|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
7-620 |
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: 1164.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 7 KYPTLALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHK 86
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 87 ILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNH 166
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 167 AGDIKPDMLVVLNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGVP----PIKELLKRTEEHIKGMVVPGTL 242
Cdd:COG1154 161 AGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPgigpPLYELARRAKEGLKGLVVPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 243 FEEMGFNYIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVLPKSSGGLPSYS 322
Cdd:COG1154 241 FEELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSYT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 323 KIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQ 402
Cdd:COG1154 321 DVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 403 VIHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYnDGPSTVRYPRGTGT 482
Cdd:COG1154 401 VIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIRYPRGNGP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 483 GAEL-EPLAPLPLGKGVVKRNGEKLAILNFGTLMPEAAQVAEKL-----NATLVDMRFVKPLDEALILQLAADHEVLVTL 556
Cdd:COG1154 480 GVELpAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLaaegiSATVVDARFVKPLDEELILELAREHDLVVTV 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578230400 557 EENAIMGGAGSGVNELLMAHRRAVPVLNIGLPDFFIPQGTQEEVRADLGLDAAGIEAKIRDWLA 620
Cdd:COG1154 560 EEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-619 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 1107.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 5 IAKYPTLALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYP 84
Cdd:PRK05444 1 IPKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 85 HKILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQ-RRTVCVIGDGAITAGMAFEA 163
Cdd:PRK05444 81 HKILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGEdRKVVAVIGDGALTGGMAFEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 164 MNHAGDIKPDMLVVLNDNEMSISENVGALNNHLAQLLSGklysslreggkkvfsgvppikellkrteehikgmvvpgTLF 243
Cdd:PRK05444 161 LNNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRSS--------------------------------------TLF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 244 EEMGFNYIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVLPKSSG-GLPSYS 322
Cdd:PRK05444 203 EELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKSSKpGKPSYT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 323 KIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQ 402
Cdd:PRK05444 283 KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 403 VIHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTVRYPRGTGT 482
Cdd:PRK05444 363 VIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNGV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 483 GAELEPLAPLPLGKGVVKRNGEKLAILNFGTLMPEAAQVAEKLN-ATLVDMRFVKPLDEALILQLAADHEVLVTLEENAI 561
Cdd:PRK05444 443 GVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLAsATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAI 522
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 578230400 562 MGGAGSGVNELLMAHRRAVPVLNIGLPDFFIPQGTQEEVRADLGLDAAGIEAKIRDWL 619
Cdd:PRK05444 523 MGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
11-620 |
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: 1084.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 11 LALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTG 90
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 91 RRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAGDI 170
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 171 KPDMLVVLNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGVPPIKE-LLKRTEEHIKGMVVPGTLFEEMGFN 249
Cdd:TIGR00204 161 KTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNyLAKRTEESMKGLVVPGTFFEELGFN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 250 YIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVLPKSSGGLPSYSKIFGDWL 329
Cdd:TIGR00204 241 YIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSALPSYSKIFSDTL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 330 CETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQVIHDVAI 409
Cdd:TIGR00204 321 CELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVCI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 410 QKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTVRYPRGTGTGAELEPL 489
Cdd:TIGR00204 401 QKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVGVELTPE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 490 A-PLPLGKGVVKRNGEKLAILNFGTLMPEAAQVAEKLN-----ATLVDMRFVKPLDEALILQLAADHEVLVTLEENAIMG 563
Cdd:TIGR00204 481 PeKLPIGKSEVLRKGEKILILGFGTLVPEALEVAESLNekgieATVVDARFVKPLDEELILEIAASHEKLVTVEENAIMG 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 578230400 564 GAGSGVNELLMAHRRAVPVLNIGLPDFFIPQGTQEEVRADLGLDAAGIEAKIRDWLA 620
Cdd:TIGR00204 561 GAGSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
11-282 |
5.90e-178 |
|
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: 504.63 E-value: 5.90e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 11 LALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTG 90
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 91 RRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAGDI 170
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 171 KPDMLVVLNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGV--PPIKELLKRTEEHIKGMVVPGTLFEEMGF 248
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLKPKigPPLYELARRAKESLKGLVVPGTLFEELGF 240
|
250 260 270
....*....|....*....|....*....|....
gi 578230400 249 NYIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMT 282
Cdd:pfam13292 241 KYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
47-288 |
1.42e-118 |
|
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: 350.31 E-value: 1.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 47 SGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTS 126
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 127 ISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAGDIKPDMLVVLNDNEMSISENVGalnnhlaqllsgklys 206
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 207 slreggkkvfsgvppikellkrteehikgmvVPGTLFEEMGFNYIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMTKKGR 286
Cdd:cd02007 145 -------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKGK 193
|
..
gi 578230400 287 GY 288
Cdd:cd02007 194 GY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
364-483 |
4.13e-46 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 159.19 E-value: 4.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 364 FDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQVIHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCI 443
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 578230400 444 PEMVIMTPSDENECRQMLYTGYHYnDGPSTVRYPRGTGTG 483
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIRD-DGPVVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
7-620 |
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: 1164.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 7 KYPTLALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHK 86
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 87 ILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNH 166
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 167 AGDIKPDMLVVLNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGVP----PIKELLKRTEEHIKGMVVPGTL 242
Cdd:COG1154 161 AGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPgigpPLYELARRAKEGLKGLVVPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 243 FEEMGFNYIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVLPKSSGGLPSYS 322
Cdd:COG1154 241 FEELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSYT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 323 KIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQ 402
Cdd:COG1154 321 DVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 403 VIHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYnDGPSTVRYPRGTGT 482
Cdd:COG1154 401 VIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIRYPRGNGP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 483 GAEL-EPLAPLPLGKGVVKRNGEKLAILNFGTLMPEAAQVAEKL-----NATLVDMRFVKPLDEALILQLAADHEVLVTL 556
Cdd:COG1154 480 GVELpAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLaaegiSATVVDARFVKPLDEELILELAREHDLVVTV 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578230400 557 EENAIMGGAGSGVNELLMAHRRAVPVLNIGLPDFFIPQGTQEEVRADLGLDAAGIEAKIRDWLA 620
Cdd:COG1154 560 EEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-619 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 1107.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 5 IAKYPTLALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYP 84
Cdd:PRK05444 1 IPKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 85 HKILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQ-RRTVCVIGDGAITAGMAFEA 163
Cdd:PRK05444 81 HKILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGEdRKVVAVIGDGALTGGMAFEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 164 MNHAGDIKPDMLVVLNDNEMSISENVGALNNHLAQLLSGklysslreggkkvfsgvppikellkrteehikgmvvpgTLF 243
Cdd:PRK05444 161 LNNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRSS--------------------------------------TLF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 244 EEMGFNYIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVLPKSSG-GLPSYS 322
Cdd:PRK05444 203 EELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKSSKpGKPSYT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 323 KIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQ 402
Cdd:PRK05444 283 KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 403 VIHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTVRYPRGTGT 482
Cdd:PRK05444 363 VIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNGV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 483 GAELEPLAPLPLGKGVVKRNGEKLAILNFGTLMPEAAQVAEKLN-ATLVDMRFVKPLDEALILQLAADHEVLVTLEENAI 561
Cdd:PRK05444 443 GVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLAsATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAI 522
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 578230400 562 MGGAGSGVNELLMAHRRAVPVLNIGLPDFFIPQGTQEEVRADLGLDAAGIEAKIRDWL 619
Cdd:PRK05444 523 MGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
11-620 |
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: 1084.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 11 LALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTG 90
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 91 RRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAGDI 170
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 171 KPDMLVVLNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGVPPIKE-LLKRTEEHIKGMVVPGTLFEEMGFN 249
Cdd:TIGR00204 161 KTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNyLAKRTEESMKGLVVPGTFFEELGFN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 250 YIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVLPKSSGGLPSYSKIFGDWL 329
Cdd:TIGR00204 241 YIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSALPSYSKIFSDTL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 330 CETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQVIHDVAI 409
Cdd:TIGR00204 321 CELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVCI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 410 QKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTVRYPRGTGTGAELEPL 489
Cdd:TIGR00204 401 QKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVGVELTPE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 490 A-PLPLGKGVVKRNGEKLAILNFGTLMPEAAQVAEKLN-----ATLVDMRFVKPLDEALILQLAADHEVLVTLEENAIMG 563
Cdd:TIGR00204 481 PeKLPIGKSEVLRKGEKILILGFGTLVPEALEVAESLNekgieATVVDARFVKPLDEELILEIAASHEKLVTVEENAIMG 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 578230400 564 GAGSGVNELLMAHRRAVPVLNIGLPDFFIPQGTQEEVRADLGLDAAGIEAKIRDWLA 620
Cdd:TIGR00204 561 GAGSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
7-620 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 744.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 7 KYPTLALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHK 86
Cdd:PRK12571 5 KTPLLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCYPHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 87 ILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNH 166
Cdd:PRK12571 85 ILTGRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYEALNN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 167 AGDIKPDMLVVLNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGVP-PIKELLKRTEEHIKGMVVPGTLFEE 245
Cdd:PRK12571 165 AGAADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIAKGVEERLPgPLRDGARRARELVTGMIGGGTLFEE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 246 MGFNYIGPVDGHDVLGLVNTLKNMRDLK-GPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVLPKSSGGLPSYSKI 324
Cdd:PRK12571 245 LGFTYVGPIDGHDMEALLSVLRAARARAdGPVLVHVVTEKGRGYAPAEADEDKYHAVGKFDVVTGLQKKSAPSAPSYTSV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 325 FGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQVI 404
Cdd:PRK12571 325 FGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQRGYDQLL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 405 HDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTVRYPRGTGTGA 484
Cdd:PRK12571 405 HDVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVGV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 485 ELEPLA-PLPLGKGVVKRNGEKLAILNFGTLMPEAAQVAEKLNA-----TLVDMRFVKPLDEALILQLAADHEVLVTLEE 558
Cdd:PRK12571 485 EIPAEGtILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAegisvTVADPRFVKPLDEALTDLLVRHHIVVIVEEQ 564
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578230400 559 NAiMGGAGSGVNELLMAHRRA---VPVLNIGLPDFFIPQGTQEEVRADLGLDAAGIEAKIRDWLA 620
Cdd:PRK12571 565 GA-MGGFGAHVLHHLADTGLLdggLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALA 628
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
9-615 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 590.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 9 PTLALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKIL 88
Cdd:PLN02582 32 PLLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQSYPHKIL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 89 TGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAG 168
Cdd:PLN02582 112 TGRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 169 DIKPDMLVVLNDN-EMSI--------SENVGALNNHLAQLLSGKLYSSLREGGKKVFSGVP-PIKELLKRTEEHIKGMVV 238
Cdd:PLN02582 192 YLDSDMIVILNDNkQVSLptatldgpAPPVGALSSALSRLQSSRPLRELREVAKGVTKQIGgPMHELAAKVDEYARGMIS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 239 -PG-TLFEEMGFNYIGPVDGHDVLGLVNTLKNMRDLK--GPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVLPKS 314
Cdd:PLN02582 272 gSGsTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKttGPVLIHVVTEKGRGYPYAERAADKYHGVVKFDPATGKQFKV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 315 SGGLPSYSKIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYST 394
Cdd:PLN02582 352 KAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 395 FLQRAYDQVIHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTV 474
Cdd:PLN02582 432 FLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIDDRPSCF 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 475 RYPRGTGTGAELEPL---APLPLGKGVVKRNGEKLAILNFGTLMPE---AAQVAEK--LNATLVDMRFVKPLDEALILQL 546
Cdd:PLN02582 512 RYPRGNGIGVQLPPNnkgIPIEVGKGRILLEGERVALLGYGTAVQSclaAASLLERhgLSATVADARFCKPLDRALIRSL 591
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578230400 547 AADHEVLVTLEENAImGGAGSGV------NELLMAHRRAVPVLnigLPDFFIPQGTQEEVRADLGLDAAGIEAKI 615
Cdd:PLN02582 592 AKSHEVLITVEEGSI-GGFGSHVaqfmalDGLLDGKLKWRPLV---LPDRYIDHGAPADQLAEAGLTPSHIAATV 662
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
11-282 |
5.90e-178 |
|
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: 504.63 E-value: 5.90e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 11 LALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTG 90
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 91 RRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAGDI 170
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 171 KPDMLVVLNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGV--PPIKELLKRTEEHIKGMVVPGTLFEEMGF 248
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLKPKigPPLYELARRAKESLKGLVVPGTLFEELGF 240
|
250 260 270
....*....|....*....|....*....|....
gi 578230400 249 NYIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMT 282
Cdd:pfam13292 241 KYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
9-573 |
8.65e-167 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 490.38 E-value: 8.65e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 9 PTLALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKIL 88
Cdd:PLN02234 65 PLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKIL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 89 TGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAG 168
Cdd:PLN02234 145 TGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 169 DIKPDMLVVLNDN-EMSI--------SENVGALNNHLAQLLSGklYSSLREGGKkvfsgvppikellkrteehikgmvvp 239
Cdd:PLN02234 225 YLHSNMIVILNDNkQVSLptanldgpTQPVGALSCALSRLQSN--CGMIRETSS-------------------------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 240 gTLFEEMGFNYIGPVDGHDVLGLVNTLKNMRDLK--GPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVLPKSSGG 317
Cdd:PLN02234 277 -TLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQFKNISK 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 318 LPSYSKIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQ 397
Cdd:PLN02234 356 TQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQ 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 398 RAYDQVIHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTVRYP 477
Cdd:PLN02234 436 RAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYH 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 478 RGTGTGAELEP---LAPLPLGKGVVKRNGEKLAILNFGT----LMPEAAQVAEK-LNATLVDMRFVKPLDEALILQLAAD 549
Cdd:PLN02234 516 RGNGIGVSLPPgnkGVPLQIGRGRILRDGERVALLGYGSavqrCLEAASMLSERgLKITVADARFCKPLDVALIRSLAKS 595
|
570 580
....*....|....*....|....
gi 578230400 550 HEVLVTLEENAImGGAGSGVNELL 573
Cdd:PLN02234 596 HEVLITVEEGSI-GGFGSHVVQFL 618
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
11-606 |
2.86e-153 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 453.69 E-value: 2.86e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 11 LALVDSTQELRLLPKDSLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTG 90
Cdd:PRK12315 3 LEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKMLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 91 RRDkigtirqkGGLHPFPWRG--------ESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFE 162
Cdd:PRK12315 83 RKE--------AFLDPDHYDDvtgytnpeESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 163 AMNHAGDIKPDMLVVLNDNEMSISENVGALNNHLAQLlsgklysslREGGKKVfsgvppikellkrteehikgmvvPGTL 242
Cdd:PRK12315 155 GLNNAAELKSNLIIIVNDNQMSIAENHGGLYKNLKEL---------RDTNGQS-----------------------ENNL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 243 FEEMGFNYIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDHTSGVlPKSSGGLPSYS 322
Cdd:PRK12315 203 FKAMGLDYRYVEDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKGYQPAEENKEAFHWHMPFDLETGQ-SKVPASGESYS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 323 KIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQ 402
Cdd:PRK12315 282 SVTLDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQRAYDQ 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 403 VIHDVAIQKLPVLFAIDRAGIVGADgQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTVRYPrgtGT 482
Cdd:PRK12315 362 LSHDLAINNNPAVMIVFGGSISGND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAIRVP---EH 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 483 GAELEPLAPLPLGK---GVVKRnGEKLAILNFGTLMPEAAQVAEKL------NATLVDMRFVKPLDEALILQLAADHEVL 553
Cdd:PRK12315 438 GVESGPTVDTDYSTlkyEVTKA-GEKVAILALGDFYELGEKVAKKLkeelgiDATLINPKFITGLDEELLEKLKEDHELV 516
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 578230400 554 VTLEENAIMGGAGSGVNELLMAhrRAVPVLNIGLPDFFIPQGTQEEVRADLGL 606
Cdd:PRK12315 517 VTLEDGILDGGFGEKIARYYGN--SDMKVLNYGAKKEFNDRVPVEELYKRNHL 567
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
9-613 |
1.70e-122 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 378.67 E-value: 1.70e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 9 PTLALVDSTQELRLLPKDSLPKLCDELRRYLLDSV-SRSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKI 87
Cdd:PLN02225 77 PILDSIETPLQLKNLSVKELKLLADEIRTELHSVLwKKTQKSMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAHKV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 88 LTGRRDKIGTiRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHA 167
Cdd:PLN02225 157 LTRRWSAIPS-RQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGKRDRVVAVIDNATITAGQAYEAMSNA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 168 GDIKPDMLVVLNDNEMSISEN--------VGALNNHLAQLLSGKLYSSLREGGKKVFSGVPP-IKELLKRTEEHIKGMVV 238
Cdd:PLN02225 236 GYLDSNMIVILNDSRHSLHPNmeegskasISALSSIMSKIQSSKIFRKFRELAKAMTKRIGKgMYEWAAKVDEYARGMVG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 239 P--GTLFEEMGFNYIGPVDGHDVLGLVNTLKNMRDLK--GPQFLHIMTKKGRGYEPAEKdpitfhavpkfdhtsgVLPKS 314
Cdd:PLN02225 316 PtgSTLFEELGLYYIGPVDGHNIEDLVCVLREVSSLDsmGPVLVHVITEENRDAETGKN----------------IMVKD 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 315 SgglPSYSKIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYST 394
Cdd:PLN02225 380 R---RTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 395 FLQRAYDQVIHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTV 474
Cdd:PLN02225 457 FLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDRPVCF 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 475 RYPRGTGTGAE-LEPLA-PLPLGKGVVKRNGEKLAILNFGTLMP---EAAQVAEK--LNATLVDMRFVKPLDEALILQLA 547
Cdd:PLN02225 537 RFPRGSIVNMNyLVPTGlPIEIGRGRVLVEGQDVALLGYGAMVQnclHAHSLLSKlgLNVTVADARFCKPLDIKLVRDLC 616
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578230400 548 ADHEVLVTLEENAImGGAGSGVNELLMAHRRA---VPVLNIGLPDFFIPQGTQEEVRADLGLDAAGIEA 613
Cdd:PLN02225 617 QNHKFLITVEEGCV-GGFGSHVAQFIALDGQLdgnIKWRPIVLPDGYIEEASPREQLALAGLTGHHIAA 684
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
47-288 |
1.42e-118 |
|
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: 350.31 E-value: 1.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 47 SGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTS 126
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 127 ISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAGDIKPDMLVVLNDNEMSISENVGalnnhlaqllsgklys 206
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 207 slreggkkvfsgvppikellkrteehikgmvVPGTLFEEMGFNYIGPVDGHDVLGLVNTLKNMRDLKGPQFLHIMTKKGR 286
Cdd:cd02007 145 -------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKGK 193
|
..
gi 578230400 287 GY 288
Cdd:cd02007 194 GY 195
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
323-619 |
1.49e-76 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 246.15 E-value: 1.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 323 KIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFL-QRAYD 401
Cdd:COG3958 8 DAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLtGRAYE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 402 QVIHDVAIQKLPV-LFAIDrAGI-VGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYnDGPSTVRYPRG 479
Cdd:COG3958 88 QIRNDIAYPNLNVkIVGSH-AGLsYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEH-DGPVYLRLGRG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 480 tGTGAELEPLAPLPLGKGVVKRNGEKLAILNFGTLMPEAAQVAEKL-----NATLVDMRFVKPLDEALILQLAADHEVLV 554
Cdd:COG3958 166 -AVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLakegiSARVINMHTIKPLDEEAILKAARKTGAVV 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578230400 555 TLEENAIMGGAGSGVNELLmAHRRAVPVLNIGLPDFFIPQGTQEEVRADLGLDAAGIEAKIRDWL 619
Cdd:COG3958 245 TAEEHSIIGGLGSAVAEVL-AENYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
323-478 |
1.34e-72 |
|
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: 230.02 E-value: 1.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 323 KIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQ 402
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578230400 403 VIHDVAIQKLPVLFAIDRAGI-VGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYnDGPSTVRYPR 478
Cdd:cd07033 81 IRHDVALQNLPVKFVGTHAGIsVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEY-DGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
319-479 |
4.29e-50 |
|
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: 171.19 E-value: 4.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 319 PSYSKIFGDWLCETAAKDDKLMAVTPAMREGSGMVEFSKKFPD---RYFDVAIAEQHAVTFAAGMAIGG--YKPIVAIYS 393
Cdd:pfam02779 3 IATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEATFS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 394 TFLQRAYDQVIHDVAIQKLPVLFAIDRAGI-VGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYND-GP 471
Cdd:pfam02779 83 DFLNRADDAIRHGAALGKLPVPFVVTRDPIgVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGrKP 162
|
....*...
gi 578230400 472 STVRYPRG 479
Cdd:pfam02779 163 VVLRLPRQ 170
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
364-483 |
4.13e-46 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 159.19 E-value: 4.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 364 FDVAIAEQHAVTFAAGMAIGGYKPIVAIYSTFLQRAYDQVIHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCI 443
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 578230400 444 PEMVIMTPSDENECRQMLYTGYHYnDGPSTVRYPRGTGTG 483
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIRD-DGPVVIRLERKSLYR 136
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
323-478 |
1.42e-45 |
|
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: 158.66 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 323 KIFGDWLCETAakddKLMAVTPAMREGSGMVEFSKKFPDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIY-STFLQRAYD 401
Cdd:cd06586 1 AAFAEVLTAWG----VRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTsGTGLLNAIN 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578230400 402 QVIhDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYND--GPSTVRYPR 478
Cdd:cd06586 77 GLA-DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAsqGPVVVRLPR 154
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
495-611 |
1.19e-30 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 116.16 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 495 GKGVVKRNGEKLAILNFGTLMPEAAQVAEKL-----NATLVDMRFVKPLDEALILQLAADHEVLVTLEENAIMGGAGSGV 569
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLakegiSAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 578230400 570 NELLMAHRRA---VPVLNIGLPDfFIPQGTQEEVRADLGLDAAGI 611
Cdd:pfam02780 81 AAALAEEAFDgldAPVLRVGGPD-FPEPGSADELEKLYGLTPEKI 124
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
127-619 |
1.30e-24 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 108.30 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 127 ISAGIGVAIAAEKEGKQR----------RTVCVIGDGAITAGMAFEAMNHAGDIKPDMLVVL-NDNEMSISENVgalnnh 195
Cdd:PRK05899 124 LANAVGMALAEKYLAALFnrpgldivdhYTYVLCGDGDLMEGISHEACSLAGHLKLGNLIVIyDDNRISIDGPT------ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 196 laqllsgklysslreggKKVFSgvppikellkrteEHIKGMvvpgtlFEEMGFNYIgPVDGHDVLGLVNTLKNMRDLKGP 275
Cdd:PRK05899 198 -----------------EGWFT-------------EDVKKR------FEAYGWHVI-EVDGHDVEAIDAAIEEAKASTKP 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 276 QFLHIMTKKGRGyepaekdpitfhaVPKFDHTSGV----LP-------KSSGGLPsYSKIFGDWLCETAAKDDKLMA--- 341
Cdd:PRK05899 241 TLIIAKTIIGKG-------------APNKEGTHKVhgapLGaeeiaaaKKELGWD-YRKASGKALNALAKALPELVGgsa 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 342 -VTPA-MREGSGMVEFSKK-FPDRYFDVAIAEQHAVTFAAGMAI-GGYKPIVAIYSTFLQRAYDQvIHDVAIQKLPVLFA 417
Cdd:PRK05899 307 dLAGSnNTKIKGSKDFAPEdYSGRYIHYGVREFAMAAIANGLALhGGFIPFGGTFLVFSDYARNA-IRLAALMKLPVIYV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 418 IDRAGI-VGADGQTHQGAFDLSFLRCIPEMVIMTPSDENEC----RQMLytgyHYNDGPSTVRYPR-GTGTGAELEPLAP 491
Cdd:PRK05899 386 FTHDSIgVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETaaawKYAL----ERKDGPSALVLTRqNLPVLERTAQEEG 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 492 LPLGKGVVKRNGEkLAILNFGTLMPEAAQVAEKL-----NATLVDMRFVKPLDEalilQLAADHE-VLVTLEENAIMGGA 565
Cdd:PRK05899 462 VAKGGYVLRDDPD-VILIATGSEVHLALEAADELeaegiKVRVVSMPSTELFDE----QDAAYKEsVLPAAVTARVAVEA 536
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 578230400 566 GSGvnellMAHRRAV--PVLNIGLPDFFIpQGTQEEVRADLGLDAAGIEAKIRDWL 619
Cdd:PRK05899 537 GVA-----DGWYKYVglDGKVLGIDTFGA-SAPADELFKEFGFTVENIVAAAKELL 586
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
355-620 |
4.54e-19 |
|
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 439793 [Multi-domain] Cd Length: 325 Bit Score: 88.53 E-value: 4.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 355 FSKKF-PDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAI-YSTFLQRAYDQVIHDVA--------IQKLPVLF-AIDRAGI 423
Cdd:COG0022 44 LQEKFgPDRVFDTPISEAGIVGAAIGAALAGLRPVVEIqFADFIYPAFDQIVNQAAklrymsggQFKVPMVIrTPYGGGI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 424 vGAdGQTHQGAFDlSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDgP-----STVRYPRgtgTGAELEPLAPLPLGKGV 498
Cdd:COG0022 124 -GA-GAQHSQSLE-AWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDD-PvifleHKRLYRL---KGEVPEEDYTVPLGKAR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 499 VKRNGEKLAILNFGTLMPEAAQVAEKL-----NATLVDMRFVKPLDEALILQLAADHEVLVTLEENAIMGGAGSG----V 569
Cdd:COG0022 197 VVREGTDVTIVTYGAMVHRALEAAEELaeegiSAEVIDLRTLSPLDEETILESVKKTGRLVVVDEAPRTGGFGAEiaarI 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 578230400 570 NELLMAHRRAvPVLNIGLPDFFIPQGTQEEvRADLgLDAAGIEAKIRDWLA 620
Cdd:COG0022 277 AEEAFDYLDA-PVKRVTGPDTPIPYAPALE-KAYL-PSADRIVAAVRELLA 324
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
353-567 |
6.94e-18 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 85.42 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 353 VEFSKKF-PDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAI-YSTFLQRAYDQVIHDVA--------IQKLPVLFaidRA- 421
Cdd:PTZ00182 73 KGLLDKYgPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFmFADFIFPAFDQIVNEAAkyrymsggQFDCPIVI---RGp 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 422 -GIVGADGQTHQGAFDlSFLRCIPEMVIMTPSDENECRQMLYTGYHyNDGPSTVRYPRGTGTGAELEPLAP---LPLGKG 497
Cdd:PTZ00182 150 nGAVGHGGAYHSQSFE-AYFAHVPGLKVVAPSDPEDAKGLLKAAIR-DPNPVVFFEPKLLYRESVEVVPEAdytLPLGKA 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578230400 498 VVKRNGEKLAILNFGT---LMPEAAQVAEK--LNATLVDMRFVKPLDEALILQLAADHEVLVTLEENAIMGGAGS 567
Cdd:PTZ00182 228 KVVREGKDVTIVGYGSqvhVALKAAEELAKegISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGA 302
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
351-576 |
2.76e-14 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 74.37 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 351 GMVEfskKF-PDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYS-TFLQRAYDQVIHDVAIQ--------KLPVLF--AI 418
Cdd:PRK09212 43 GLLE---QFgPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFMTfNFSMQAIDQIVNSAAKTnymsggqlKCPIVFrgPN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 419 DRAGIVGADgqtHQGAFDlSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTVRYPRGTGTGAEL-EPLAPLPLGKG 497
Cdd:PRK09212 120 GAAARVAAQ---HSQCYA-AWYSHIPGLKVVAPYFAADCKGLLKTAIRDPNPVIFLENEILYGHSHEVpEEEESIPIGKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 498 VVKRNGEKLAILNFGTLMPEAAQVAEKL-----NATLVDMRFVKPLDEALILQLAADHEVLVTLEENAIMGGAGSGVNEL 572
Cdd:PRK09212 196 AILREGSDVTIVTFSIQVKLALEAAELLekegiSVEVIDLRTLRPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAAL 275
|
....
gi 578230400 573 LMAH 576
Cdd:PRK09212 276 IMKE 279
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
33-303 |
3.05e-14 |
|
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: 72.92 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 33 DELRRYLLDSVSRS-SGHFASGLGTVELTVAL---HYVYNtPF-------DRLIWDVGHQA---YPHKILTG--RRDKIG 96
Cdd:cd02012 1 NRIRRLSIDMVQKAgSGHPGGSLSAADILAVLyfkVLKYD-PAdpkwpnrDRFVLSKGHASpalYAVLALAGylPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 97 TIRQKGGL---HPfpwrgesEYDVLSVGHSSTS-----ISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAG 168
Cdd:cd02012 80 TFRQLGSRlpgHP-------EYGLTPGVEVTTGslgqgLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 169 DIKPDMLVVLND-NEMSISENVGALNNhlaqllsgklysslreggkkvfsgVPPIKellKRteehikgmvvpgtlFEEMG 247
Cdd:cd02012 153 HYKLDNLIAIVDsNRIQIDGPTDDILF------------------------TEDLA---KK--------------FEAFG 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 578230400 248 FNYIgPVDGHDVLGLVNTLKNMRDLKG-PQFLHIMTKKGRGYEPAEKDPITFHAVPK 303
Cdd:cd02012 192 WNVI-EVDGHDVEEILAALEEAKKSKGkPTLIIAKTIKGKGVPFMENTAKWHGKPLG 247
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
329-574 |
4.74e-10 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 61.76 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 329 LCETAAKDDKLMAVTPAMREGSGMVEFSK----KF-PDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAIYS-TFLQRAYDQ 402
Cdd:PLN02683 37 LDEEMSADPKVFIMGEEVGEYQGAYKITKgllqKYgPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTfNFSMQAIDH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 403 VIHDVAIQ--------KLPVLFAIDRAGIVGADGQtHQGAFdLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDgP--- 471
Cdd:PLN02683 117 IINSAAKTnymsagqiSVPIVFRGPNGAAAGVGAQ-HSQCF-AAWYSSVPGLKVLAPYSSEDARGLLKAAIRDPD-Pvvf 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 472 --STVRYPRGTGTGAE-LEPLAPLPLGKGVVKRNGEKLAILNFGTLMPEAAQVAEKL-----NATLVDMRFVKPLDEALI 543
Cdd:PLN02683 194 leNELLYGESFPVSAEvLDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILakegiSAEVINLRSIRPLDRDTI 273
|
250 260 270
....*....|....*....|....*....|.
gi 578230400 544 LQLAADHEVLVTLEENAIMGGAGSGVNELLM 574
Cdd:PLN02683 274 NASVRKTNRLVTVEEGWPQHGVGAEICASVV 304
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
95-282 |
3.15e-09 |
|
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: 56.49 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 95 IGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGVAIAAekegKQRRTVCVIGDGAitAGMAFEAMNHAGDIKPDM 174
Cdd:cd00568 20 AGNSAYWAYRYLPLRRGRRFLTSTGFGAMGYGLPAAIGAALAA----PDRPVVCIAGDGG--FMMTGQELATAVRYGLPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 175 LVVLNDNEMsisenvgalnnhlaqllsgklYSSLREGGKKVFSGVPPIKELlkRTEEHIKgmvvpgtLFEEMGFNYIGPV 254
Cdd:cd00568 94 IVVVFNNGG---------------------YGTIRMHQEAFYGGRVSGTDL--SNPDFAA-------LAEAYGAKGVRVE 143
|
170 180
....*....|....*....|....*...
gi 578230400 255 DGHDvlgLVNTLKNMRDLKGPQFLHIMT 282
Cdd:cd00568 144 DPED---LEAALAEALAAGGPALIEVKT 168
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
355-461 |
9.09e-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: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 355 FSKKF-PDRYFDVAIAEQHAVTFAAGMAIGGYKPIVAI-YSTFLQRAYDQVIHDVA--------IQKLPVLFaidRA--G 422
Cdd:cd07036 37 LLDKFgPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFALPAFDQIVNEAAklrymsggQFKVPIVI---RGpnG 113
|
90 100 110
....*....|....*....|....*....|....*....
gi 578230400 423 IVGADGQTHQGAFDlSFLRCIPEMVIMTPSDENECRQML 461
Cdd:cd07036 114 GGIGGGAQHSQSLE-AWFAHIPGLKVVAPSTPYDAKGLL 151
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
46-456 |
2.72e-06 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 50.44 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 46 SSGHFASGLGTVELTVAL------HYVYNTPF---DRLIWDVGHQA---YPHKILTGRR---DKIGTIRQKGGLHP-FPW 109
Cdd:PTZ00089 25 NSGHPGAPMGMAPIAHILwsevmkYNPKDPRWinrDRFVLSNGHASallYSMLHLTGYDlsmEDLKNFRQLGSRTPgHPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 110 RGESEYDVLSVGHSSTSISAGIGVAIAAE-------KEGKQ---RRTVCVIGDGAITAGMAFEAMNHAGDIKPDMLVVL- 178
Cdd:PTZ00089 105 RHITPGVEVTTGPLGQGIANAVGLAIAEKhlaakfnRPGHPifdNYVYVICGDGCLQEGVSQEALSLAGHLGLEKLIVLy 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 179 NDNEMSISENVgalnnHLAQLLS-GKLYSSLREGGKKVFSGVPPIKELLKRTEE--HIKG---MVVPGTlfeEMGF--NY 250
Cdd:PTZ00089 185 DDNKITIDGNT-----DLSFTEDvEKKYEAYGWHVIEVDNGNTDFDGLRKAIEEakKSKGkpkLIIVKT---TIGYgsSK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 251 IGPVDGHDVLGLVNTLKNMRDLKG--PQ------------FLHIMTKKGRGYE-------------PAEKDpiTFHAVPK 303
Cdd:PTZ00089 257 AGTEKVHGAPLGDEDIAQVKELFGldPEkkfhvseevrqfFEQHVEKKKENYEawkkrfakytaafPKEAQ--AIERRFK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 304 FDHTSGVLPKSSGGLPSYSKIFGDWLCETAAkdDKLMAVTPAMREGS------------GMVEFSKKFPD-RYFDVAIAE 370
Cdd:PTZ00089 335 GELPPGWEKKLPKYTTNDKAIATRKASENVL--NPLFQILPELIGGSadltpsnltrpkEANDFTKASPEgRYIRFGVRE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 371 QHAVTFAAGM-AIGGYKPIVAIYSTFLQRAYDQViHDVAIQKLPVLFAIDRAGI-VGADGQTHQGAFDLSFLRCIPEMVI 448
Cdd:PTZ00089 413 HAMCAIMNGIaAHGGFIPFGATFLNFYGYALGAV-RLAALSHHPVIYVATHDSIgLGEDGPTHQPVETLALLRATPNLLV 491
|
....*...
gi 578230400 449 MTPSDENE 456
Cdd:PTZ00089 492 IRPADGTE 499
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
125-186 |
5.46e-04 |
|
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: 42.48 E-value: 5.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578230400 125 TSISAGIGVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAGDIKPDMLVVLNDNEMSIS 186
Cdd:cd02000 108 GQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCENNGYAIS 169
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
132-186 |
6.44e-04 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 42.44 E-value: 6.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 578230400 132 GVAIAAEKEGKQRRTVCVIGDGAITAGMAFEAMNHAGDIKPDMLVVLNDNEMSIS 186
Cdd:COG1071 138 GAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENNGYAIS 192
|
|
| PLN02790 |
PLN02790 |
transketolase |
355-535 |
7.35e-04 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 42.70 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 355 FSKKFP-DRYFDVAIAEQHAVTFAAGMAI--GGYKPIVAiysTFLQRAyDQVIHDV---AIQKLPVLFAIDRAGI-VGAD 427
Cdd:PLN02790 385 FQKDTPeERNVRFGVREHGMGAICNGIALhsSGLIPYCA---TFFVFT-DYMRAAMrlsALSEAGVIYVMTHDSIgLGED 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578230400 428 GQTHQGAFDLSFLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSTVRYPRGT-----GTGAELeplaplpLGKG--VVK 500
Cdd:PLN02790 461 GPTHQPIEHLASLRAMPNILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKvpnlpGTSIEG-------VEKGgyVIS 533
|
170 180 190
....*....|....*....|....*....|....*....
gi 578230400 501 RNGEK----LAILNFGTLMPEAAQVAEKLNATLVDMRFV 535
Cdd:PLN02790 534 DNSSGnkpdLILIGTGSELEIAAKAAKELRKEGKKVRVV 572
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
130-182 |
1.31e-03 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 39.49 E-value: 1.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 578230400 130 GIGVAIAAEKEGKQRRTVCVIGDGAItaGMAFEAMNHAGDIKPDMLVVLNDNE 182
Cdd:pfam02775 33 GLPAAIGAKLARPDRPVVAIAGDGGF--QMNLQELATAVRYNLPITVVVLNNG 83
|
|
| |
