|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
1-641 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 1295.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 1 MSYQTQINKFSQMALSVFAFPSYINRNPSLKYLKPSSMSSTKYSKVRATTFSEKGEYYSNRPPTPLLDTINHPMHMKNLS 80
Cdd:PLN02234 1 MSYQTQINKFSQMALSVFAFPSYINRNPSLKYLKPSSMSSTKYSKVRATTFSEKGEYYSNRPPTPLLDTINHPMHMKNLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 81 IKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTGRRGKMKTIRQTNGL 160
Cdd:PLN02234 81 IKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTGRRGKMKTIRQTNGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 161 SGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQV 240
Cdd:PLN02234 161 SGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 241 SLPTANLDGPTQPVGALSCALSRLQSNCGMIRETSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKTIGPVLIHVVT 320
Cdd:PLN02234 241 SLPTANLDGPTQPVGALSCALSRLQSNCGMIRETSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKTIGPVLIHVVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 321 EKGRGYPYAERADDKYHGVLKFDPETGKQFKNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTR 400
Cdd:PLN02234 321 EKGRGYPYAERADDKYHGVLKFDPETGKQFKNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 401 CFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMAC 480
Cdd:PLN02234 401 CFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMAC 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 481 LPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCL 560
Cdd:PLN02234 481 LPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 561 EAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKVYRTWITNGST 640
Cdd:PLN02234 561 EAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKVYRTWITNGST 640
|
.
gi 186510290 641 S 641
Cdd:PLN02234 641 S 641
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
63-624 |
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: 944.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 63 PTPLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHK 142
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 143 ILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNN 222
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 223 AGYLHSNMIVILNDNKqVSLptanldgpTQPVGALSCALSRLQSN--------------------CGMIRE--------- 273
Cdd:COG1154 161 AGHLKKDLIVILNDNE-MSI--------SPNVGALSNYLARLRTSptynklreevkkllkklpgiGPPLYElarrakegl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 274 ----TSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQ 349
Cdd:COG1154 232 kglvVPGTLFEELGFKYIGPIDGHDLDALVETLRNAKDLK--GPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 350 FKNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTI 429
Cdd:COG1154 310 KKSKSSAPSYTDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 430 YSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIdDRP 509
Cdd:COG1154 390 YSTFLQRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 510 SCFRYHRGNGIGVSLPPgnKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALI 589
Cdd:COG1154 469 TAIRYPRGNGPGVELPA--ELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELI 546
|
570 580 590
....*....|....*....|....*....|....*.
gi 186510290 590 RSLAKSHEVLITVEEGSI-GGFGSHVVQFLALDGLL 624
Cdd:COG1154 547 LELAREHDLVVTVEEGVLaGGFGSAVLEFLADAGLD 582
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
67-624 |
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: 686.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 67 LDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTG 146
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 147 RRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYL 226
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 227 HSNMIVILNDNkQVSLPTanldgptqPVGALSCALSRLQSNCGM--IRE----------------------------TSS 276
Cdd:TIGR00204 161 KTDMIVILNDN-EMSISE--------NVGALSNHLAQLRSGSLYqsLRDglkkifsklppiknylakrteesmkglvVPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 277 TLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQFKNISKT 356
Cdd:TIGR00204 232 TFFEELGFNYIGPVDGHDLLELIETLKNAKKLK--GPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSAL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 357 QSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQR 436
Cdd:TIGR00204 310 PSYSKIFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 437 AYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHR 516
Cdd:TIGR00204 390 AYDQVVHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 517 GNGIGVSLPPGNKGVPlqIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSH 596
Cdd:TIGR00204 470 GNAVGVELTPEPEKLP--IGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASH 547
|
570 580
....*....|....*....|....*....
gi 186510290 597 EVLITVEEGSI-GGFGSHVVQFLALDGLL 624
Cdd:TIGR00204 548 EKLVTVEENAImGGAGSAVLEFLMDQNKL 576
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
67-320 |
1.32e-143 |
|
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: 417.96 E-value: 1.32e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 67 LDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTG 146
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 147 RRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYL 226
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 227 HSNMIVILNDNkQVSLptanldgpTQPVGALSCALSRLQSNCGM--IRE-----------------------------TS 275
Cdd:pfam13292 161 KKDLIVILNDN-EMSI--------SPNVGALSNYLSRLRTSPTYnrLKEevkkllkpkigpplyelarrakeslkglvVP 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 186510290 276 STLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVT 320
Cdd:pfam13292 232 GTLFEELGFKYIGPIDGHDLDALVKVLENAKDLK--GPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
103-326 |
5.10e-123 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 362.25 E-value: 5.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 103 GGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTT 182
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 183 LSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTanldgptqpVGalscals 262
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPN---------VG------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186510290 263 rlqsncgmireTSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGY 326
Cdd:cd02007 145 -----------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLK--GPVLLHVVTKKGKGY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
402-521 |
2.12e-44 |
|
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: 154.95 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 402 FDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACL 481
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 186510290 482 PNMIVMAPSDEAELFNMVATAAAiDDRPSCFRYHRGNGIG 521
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
1-641 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 1295.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 1 MSYQTQINKFSQMALSVFAFPSYINRNPSLKYLKPSSMSSTKYSKVRATTFSEKGEYYSNRPPTPLLDTINHPMHMKNLS 80
Cdd:PLN02234 1 MSYQTQINKFSQMALSVFAFPSYINRNPSLKYLKPSSMSSTKYSKVRATTFSEKGEYYSNRPPTPLLDTINHPMHMKNLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 81 IKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTGRRGKMKTIRQTNGL 160
Cdd:PLN02234 81 IKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTGRRGKMKTIRQTNGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 161 SGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQV 240
Cdd:PLN02234 161 SGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 241 SLPTANLDGPTQPVGALSCALSRLQSNCGMIRETSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKTIGPVLIHVVT 320
Cdd:PLN02234 241 SLPTANLDGPTQPVGALSCALSRLQSNCGMIRETSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKTIGPVLIHVVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 321 EKGRGYPYAERADDKYHGVLKFDPETGKQFKNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTR 400
Cdd:PLN02234 321 EKGRGYPYAERADDKYHGVLKFDPETGKQFKNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 401 CFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMAC 480
Cdd:PLN02234 401 CFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMAC 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 481 LPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCL 560
Cdd:PLN02234 481 LPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 561 EAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKVYRTWITNGST 640
Cdd:PLN02234 561 EAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKVYRTWITNGST 640
|
.
gi 186510290 641 S 641
Cdd:PLN02234 641 S 641
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
44-629 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 1138.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 44 SKVRAT-TFSEKGEYYSNRPPTPLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYI 122
Cdd:PLN02582 10 SGVCASlSPEESAEYPSQRPPTPLLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 123 FNTPHDKILWDVGHQSYPHKILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSV 202
Cdd:PLN02582 90 FNAPQDKILWDVGHQSYPHKILTGRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKNNV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 203 VSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTANLDGPTQPVGALSCALSRLQSNC-------------- 268
Cdd:PLN02582 170 VAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLPTATLDGPAPPVGALSSALSRLQSSRplrelrevakgvtk 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 269 ------------------GMIRETSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKTIGPVLIHVVTEKGRGYPYAE 330
Cdd:PLN02582 250 qiggpmhelaakvdeyarGMISGSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKTTGPVLIHVVTEKGRGYPYAE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 331 RADDKYHGVLKFDPETGKQFKNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQH 410
Cdd:PLN02582 330 RAADKYHGVVKFDPATGKQFKVKAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQH 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 411 AVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPS 490
Cdd:PLN02582 410 AVTFAAGLACEGLKPFCAIYSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPS 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 491 DEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERG 570
Cdd:PLN02582 490 DEAELFHMVATAAAIDDRPSCFRYPRGNGIGVQLPPNNKGIPIEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHG 569
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 186510290 571 LKITVADARFCKPLDVALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLK 629
Cdd:PLN02582 570 LSATVADARFCKPLDRALIRSLAKSHEVLITVEEGSIGGFGSHVAQFMALDGLLDGKLK 628
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
63-624 |
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: 944.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 63 PTPLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHK 142
Cdd:COG1154 1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 143 ILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNN 222
Cdd:COG1154 81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 223 AGYLHSNMIVILNDNKqVSLptanldgpTQPVGALSCALSRLQSN--------------------CGMIRE--------- 273
Cdd:COG1154 161 AGHLKKDLIVILNDNE-MSI--------SPNVGALSNYLARLRTSptynklreevkkllkklpgiGPPLYElarrakegl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 274 ----TSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQ 349
Cdd:COG1154 232 kglvVPGTLFEELGFKYIGPIDGHDLDALVETLRNAKDLK--GPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 350 FKNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTI 429
Cdd:COG1154 310 KKSKSSAPSYTDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 430 YSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIdDRP 509
Cdd:COG1154 390 YSTFLQRAYDQVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 510 SCFRYHRGNGIGVSLPPgnKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALI 589
Cdd:COG1154 469 TAIRYPRGNGPGVELPA--ELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELI 546
|
570 580 590
....*....|....*....|....*....|....*.
gi 186510290 590 RSLAKSHEVLITVEEGSI-GGFGSHVVQFLALDGLL 624
Cdd:COG1154 547 LELAREHDLVVTVEEGVLaGGFGSAVLEFLADAGLD 582
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
61-619 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 922.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 61 RPPTPLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYP 140
Cdd:PRK05444 1 IPKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 141 HKILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGM-NNSVVSVIGDGAMTAGQAYEA 219
Cdd:PRK05444 81 HKILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGeDRKVVAVIGDGALTGGMAFEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 220 MNNAGYLHSNMIVILNDNkQVSLptanldgpTQPVGALSCALSRLqsncgmireTSSTLFEELGFHYVGPVDGHNIDDLV 299
Cdd:PRK05444 161 LNNAGDLKSDLIVILNDN-EMSI--------SPNVGALSNYLARL---------RSSTLFEELGFNYIGPIDGHDLDALI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 300 SILETLKSTKtiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQFK-NISKTQSYTSCFVEALIAEAEADKDIV 378
Cdd:PRK05444 223 ETLKNAKDLK--GPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKsSKPGKPSYTKVFGETLCELAEKDPKIV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 379 AIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDR 458
Cdd:PRK05444 301 AITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQVIHDVALQNLPVTFAIDR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 459 AGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPPGNkgvPLQIGRG 538
Cdd:PRK05444 381 AGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNGVGVELPELE---PLPIGKG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 539 RILRDGERVALLGYGSAVQRCLEAASMLSErglkITVADARFCKPLDVALIRSLAKSHEVLITVEEGSI-GGFGSHVVQF 617
Cdd:PRK05444 458 EVLREGEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAImGGFGSAVLEF 533
|
..
gi 186510290 618 LA 619
Cdd:PRK05444 534 LA 535
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
61-631 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 805.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 61 RPPTPLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYP 140
Cdd:PRK12571 3 RPKTPLLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 141 HKILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAM 220
Cdd:PRK12571 83 HKILTGRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 221 NNAGYLHSNMIVILNDNKQVSLPtanldgptqPVGALSCALSRLQSNCGMIR---------------------------- 272
Cdd:PRK12571 163 NNAGAADRRLIVILNDNEMSIAP---------PVGALAAYLSTLRSSDPFARlraiakgveerlpgplrdgarrarelvt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 273 --ETSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQF 350
Cdd:PRK12571 234 gmIGGGTLFEELGFTYVGPIDGHDMEALLSVLRAARARAD-GPVLVHVVTEKGRGYAPAEADEDKYHAVGKFDVVTGLQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 351 KNISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIY 430
Cdd:PRK12571 313 KSAPSAPSYTSVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 431 SSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPS 510
Cdd:PRK12571 393 STFLQRGYDQLLHDVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 511 CFRYHRGNGIGVSLPpgNKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIR 590
Cdd:PRK12571 473 AVRFPRGEGVGVEIP--AEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTD 550
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 186510290 591 SLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKVY 631
Cdd:PRK12571 551 LLVRHHIVVIVEEQGAMGGFGAHVLHHLADTGLLDGGLKLR 591
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
67-624 |
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: 686.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 67 LDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTG 146
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 147 RRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYL 226
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 227 HSNMIVILNDNkQVSLPTanldgptqPVGALSCALSRLQSNCGM--IRE----------------------------TSS 276
Cdd:TIGR00204 161 KTDMIVILNDN-EMSISE--------NVGALSNHLAQLRSGSLYqsLRDglkkifsklppiknylakrteesmkglvVPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 277 TLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQFKNISKT 356
Cdd:TIGR00204 232 TFFEELGFNYIGPVDGHDLLELIETLKNAKKLK--GPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSAL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 357 QSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQR 436
Cdd:TIGR00204 310 PSYSKIFSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 437 AYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHR 516
Cdd:TIGR00204 390 AYDQVVHDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 517 GNGIGVSLPPGNKGVPlqIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSH 596
Cdd:TIGR00204 470 GNAVGVELTPEPEKLP--IGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASH 547
|
570 580
....*....|....*....|....*....
gi 186510290 597 EVLITVEEGSI-GGFGSHVVQFLALDGLL 624
Cdd:TIGR00204 548 EKLVTVEENAImGGAGSAVLEFLMDQNKL 576
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
15-629 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 629.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 15 LSVFAFPSYINRNPSLKYLKPSSMSSTKYSKVRAT-TFSEKGEYYSNRPPTPLLDTINHPMHMKNLSIKELKVLSDELRS 93
Cdd:PLN02225 26 ITVSSLPCKLDVSIKSLFSAPSSTHKECSNRARVCcSLPNTDEYCDEKFETPILDSIETPLQLKNLSVKELKLLADEIRT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 94 DVIFNV-SKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTgRRGKMKTIRQTNGLSGYTKRRESEHD 172
Cdd:PLN02225 106 ELHSVLwKKTQKSMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAHKVLT-RRWSAIPSRQKNGISGVTSQLESEYD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 173 SFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTANlDGPTQ 252
Cdd:PLN02225 185 SFGTGHGCNSISAGLGLAVARDIKGKRDRVVAVIDNATITAGQAYEAMSNAGYLDSNMIVILNDSRHSLHPNME-EGSKA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 253 PVGALSCALSRLQSNC--------------------------------GMIRETSSTLFEELGFHYVGPVDGHNIDDLVS 300
Cdd:PLN02225 264 SISALSSIMSKIQSSKifrkfrelakamtkrigkgmyewaakvdeyarGMVGPTGSTLFEELGLYYIGPVDGHNIEDLVC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 301 ILETLKSTKTIGPVLIHVVTEKGRgypyaeraddkyhgvlkfDPETGKQFKnISKTQSYTSCFVEALIAEAEADKDIVAI 380
Cdd:PLN02225 344 VLREVSSLDSMGPVLVHVITEENR------------------DAETGKNIM-VKDRRTYSDCFVEALVMEAEKDRDIVVV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 381 HAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAG 460
Cdd:PLN02225 405 HAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSAFLQRAYDQVVHDVDRQRKAVRFVITSAG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 461 LMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVS-LPPgnKGVPLQIGRGR 539
Cdd:PLN02225 485 LVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDRPVCFRFPRGSIVNMNyLVP--TGLPIEIGRGR 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 540 ILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLA 619
Cdd:PLN02225 563 VLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITVEEGCVGGFGSHVAQFIA 642
|
650
....*....|
gi 186510290 620 LDGLLDGKLK 629
Cdd:PLN02225 643 LDGQLDGNIK 652
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
65-631 |
4.09e-163 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 479.50 E-value: 4.09e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 65 PLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKIL 144
Cdd:PRK12315 1 MYLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 145 TGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAG 224
Cdd:PRK12315 81 TGRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 225 YLHSNMIVILNDNkQVSLptanldgpTQPVGALSCALSRLQSNCGmirETSSTLFEELGFHYVGPVDGHnidDLVSILET 304
Cdd:PRK12315 161 ELKSNLIIIVNDN-QMSI--------AENHGGLYKNLKELRDTNG---QSENNLFKAMGLDYRYVEDGN---DIESLIEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 305 LKSTKTIG-PVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQfKNISKTQSYTSCFVEALIAEAEADKDIVAIHAA 383
Cdd:PRK12315 226 FKEVKDIDhPIVLHIHTLKGKGYQPAEENKEAFHWHMPFDLETGQS-KVPASGESYSSVTLDYLLKKIKEGKPVVAINAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 384 MGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMG 463
Cdd:PRK12315 305 IPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQRAYDQLSHDLAINNNPAVMIVFGGSISG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 464 ADgPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPPGNKGVPlqigRGRILRD 543
Cdd:PRK12315 385 ND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAIRVPEHGVESGPTVDTDYSTL----KYEVTKA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 544 GERVALLGYGSAVQRCLEAASMLSER-GLKITVADARFCKPLDVALIRSLAKSHEVLITVEEGSI-GGFGSHVVQFLald 621
Cdd:PRK12315 460 GEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEELLEKLKEDHELVVTLEDGILdGGFGEKIARYY--- 536
|
570
....*....|
gi 186510290 622 GLLDGKLKVY 631
Cdd:PRK12315 537 GNSDMKVLNY 546
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
67-320 |
1.32e-143 |
|
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: 417.96 E-value: 1.32e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 67 LDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTG 146
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 147 RRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYL 226
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 227 HSNMIVILNDNkQVSLptanldgpTQPVGALSCALSRLQSNCGM--IRE-----------------------------TS 275
Cdd:pfam13292 161 KKDLIVILNDN-EMSI--------SPNVGALSNYLSRLRTSPTYnrLKEevkkllkpkigpplyelarrakeslkglvVP 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 186510290 276 STLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVT 320
Cdd:pfam13292 232 GTLFEELGFKYIGPIDGHDLDALVKVLENAKDLK--GPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
103-326 |
5.10e-123 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 362.25 E-value: 5.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 103 GGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTT 182
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 183 LSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTanldgptqpVGalscals 262
Cdd:cd02007 81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPN---------VG------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186510290 263 rlqsncgmireTSSTLFEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGY 326
Cdd:cd02007 145 -----------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLK--GPVLLHVVTKKGKGY 195
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
363-619 |
8.39e-69 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 226.12 E-value: 8.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 363 FVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSF-MQRAYDQV 441
Cdd:COG3958 10 FGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFlTGRAYEQI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 442 VHDVDLQKLPVR-FAIDrAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDrPSCFRYHRGNg 519
Cdd:COG3958 90 RNDIAYPNLNVKiVGSH-AGLsYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDG-PVYLRLGRGA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 520 igvsLPPG-NKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEV 598
Cdd:COG3958 167 ----VPVVyDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGA 242
|
250 260
....*....|....*....|..
gi 186510290 599 LITVEEGSI-GGFGSHVVQFLA 619
Cdd:COG3958 243 VVTAEEHSIiGGLGSAVAEVLA 264
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
363-516 |
1.01e-68 |
|
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: 220.39 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 363 FVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVV 442
Cdd:cd07033 3 FGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQIR 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186510290 443 HDVDLQKLPVRFAIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDrPSCFRYHR 516
Cdd:cd07033 83 HDVALQNLPVKFVGTHAGIsVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDG-PVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
355-518 |
4.12e-52 |
|
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: 176.97 E-value: 4.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 355 KTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPT---RCFDVGIAEQHAVTFAAGLACEG--LKPFCTI 429
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 430 YSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDR 508
Cdd:pfam02779 81 FSDFLNRADDAIRHGAALGKLPVPFVVTRDPIgVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 186510290 509 -PSCFRYHRGN 518
Cdd:pfam02779 161 kPVVLRLPRQL 171
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
402-521 |
2.12e-44 |
|
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: 154.95 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 402 FDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACL 481
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 186510290 482 PNMIVMAPSDEAELFNMVATAAAiDDRPSCFRYHRGNGIG 521
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSLYR 136
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
181-614 |
1.07e-33 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 136.03 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 181 TT--LSAGLGMAVG-----RDLKGMNNSVVSVI---------GDGAMTAGQAYEAMNNAGYLH-SNMIVILNDNKqvslp 243
Cdd:PRK05899 116 TTgpLGQGLANAVGmalaeKYLAALFNRPGLDIvdhytyvlcGDGDLMEGISHEACSLAGHLKlGNLIVIYDDNR----- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 244 tANLDGPTqpvgalscalsrlqsnCGMIRETSSTLFEELGFHYVgPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKG 323
Cdd:PRK05899 191 -ISIDGPT----------------EGWFTEDVKKRFEAYGWHVI-EVDGHDVEAIDAAIEEAKAST--KPTLIIAKTIIG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 324 RGYPYAErADDKYHG-VLKFDpetgkqfkNISKTQ-----SYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESR- 396
Cdd:PRK05899 251 KGAPNKE-GTHKVHGaPLGAE--------EIAAAKkelgwDYRKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKd 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 397 -----FPTRCFDVGIAEQHAVTFAAGLACEG-LKPFCTIYSSFMQRAYDQvVHDVDLQKLPVRFAIDRAGL-MGADGPTH 469
Cdd:PRK05899 322 fapedYSGRYIHYGVREFAMAAIANGLALHGgFIPFGGTFLVFSDYARNA-IRLAALMKLPVIYVFTHDSIgVGEDGPTH 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 470 CGAFDVTFMACLPNMIVMAPSDEAElfNMVATAAAID--DRPSCFRYHRGNgigvsLP--PGNKGVPLQIGRGRILRDGE 545
Cdd:PRK05899 401 QPVEQLASLRAIPNLTVIRPADANE--TAAAWKYALErkDGPSALVLTRQN-----LPvlERTAQEEGVAKGGYVLRDDP 473
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186510290 546 RVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDV---ALIRS-LAKSHEVLITVEEGSIGGFGSHV 614
Cdd:PRK05899 474 DVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEqdaAYKESvLPAAVTARVAVEAGVADGWYKYV 546
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
536-632 |
5.03e-31 |
|
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: 117.31 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 536 GRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEGS-IGGFGSHV 614
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVpRGGFGSEV 80
|
90
....*....|....*...
gi 186510290 615 VQFLALDGLLDGKLKVYR 632
Cdd:pfam02780 81 AAALAEEAFDGLDAPVLR 98
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
390-612 |
8.98e-24 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 103.14 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 390 LNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTI-YSSFMQRAYDQVVHDV--------DLQKLPVRFaidRA- 459
Cdd:PTZ00182 73 KGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFmFADFIFPAFDQIVNEAakyrymsgGQFDCPIVI---RGp 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 460 -GLMGADGPTHCGAFDVTFMAClPNMIVMAPSDEAELFNMVAtaAAI-DDRPSCFRYHR---GNGIGVSlPPGNKGVPlq 534
Cdd:PTZ00182 150 nGAVGHGGAYHSQSFEAYFAHV-PGLKVVAPSDPEDAKGLLK--AAIrDPNPVVFFEPKllyRESVEVV-PEADYTLP-- 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186510290 535 IGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDV-ALIRSLAKSHEVLITVEEGSIGGFGS 612
Cdd:PTZ00182 224 LGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDReTIVKSVKKTGRCVIVHEAPPTCGIGA 302
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
77-345 |
2.91e-19 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 88.21 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 77 KNLSIKELKVLSDELRSDVIFNVSKTG-GHLGSNLGVVELTVALHY-IFNTPHDKILWDV--------GHQS---YPHKI 143
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGsGHPGGSLSAADILAALYFkVMNIDPKNPDWPDrdrfilskGHAApalYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 144 LTGR--RGKMKTIRQTNG-LSGytkrreseH-DSFGT-GHSSTT------LSAGLGMAVGRDLKGMNNSVVSVIGDGAMT 212
Cdd:COG3959 81 EKGYfpKEELATFRKLGSrLQG--------HpDMKKTpGVEMSTgslgqgLSVAVGMALAAKLDGKDYRVYVLLGDGELQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 213 AGQAYEAMNNAGYLH-SNMIVILNDNKQvslptaNLDGPTQPVGALscalsrlqsncGMIRETsstlFEELGFHyVGPVD 291
Cdd:COG3959 153 EGQVWEAAMAAAHYKlDNLIAIVDRNGL------QIDGPTEDVMSL-----------EPLAEK----WEAFGWH-VIEVD 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 186510290 292 GHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAErADDKYHGVlKFDPE 345
Cdd:COG3959 211 GHDIEALLAALDEAKAVKG-KPTVIIAHTVKGKGVSFME-NRPKWHGK-APNDE 261
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
89-338 |
2.30e-17 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 82.17 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 89 DELRSDVIFNVSKTG-GHLGSNLGVVELTVAL-----HYIFNTPHDK-----ILwDVGHQS---YPHKILTG--RRGKMK 152
Cdd:cd02012 1 NRIRRLSIDMVQKAGsGHPGGSLSAADILAVLyfkvlKYDPADPKWPnrdrfVL-SKGHASpalYAVLALAGylPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 153 TIRQTNG-LSGYTKRRESEHDSFGTG---HSsttLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLH- 227
Cdd:cd02012 80 TFRQLGSrLPGHPEYGLTPGVEVTTGslgQG---LSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 228 SNMIVILNDNKQvslptaNLDGPTqpvgalscalsRLQSNCGMIRETsstlFEELGFHYVgPVDGHNIDDLVSILETLKS 307
Cdd:cd02012 157 DNLIAIVDSNRI------QIDGPT-----------DDILFTEDLAKK----FEAFGWNVI-EVDGHDVEEILAALEEAKK 214
|
250 260 270
....*....|....*....|....*....|.
gi 186510290 308 TKTiGPVLIHVVTEKGRGYPYAErADDKYHG 338
Cdd:cd02012 215 SKG-KPTLIIAKTIKGKGVPFME-NTAKWHG 243
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
363-494 |
3.18e-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: 78.93 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 363 FVEALIAEAeadKDIVAIhAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSS-FMQRAYDQV 441
Cdd:cd06586 3 FAEVLTAWG---VRHVFG-YPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGtGLLNAINGL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 186510290 442 VhDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAE 494
Cdd:cd06586 79 A-DAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAEL 130
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
104-575 |
2.84e-14 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 76.25 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 104 GHLGSNLGVVELTVALH---YIFNTPH------DKILWDVGHQS---YPHKILTGRRGKM---KTIRQTNGLS-GYTKRr 167
Cdd:PTZ00089 27 GHPGAPMGMAPIAHILWsevMKYNPKDprwinrDRFVLSNGHASallYSMLHLTGYDLSMedlKNFRQLGSRTpGHPER- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 168 eseHDSFGTGHSSTTLSAGLGMAVG-------------RDLKGM-NNSVVSVIGDGAMTAGQAYEAMNNAGYLH-SNMIV 232
Cdd:PTZ00089 106 ---HITPGVEVTTGPLGQGIANAVGlaiaekhlaakfnRPGHPIfDNYVYVICGDGCLQEGVSQEALSLAGHLGlEKLIV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 233 ILNDNKqvslptANLDGPTqpvgalscALSrlqsncgmIRETSSTLFEELGFHyVGPVDGHN--IDDLVSILETLKSTKT 310
Cdd:PTZ00089 183 LYDDNK------ITIDGNT--------DLS--------FTEDVEKKYEAYGWH-VIEVDNGNtdFDGLRKAIEEAKKSKG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 311 iGPVLIHVVT-----------EKGRGYPYAERADDKYHGVLKFDP--------ETGKQFKNISKTQS------------Y 359
Cdd:PTZ00089 240 -KPKLIIVKTtigygsskagtEKVHGAPLGDEDIAQVKELFGLDPekkfhvseEVRQFFEQHVEKKKenyeawkkrfakY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 360 TSCF----------------------------VEALIAEAEADKDIVA-----IHAAMGGGTML-----------NLFES 395
Cdd:PTZ00089 319 TAAFpkeaqaierrfkgelppgwekklpkyttNDKAIATRKASENVLNplfqiLPELIGGSADLtpsnltrpkeaNDFTK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 396 RFPT-RCFDVGIAEQHAVTFAAGLACEG-LKPFCTIYSSFMQRAYDqVVHDVDLQKLPVRFAI--DRAGLmGADGPTHCG 471
Cdd:PTZ00089 399 ASPEgRYIRFGVREHAMCAIMNGIAAHGgFIPFGATFLNFYGYALG-AVRLAALSHHPVIYVAthDSIGL-GEDGPTHQP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 472 AFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNgigvsLPPGNKGVPLQIGRGR-ILRDGE---RV 547
Cdd:PTZ00089 477 VETLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQN-----TPPLPGSSIEGVLKGAyIVVDFTnspQL 551
|
570 580
....*....|....*....|....*...
gi 186510290 548 ALLGYGSAVQRCLEAASMLSErGLKITV 575
Cdd:PTZ00089 552 ILVASGSEVSLCVEAAKALSK-ELNVRV 578
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
392-623 |
5.02e-14 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 73.60 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 392 LFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHDVDLQ--------KLPVRFAidraGLM 462
Cdd:PRK09212 44 LLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFMTfNFSMQAIDQIVNSAAKTnymsggqlKCPIVFR----GPN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 463 GADG---PTHCGAFDVTFmACLPNMIVMAPSDEAELFNMVATAAAiDDRPSCF-RYHRGNGIGVSLPPGNKGVPlqIGRG 538
Cdd:PRK09212 120 GAAArvaAQHSQCYAAWY-SHIPGLKVVAPYFAADCKGLLKTAIR-DPNPVIFlENEILYGHSHEVPEEEESIP--IGKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 539 RILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDV-ALIRSLAKSHEvLITVEEG-SIGGFGS---H 613
Cdd:PRK09212 196 AILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTeTIIESVKKTNR-LVVVEEGwPFAGVGAeiaA 274
|
250
....*....|
gi 186510290 614 VVQFLALDGL 623
Cdd:PRK09212 275 LIMKEAFDYL 284
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
392-605 |
3.17e-13 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 71.39 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 392 LFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHDVDLQ--------KLPVRFAIDRAGLM 462
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTfNFSMQAIDHIINSAAKTnymsagqiSVPIVFRGPNGAAA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 463 GAdGPTHCGAFDVTFMAClPNMIVMAPSDeAELFNMVATAAAIDDRPSCFRYHR---GNGIGVSLPPGNKGVPLQIGRGR 539
Cdd:PLN02683 147 GV-GAQHSQCFAAWYSSV-PGLKVLAPYS-SEDARGLLKAAIRDPDPVVFLENEllyGESFPVSAEVLDSSFVLPIGKAK 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186510290 540 ILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEG 605
Cdd:PLN02683 224 IEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEG 289
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
533-615 |
1.27e-09 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 60.70 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 533 LQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVA-LIRSLAKSHEvLITVEEG-SIGGF 610
Cdd:PRK11892 329 LPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTEtIVESVKKTNR-LVTVEEGwPQSGV 407
|
....*
gi 186510290 611 GSHVV 615
Cdd:PRK11892 408 GAEIA 412
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
365-512 |
2.95e-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: 56.33 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 365 EALIAEAEADKDIVAIH---AAMGG--GTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTI-YSSFMQRAY 438
Cdd:cd07036 5 EALDEEMERDPRVVVLGedvGDYGGvfKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFALPAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 439 DQVVHDV--------DLQKLPVRFaidRaGLMGA---DGPTHCGAFDVTFMAClPNMIVMAPSDEAELFNMVaTAAAIDD 507
Cdd:cd07036 85 DQIVNEAaklrymsgGQFKVPIVI---R-GPNGGgigGGAQHSQSLEAWFAHI-PGLKVVAPSTPYDAKGLL-KAAIRDD 158
|
....*
gi 186510290 508 RPSCF 512
Cdd:cd07036 159 DPVIF 163
|
|
| PLN02790 |
PLN02790 |
transketolase |
160-575 |
2.25e-07 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 53.87 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 160 LSGYTKRRESE------HDSFGTGH---------SSTT--LSAGLGMAVG--------------RDLKGMNNSVVSVIGD 208
Cdd:PLN02790 67 LAGYDSVQMEDlkqfrqWGSRTPGHpenfetpgiEVTTgpLGQGIANAVGlalaekhlaarfnkPDHKIVDHYTYCILGD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 209 GAMTAGQAYEAMNNAGYLH-SNMIVILNDNkQVSLptanlDGPTqpvgalSCALSrlqsncgmirETSSTLFEELGFHYV 287
Cdd:PLN02790 147 GCQMEGISNEAASLAGHWGlGKLIVLYDDN-HISI-----DGDT------EIAFT----------EDVDKRYEALGWHTI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 288 GPVDGHNidDLVSILETLKSTKTIG--PVLIHVVTEKGRGYPYAERADDkYHGVLKFDPETGKQFKNIS----------K 355
Cdd:PLN02790 205 WVKNGNT--DYDEIRAAIKEAKAVTdkPTLIKVTTTIGYGSPNKANSYS-VHGAALGEKEVDATRKNLGwpyepfhvpeD 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 356 TQSYTS-CFVEALIAEAEADKDIVAIHAA--------------------------------------------------- 383
Cdd:PLN02790 282 VKSHWSkHTKEGAALEAEWNAKFAEYKKKypeeaaelkslisgelpsgwekalptftpedpadatrnlsqkclnalakvl 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 384 ---MGGG--------TMLNLF----ESRFPTRCFDVGIAEQHAVTFAAGLA--CEGLKPFCT---IYSSFMQRAydqvVH 443
Cdd:PLN02790 362 pglIGGSadlassnmTLLKDFgdfqKDTPEERNVRFGVREHGMGAICNGIAlhSSGLIPYCAtffVFTDYMRAA----MR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 444 DVDLQKLPVRFAI--DRAGLmGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNgig 521
Cdd:PLN02790 438 LSALSEAGVIYVMthDSIGL-GEDGPTHQPIEHLASLRAMPNILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQK--- 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 186510290 522 VSLPPGNKGVPLQIGrGRILRDGER-----VALLGYGSAVQRCLEAASMLSERGLKITV 575
Cdd:PLN02790 514 VPNLPGTSIEGVEKG-GYVISDNSSgnkpdLILIGTGSELEIAAKAAKELRKEGKKVRV 571
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
162-320 |
1.48e-05 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 47.11 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 162 GYTK-RRESEHDSF-------GTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVI 233
Cdd:cd02000 81 GPCKgRGGSMHIGDkeknffgGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 234 LNDNKqvslptanldgptqpvGALSCALSRlQSNCGMIretsSTLFEELGFHYVgPVDGhniDDLVSILETLKSTKTI-- 311
Cdd:cd02000 161 CENNG----------------YAISTPTSR-QTAGTSI----ADRAAAYGIPGI-RVDG---NDVLAVYEAAKEAVERar 215
|
170
....*....|..
gi 186510290 312 ---GPVLIHVVT 320
Cdd:cd02000 216 aggGPTLIEAVT 227
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
365-625 |
2.48e-05 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 46.66 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 365 EALIAEAEADKDIVAIHAAMG--GGT---MLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCT-IYSSFMQRAY 438
Cdd:CHL00144 12 EAIDEEMARDPRVFVIGEDVGhyGGSykvTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEgMNMGFLLLAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 439 DQVVHDVDLQ--------KLPVrfAIDRAGLMGAD-GPTHCGAFDVTFMAcLPNMIVMAPSDEAELFNMVaTAAAIDDRP 509
Cdd:CHL00144 92 NQISNNAGMLhytsggnfTIPI--VIRGPGGVGRQlGAEHSQRLESYFQS-VPGLQIVACSTPYNAKGLL-KSAIRSNNP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 510 SCFRYH------RGNgigvsLPPGNKGVPLQigRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKP 583
Cdd:CHL00144 168 VIFFEHvllynlKEE-----IPDNEYLLPLE--KAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 186510290 584 LDVALI-RSLAKSHEVLITVEEGSIGGFGShVVQFLALDGLLD 625
Cdd:CHL00144 241 LDLGTIsKSVKKTHKVLIVEECMKTGGIGA-ELIAQINEHLFD 282
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
164-320 |
1.40e-04 |
|
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: 43.01 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 164 TKRRESEHDSFGTGHSSTTLSAGLGMAVGRDlkgmNNSVVSVIGDGAMtaGQAYEAMNNAGYLHSNMIVILNDNkQVSLP 243
Cdd:cd00568 33 LRRGRRFLTSTGFGAMGYGLPAAIGAALAAP----DRPVVCIAGDGGF--MMTGQELATAVRYGLPVIVVVFNN-GGYGT 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186510290 244 TANLDGPTQPVGALSCALSRLQsncgmiretSSTLFEELGFHYVGPVDghnIDDLVSILETLKSTKtiGPVLIHVVT 320
Cdd:cd00568 106 IRMHQEAFYGGRVSGTDLSNPD---------FAALAEAYGAKGVRVED---PEDLEAALAEALAAG--GPALIEVKT 168
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
85-327 |
1.46e-04 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 44.30 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 85 KVLSDELRSDVIFNVSKTG-GHLGSNLGVVELTVAL-----HYIFNTPH----DKILWDVGHQS---YPHKILTGRRGKM 151
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANsGHPGAPMGMAPIAEVLfkrflKHNPNDPKwinrDRFVLSNGHGSmllYSLLHLTGYDLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 152 KTIRQTNGLSGYTK-RRESEHDSfgtGHSSTT--LSAGLGMAVG-----RDLKGMNN--------SVVSVI-GDGAMTAG 214
Cdd:pfam00456 83 EDLKSFRQLGSKTPgHPEFGHTA---GVEVTTgpLGQGIANAVGmaiaeRNLAATYNrpgfdivdHYTYVFlGDGCLMEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186510290 215 QAYEAMNNAGYLH-SNMIVILNDNKqvslptANLDGPTQpvGALScalsrlqsncgmirETSSTLFEELGFHYVGPVDGH 293
Cdd:pfam00456 160 VSSEASSLAGHLGlGNLIVFYDDNQ------ISIDGETK--ISFT--------------EDTAARFEAYGWHVIEVEDGH 217
|
250 260 270
....*....|....*....|....*....|....
gi 186510290 294 NIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYP 327
Cdd:pfam00456 218 DVEAIAAAIEEAKAEKD-KPTLIKCRTVIGYGSP 250
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
185-237 |
2.06e-03 |
|
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: 40.89 E-value: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 186510290 185 AGLGMAVgrDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDN 237
Cdd:COG1071 137 VGAALAA--KLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCENN 187
|
|
| |
