 LV-ELASAHRLVVTVEDGvRIGGVGSALAQAMR-DA--DVRVPVKDMGVPADWHPHGSRAQILADLRLTAQDVARDV 624
Cdd:PLN02582 587 LIrSLAKSHEVLITVEEG-SIGGFGSHVAQFMAlDGllDGKLKWRPLVLPDRYIDHGAPADQLAEAGLTPSHIAATV 662
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
13-628 |
3.82e-148 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 441.37 E-value: 3.82e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 13 LLGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILT 92
Cdd:PRK12315 2 YLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKMLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 93 GRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIAT 172
Cdd:PRK12315 82 GRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 173 AGNPLVIVVNDNGRSYSPTIGGLADHLSSLRlnpgyekvlDTvkdalgntpfvgkpmyevlhavkkgikDAVAPQAMFED 252
Cdd:PRK12315 162 LKSNLIIIVNDNQMSIAENHGGLYKNLKELR---------DT---------------------------NGQSENNLFKA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 253 LGIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVTRKGYGYRPAEDDEADcLHGPGAFDAETGKLLaVPSVKW--TNV 330
Cdd:PRK12315 206 MGLDYRYVEDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKGYQPAEENKEA-FHWHMPFDLETGQSK-VPASGEsySSV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 331 FADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQVL 410
Cdd:PRK12315 284 TLDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQRAYDQLS 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 411 LDVAMHKLPVTFVLDRAGITGPDgPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPTILRFPTGTVAAD 490
Cdd:PRK12315 364 HDLAINNNPAVMIVFGGSISGND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAIRVPEHGVESG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 491 LPAVRRVGPVDVLAESARTDVLLVAVGSFAGLGVEVAARVAEQ-GYGVTVVDPRWVRPVPAELVE-LASAHRLVVTVEDG 568
Cdd:PRK12315 443 PTVDTDYSTLKYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEELLEkLKEDHELVVTLEDG 522
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 569 VRIGGVGSALAQAMRDADVRvpVKDMGVPADWHPHGSRAQILADLRLTAQDVARDVTGWI 628
Cdd:PRK12315 523 ILDGGFGEKIARYYGNSDMK--VLNYGAKKEFNDRVPVEELYKRNHLTPEQIVEDILSVL 580
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
13-605 |
4.54e-126 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 386.76 E-value: 4.54e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 13 LLGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKVSRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILT 92
Cdd:PLN02234 66 LLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 93 GRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIAT 172
Cdd:PLN02234 146 GRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGY 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 173 AGNPLVIVVNDNGRSYSPTIGgladhlsslrlnpgyekvLDtvkdalGNTPFVGKPMYEVLHAVKKGIKDAVAPQAMFED 252
Cdd:PLN02234 226 LHSNMIVILNDNKQVSLPTAN------------------LD------GPTQPVGALSCALSRLQSNCGMIRETSSTLFEE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 253 LGIKYVGPVDGHDVPAVEAALRAAKNFG--GPVIVHAVTRKGYGYRPAEDDEaDCLHGPGAFDAETGKLLA--VPSVKWT 328
Cdd:PLN02234 282 LGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERAD-DKYHGVLKFDPETGKQFKniSKTQSYT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 329 NVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQ 408
Cdd:PLN02234 361 SCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQ 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 409 VLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPTILRFPTGT-V 487
Cdd:PLN02234 441 VVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNgI 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 488 AADLPAVRR-----VGPVDVLAESARtdVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELVE-LASAHRL 561
Cdd:PLN02234 521 GVSLPPGNKgvplqIGRGRILRDGER--VALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRsLAKSHEV 598
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1033141171 562 VVTVEDGvRIGGVGSALAQ-----AMRDADVRVPVKdmgvpadWHPHGS 605
Cdd:PLN02234 599 LITVEEG-SIGGFGSHVVQflaldGLLDGKLKVYRT-------WITNGS 639
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
50-295 |
4.40e-99 |
|
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: 301.00 E-value: 4.40e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 50 GGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKILTGRQEGFDKLRQRGGLSGYPSQAESEHDLIENSHASTA 129
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 130 LSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIATAGNPLVIVVNDNGRSYSPTIGgladhlsslrlnpgye 209
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 210 kvldtvkdalgntpfvgkpmyevlhavkkgikdavAPQAMFEDLGIKYVGPVDGHDVPAVEAALRAAKNFGGPVIVHAVT 289
Cdd:cd02007 145 -----------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVT 189
|
....*.
gi 1033141171 290 RKGYGY 295
Cdd:cd02007 190 KKGKGY 195
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
13-580 |
3.43e-92 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 300.09 E-value: 3.43e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 13 LLGTVRGPQDVKRMTAEQLDILAAEIRDFLIAKV-SRTGGHVGPNLGVVELTLAMHRVFDSPRDRLLFDTGHQAYVHKIL 91
Cdd:PLN02225 78 ILDSIETPLQLKNLSVKELKLLADEIRTELHSVLwKKTQKSMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAHKVL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 92 TGRQEGFDKlRQRGGLSGYPSQAESEHDLIENSHASTALSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIA 171
Cdd:PLN02225 158 TRRWSAIPS-RQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGKRDRVVAVIDNATITAGQAYEAMSNAG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 172 TAGNPLVIVVNDNGRSYSP--------TIGGLADHLSSLRLNPGYEKVLDTVKDAlgnTPFVGKPMYEVLHAVKKGIKDA 243
Cdd:PLN02225 237 YLDSNMIVILNDSRHSLHPnmeegskaSISALSSIMSKIQSSKIFRKFRELAKAM---TKRIGKGMYEWAAKVDEYARGM 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 244 VAP--QAMFEDLGIKYVGPVDGHDVPAVEAALRAAKNFG--GPVIVHAVTRKGYgyrpaeddeadclhgpgafDAETGKL 319
Cdd:PLN02225 314 VGPtgSTLFEELGLYYIGPVDGHNIEDLVCVLREVSSLDsmGPVLVHVITEENR-------------------DAETGKN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 320 LAVPSVK-WTNVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVY 398
Cdd:PLN02225 375 IMVKDRRtYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIP 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 399 ATFLNRAFDQVLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPT 478
Cdd:PLN02225 455 SAFLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDRPV 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 479 ILRFPTGT-------VAADLPAvrRVGPVDVLAESarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAE 551
Cdd:PLN02225 535 CFRFPRGSivnmnylVPTGLPI--EIGRGRVLVEG--QDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIK 610
|
570 580 590
....*....|....*....|....*....|
gi 1033141171 552 LV-ELASAHRLVVTVEDGVrIGGVGSALAQ 580
Cdd:PLN02225 611 LVrDLCQNHKFLITVEEGC-VGGFGSHVAQ 639
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
329-628 |
2.42e-60 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 203.78 E-value: 2.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 329 NVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFL-NRAFD 407
Cdd:COG3958 8 DAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLtGRAYE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 408 QVLLDVAMHKLPVTFVLDRAGIT-GPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVdDGPTILRFPTGT 486
Cdd:COG3958 88 QIRNDIAYPNLNVKIVGSHAGLSyGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEH-DGPVYLRLGRGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 487 VaadlPAVR------RVGPVDVLAESarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELV-ELASAH 559
Cdd:COG3958 167 V----PVVYdedyefEIGKARVLREG--KDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAIlKAARKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033141171 560 RLVVTVEDGVRIGGVGSALAQAMRDAdVRVPVKDMGVPADWHPHGSRAQILADLRLTAQDVARDVTGWI 628
Cdd:COG3958 241 GAVVTAEEHSIIGGLGSAVAEVLAEN-YPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
329-483 |
1.10e-55 |
|
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: 186.11 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 329 NVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQ 408
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033141171 409 VLLDVAMHKLPVTFVLDRAGIT-GPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAvDDGPTILRFP 483
Cdd:cd07033 81 IRHDVALQNLPVKFVGTHAGISvGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALE-YDGPVYIRLP 155
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
327-483 |
1.02e-42 |
|
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: 151.55 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 327 WTNVFADELVAIADERPDVVGITAAMAEPTGIATLARKYPE---RVYDVGIAEQHAATSAAGLAMGG--LHPVVAVYATF 401
Cdd:pfam02779 5 TRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEATFSDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 402 LNRAFDQVLLDVAMHKLPVTFVLDRAGI-TGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDD-GPTI 479
Cdd:pfam02779 85 LNRADDAIRHGAALGKLPVPFVVTRDPIgVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGrKPVV 164
|
....
gi 1033141171 480 LRFP 483
Cdd:pfam02779 165 LRLP 168
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
370-483 |
1.29e-36 |
|
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: 133.38 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 370 YDVGIAEQHAATSAAGLAMGGLHPVVAVYATFLNRAFDQVLLDVAMHKLPVTFVLDRAGITGPDGPSHYGIWDMSVFGVV 449
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110
....*....|....*....|....*....|....
gi 1033141171 450 PGLRIAAPRDSATLREELREAIAvDDGPTILRFP 483
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLE 130
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
261-572 |
5.46e-29 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 122.16 E-value: 5.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 261 VDGHDVPAVEAALRAAKNFGGPVIVHAVTRKGYGYRPAEDDEAdcLHGPGAFDAETGKLLAVPSVKWTNVFADELVAIAD 340
Cdd:PRK05899 219 VDGHDVEAIDAAIEEAKASTKPTLIIAKTIIGKGAPNKEGTHK--VHGAPLGAEEIAAAKKELGWDYRKASGKALNALAK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 341 ERPDVVGITAAMAEPTGIATLARK------YPERVYDVGIAEQHAATSAAGLAM-GGLHPVVAVYATFLNRAFDQVLLDv 413
Cdd:PRK05899 297 ALPELVGGSADLAGSNNTKIKGSKdfapedYSGRYIHYGVREFAMAAIANGLALhGGFIPFGGTFLVFSDYARNAIRLA- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 414 AMHKLPVTFVLDRAGIT-GPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPTILRFPTGtvaaDLP 492
Cdd:PRK05899 376 ALMKLPVIYVFTHDSIGvGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQ----NLP 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 493 AVRRVGPVD-------VLAESArtDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVD---PRWVRPVPAELVE--LASAHR 560
Cdd:PRK05899 452 VLERTAQEEgvakggyVLRDDP--DVILIATGSEVHLALEAADELEAEGIKVRVVSmpsTELFDEQDAAYKEsvLPAAVT 529
|
330
....*....|..
gi 1033141171 561 LVVTVEDGVRIG 572
Cdd:PRK05899 530 ARVAVEAGVADG 541
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
509-620 |
4.88e-21 |
|
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: 89.19 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 509 TDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELV-ELASAHRLVVTVEDGVRIGGVGSALAQAMRD--- 584
Cdd:pfam02780 10 DDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETIlESVKKTGRLVTVEEAVPRGGFGSEVAAALAEeaf 89
|
90 100 110
....*....|....*....|....*....|....*.
gi 1033141171 585 ADVRVPVKDMGVPaDWHPHGSRAQILADLRLTAQDV 620
Cdd:pfam02780 90 DGLDAPVLRVGGP-DFPEPGSADELEKLYGLTPEKI 124
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
348-483 |
1.02e-17 |
|
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: 80.47 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 348 ITAAMAEPTGIATLARKYPERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYA-TFLNRAFDQVlLDVAMHKLPVTFVLDR 426
Cdd:cd06586 16 FGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSgTGLLNAINGL-ADAAAEHLPVVFLIGA 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033141171 427 AGITGPDGPSHYGIWDMSVFGVVPGLRIAAPRDSATLREELREAIAVDD--GPTILRFP 483
Cdd:cd06586 95 RGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAsqGPVVVRLP 153
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
361-585 |
1.01e-16 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 81.95 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 361 LARKY-PERVYDVGIAEQHAATSAAGLAMGGLHPVVAV-YATFLNRAFDQVLLDVAMH--------KLPVTFvldRA--G 428
Cdd:PTZ00182 75 LLDKYgPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFmFADFIFPAFDQIVNEAAKYrymsggqfDCPIVI---RGpnG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 429 ITGPDGPSH---YGIWDMSvfgvVPGLRIAAPRDSATLREELREAIAvDDGPTILRFPT---GTVAADLPAVRRVGPVDV 502
Cdd:PTZ00182 152 AVGHGGAYHsqsFEAYFAH----VPGLKVVAPSDPEDAKGLLKAAIR-DPNPVVFFEPKllyRESVEVVPEADYTLPLGK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 503 lAESAR--TDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELVE--LASAHRLvVTVEDGVRIGGVGSAL 578
Cdd:PTZ00182 227 -AKVVRegKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVksVKKTGRC-VIVHEAPPTCGIGAEI 304
|
....*...
gi 1033141171 579 -AQAMRDA 585
Cdd:PTZ00182 305 aAQIMEDC 312
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
361-582 |
4.73e-12 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 67.92 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 361 LARKY-PERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYA-TFLNRAFDQVLLDVAMH--------KLPVTFvldragiT 430
Cdd:PLN02683 67 LLQKYgPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTfNFSMQAIDHIINSAAKTnymsagqiSVPIVF-------R 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 431 GPDGPS------H---YGIWDMSVfgvvPGLRIAAPRDSATLREELREAIAVDDGPTILR--------FPTGTVAADLPA 493
Cdd:PLN02683 140 GPNGAAagvgaqHsqcFAAWYSSV----PGLKVLAPYSSEDARGLLKAAIRDPDPVVFLEnellygesFPVSAEVLDSSF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 494 VRRVGPVDVLAESarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELVeLASAHRL--VVTVEDGVRI 571
Cdd:PLN02683 216 VLPIGKAKIEREG--KDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTI-NASVRKTnrLVTVEEGWPQ 292
|
250
....*....|.
gi 1033141171 572 GGVGSALAQAM 582
Cdd:PLN02683 293 HGVGAEICASV 303
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
24-315 |
5.24e-12 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 66.64 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 24 KRMTAEQLDILAAEIRDFLIAKVSRTG-GHVGPNLGVVEL--TL---AMH----RVFDSPRDRLLFDTGHQA---YVHKI 90
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGsGHPGGSLSAADIlaALyfkVMNidpkNPDWPDRDRFILSKGHAApalYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 91 LTGR--QEGFDKLRQRGG-LSGYPSqaesEHDL--IEnshAST-----ALSYADGLAKAYALRGEKRSVVAVVGDGALTG 160
Cdd:COG3959 81 EKGYfpKEELATFRKLGSrLQGHPD----MKKTpgVE---MSTgslgqGLSVAVGMALAAKLDGKDYRVYVLLGDGELQE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 161 GMCWEA--------LNNiatagnpLVIVVNDNGRSysptIGGladhlsslrlnpgyekvldTVKDALGNTPFVGKpmyev 232
Cdd:COG3959 154 GQVWEAamaaahykLDN-------LIAIVDRNGLQ----IDG-------------------PTEDVMSLEPLAEK----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 233 lhavkkgikdavapqamFEDLGIkYVGPVDGHDVPAVEAALRAAKNF-GGPVIVHAVTRKGYGYRPAEDDEAdcLHGpGA 311
Cdd:COG3959 199 -----------------WEAFGW-HVIEVDGHDIEALLAALDEAKAVkGKPTVIIAHTVKGKGVSFMENRPK--WHG-KA 257
|
....
gi 1033141171 312 FDAE 315
Cdd:COG3959 258 PNDE 261
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
366-597 |
9.96e-12 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 66.67 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 366 PERVYDVGIAEQHAATSAAGLAMGGLHPVVAVYA-TFLNRAFDQVLLDVA-MH-------KLPVTFvldragiTGPDGPS 436
Cdd:PRK09212 50 PKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFMTfNFSMQAIDQIVNSAAkTNymsggqlKCPIVF-------RGPNGAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 437 ------H---YGIWdmsvFGVVPGLRIAAPRDSATLREELREAIAvDDGPTIlrFPTGTVA----ADLP---AVRRVGPV 500
Cdd:PRK09212 123 arvaaqHsqcYAAW----YSHIPGLKVVAPYFAADCKGLLKTAIR-DPNPVI--FLENEILyghsHEVPeeeESIPIGKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 501 DVLAESarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELVeLASAHRL--VVTVEDGVRIGGVGSAL 578
Cdd:PRK09212 196 AILREG--SDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETI-IESVKKTnrLVVVEEGWPFAGVGAEI 272
|
250 260
....*....|....*....|....*..
gi 1033141171 579 A-----QAMRDAD---VRVPVKDMGVP 597
Cdd:PRK09212 273 AalimkEAFDYLDapvERVTGKDVPLP 299
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
50-302 |
1.71e-11 |
|
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: 64.83 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 50 GGHVGPNLGVVELTLA-----MHRVFDSP----RDRLLFDTGHQA---YVHKILTGRQEGFD--KLRQRGG-LSGYPsqa 114
Cdd:cd02012 16 SGHPGGSLSAADILAVlyfkvLKYDPADPkwpnRDRFVLSKGHASpalYAVLALAGYLPEEDlkTFRQLGSrLPGHP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 115 esEHDLIENSHASTA-----LSYADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEAlnnIATAG----NPLVIVVNDNG 185
Cdd:cd02012 93 --EYGLTPGVEVTTGslgqgLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEA---ASFAGhyklDNLIAIVDSNR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 186 RSysptIGGladhlsslrlnpgyekvldTVKDALGNTPFVGKpmyevlhavkkgikdavapqamFEDLGIKYVgPVDGHD 265
Cdd:cd02012 168 IQ----IDG-------------------PTDDILFTEDLAKK----------------------FEAFGWNVI-EVDGHD 201
|
250 260 270
....*....|....*....|....*....|....*...
gi 1033141171 266 VPAVEAALRAAKNFGG-PVIVHAVTRKGYGYRPAEDDE 302
Cdd:cd02012 202 VEEILAALEEAKKSKGkPTLIIAKTIKGKGVPFMENTA 239
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
361-480 |
7.00e-11 |
|
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: 61.34 E-value: 7.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 361 LARKY-PERVYDVGIAEQHAATSAAGLAMGGLHPVVAV-YATFLNRAFDQVLLDVAMH--------KLPVTFvldRA--G 428
Cdd:cd07036 37 LLDKFgPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFALPAFDQIVNEAAKLrymsggqfKVPIVI---RGpnG 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1033141171 429 ITGPDGPSHYGiwDM-SVFGVVPGLRIAAPRDSATLREELREAIAvDDGPTIL 480
Cdd:cd07036 114 GGIGGGAQHSQ--SLeAWFAHIPGLKVVAPSTPYDAKGLLKAAIR-DDDPVIF 163
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
366-585 |
3.33e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 62.63 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 366 PERVYDVGIAEQHAATSAAGLAMGGLHPVVAvYATFlN---RAFDQVLLDVA----MH----KLPVTFvldragiTGPDG 434
Cdd:PRK11892 188 ARRVIDTPITEHGFAGIGVGAAFAGLKPIVE-FMTF-NfamQAIDQIINSAAktlyMSggqmGCPIVF-------RGPNG 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 435 PS------H---YGIWdmsvFGVVPGLRIAAPRDSATLREELREAIAvDDGPTI------LRFPTGTVAAD----LP--- 492
Cdd:PRK11892 259 AAarvaaqHsqdYAAW----YSHIPGLKVVAPYSAADAKGLLKAAIR-DPNPVIfleneiLYGQSFDVPKLddfvLPigk 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 493 -AVRRVGpvdvlaesarTDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELVeLAS---AHRLvVTVEDG 568
Cdd:PRK11892 334 aRIHREG----------KDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETI-VESvkkTNRL-VTVEEG 401
|
250
....*....|....*...
gi 1033141171 569 VRIGGVGSALA-QAMRDA 585
Cdd:PRK11892 402 WPQSGVGAEIAaRVMEQA 419
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
133-306 |
6.73e-08 |
|
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: 54.76 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 133 ADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIATAGNPLVIVVNDNG------RSYSPTIGGLADHLSslrlnp 206
Cdd:COG1071 136 AVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGyaistpVERQTAVETIADRAA------ 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 207 GYekvldtvkdalgntpfvgkpmyevlhavkkGIKdavapqamfedlGIKyvgpVDGHDVPAVEAALRAAKNF----GGP 282
Cdd:COG1071 210 GY------------------------------GIP------------GVR----VDGNDVLAVYAAVKEAVERaragEGP 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1033141171 283 VIVHAVTrkgY------------GYRPAEDDEA----DCL 306
Cdd:COG1071 244 TLIEAKT---YrlgghstsddptRYRTKEEVEEwrerDPI 280
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
127-286 |
7.00e-07 |
|
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: 49.97 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 127 STALSYADGLAKAYALRGEKRSVVAVVGDGALT-GGMcwEALNNIATAGNPLVIVVNDNGrsYSPTIGGlADHLSSLRLN 205
Cdd:cd02008 50 CTCMGASIGVAIGMAKASEDKKVVAVIGDSTFFhSGI--LGLINAVYNKANITVVILDNR--TTAMTGG-QPHPGTGKTL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 206 PGYEKVLDTVKDALGntpfvgkpmyevlhavkkgikdavapqamfedLGIKYVGPVDGHDVPAVEAALRAAKNFGGP-VI 284
Cdd:cd02008 125 TEPTTVIDIEALVRA--------------------------------IGVKRVVVVDPYDLKAIREELKEALAVPGVsVI 172
|
..
gi 1033141171 285 VH 286
Cdd:cd02008 173 IA 174
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
133-303 |
2.04e-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: 49.80 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 133 ADGLAKAYALRGEKRSVVAVVGDGALTGGMCWEALNNIATAGNPLVIVVNDNGRSYSptiggladhlsslrlnpgyekvl 212
Cdd:cd02000 113 AAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCENNGYAIS----------------------- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 213 dtvkdalgnTPFvgKPMYEVLHAVKKGIKdavapqamfedLGIKYVgPVDGHDVPAVEAALRAAKNF----GGPVIVHAV 288
Cdd:cd02000 170 ---------TPT--SRQTAGTSIADRAAA-----------YGIPGI-RVDGNDVLAVYEAAKEAVERaragGGPTLIEAV 226
|
170 180
....*....|....*....|....*..
gi 1033141171 289 TrkgY------------GYRPAEDDEA 303
Cdd:cd02000 227 T---YrlgghstsddpsRYRTKEEVEE 250
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
129-289 |
3.92e-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: 47.25 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 129 ALSYADGLAKAYALRGEKRSVVAVVGDGALtgGMCWEALNNIATAGNPLVIVVNDNGRsysptiggladhLSSLRLNPGY 208
Cdd:cd00568 47 AMGYGLPAAIGAALAAPDRPVVCIAGDGGF--MMTGQELATAVRYGLPVIVVVFNNGG------------YGTIRMHQEA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 209 EKVLDTVKDALGNTPFVgkpmyevlhavkkgikdavapqAMFEDLGIKYVGPVdghDVPAVEAALRAAKNFGGPVIVHAV 288
Cdd:cd00568 113 FYGGRVSGTDLSNPDFA----------------------ALAEAYGAKGVRVE---DPEDLEAALAEALAAGGPALIEVK 167
|
.
gi 1033141171 289 T 289
Cdd:cd00568 168 T 168
|
|
| PFOR_II |
pfam17147 |
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ... |
510-575 |
5.30e-05 |
|
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic enzyme pyruvate:ferredoxin oxidoreductase and is necessary for inter subunit contacts in conjunction with domains I and IV.
Pssm-ID: 407280 [Multi-domain] Cd Length: 102 Bit Score: 42.63 E-value: 5.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033141171 510 DVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVP-AELVELASAHRLVVTVEDGVRIGGVG 575
Cdd:pfam17147 2 EVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPeEELKELLAGVKKVVVLDRNISFGSPG 68
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
361-584 |
6.55e-04 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 42.42 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 361 LARKYPE-RVYDVGIAEQHAATSAAGLAMGGLHPVV-AVYATFLNRAFDQVLLDVAM--------HKLPVTfvldragIT 430
Cdd:CHL00144 44 LHEKYGDlRVLDTPIAENSFTGMAIGAAMTGLRPIVeGMNMGFLLLAFNQISNNAGMlhytsggnFTIPIV-------IR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 431 GPDG------PSHYGIWDmSVFGVVPGLRIAAPRDSATLREELREAIaVDDGPTIL--RFPTGTVAADLPAVRRVGPVDV 502
Cdd:CHL00144 117 GPGGvgrqlgAEHSQRLE-SYFQSVPGLQIVACSTPYNAKGLLKSAI-RSNNPVIFfeHVLLYNLKEEIPDNEYLLPLEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 503 lAESAR--TDVLLVAVGSFAGLGVEVAARVAEQGYGVTVVDPRWVRPVPAELV--ELASAHRlVVTVEDGVRIGGVGSAL 578
Cdd:CHL00144 195 -AEVVRpgNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTIskSVKKTHK-VLIVEECMKTGGIGAEL 272
|
....*.
gi 1033141171 579 AQAMRD 584
Cdd:CHL00144 273 IAQINE 278
|
|
| PLN02790 |
PLN02790 |
transketolase |
365-540 |
3.18e-03 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 40.77 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 365 YPERVYDVGIAEQHAATSAAGLAM--GGLHPVVAVYATFLNRAFDQVLLDvAMHKLPVTFVL--DRAGItGPDGPSHYGI 440
Cdd:PLN02790 390 PEERNVRFGVREHGMGAICNGIALhsSGLIPYCATFFVFTDYMRAAMRLS-ALSEAGVIYVMthDSIGL-GEDGPTHQPI 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033141171 441 WDMSVFGVVPGLRIAAPRDSATLREELREAIAVDDGPTILRFPTGTVAAdLPAVRRVGP------VDVLAESARTDVLLV 514
Cdd:PLN02790 468 EHLASLRAMPNILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPN-LPGTSIEGVekggyvISDNSSGNKPDLILI 546
|
170 180
....*....|....*....|....*.
gi 1033141171 515 AVGSFAGLGVEVAARVAEQGYGVTVV 540
Cdd:PLN02790 547 GTGSELEIAAKAAKELRKEGKKVRVV 572
|
|
| |
