|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
1-621 |
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: 964.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 1 MLEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLT 80
Cdd:COG1154 4 LLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHKILT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 81 GRSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALNNIA 160
Cdd:COG1154 84 GRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKG-EDRKVVAVIGDGALTGGMAFEALNNAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 161 AARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQPGYERVLEEGRKAVRGLPVIGEFCYQCMHSVKAGIKDALSPQVMFT 240
Cdd:COG1154 163 HLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPGIGPPLYELARRAKEGLKGLVVPGTLFE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 241 DLGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVVTRKGMGYAPAENDEaEQMHACGVIDVATGRATKVA--APGWTS 318
Cdd:COG1154 243 ELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDP-DKFHGVGPFDPETGEPKKSKssAPSYTD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 319 SFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQL 398
Cdd:COG1154 322 VFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 399 MMDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVnDAPTAIRFPKGD-VG 477
Cdd:COG1154 402 IHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIRYPRGNgPG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 478 EDIPAVRRHR---GVDVLAEpadglSDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPVP-EVLTEFAAAHKL 553
Cdd:COG1154 481 VELPAELEPLpigKGEVLRE-----GKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDeELILELAREHDL 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123369359 554 VVTVEDNGLHGGIGSSVSAALRHAEVDVPCRDVGLPQQFFDHASRGEVLADVGVTDRNISRQITGWVA 621
Cdd:COG1154 556 VVTVEEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-620 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 896.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 1 MLEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLT 80
Cdd:PRK05444 6 LLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPHKILT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 81 GRSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGHRNRHVVAVVGDGALTGGMCWEALNNIA 160
Cdd:PRK05444 86 GRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEALNNAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 161 AARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQpgyervleegrkavrglpvigefcyqcmhsvkagikdalspqVMFT 240
Cdd:PRK05444 166 DLKSDLIVILNDNEMSISPNVGALSNYLARLRSS------------------------------------------TLFE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 241 DLGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVVTRKGMGYAPAENDEAEqMHACGVIDVATGRATKVA---APGWT 317
Cdd:PRK05444 204 ELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIK-YHGVGKFDPETGEQPKSSkpgKPSYT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 318 SSFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQ 397
Cdd:PRK05444 283 KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 398 LMMDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDAPTAIRFPKGD-V 476
Cdd:PRK05444 363 VIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNgV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 477 GEDIPAVRRHR--GVDVLAEpadglSDDVLLVAVGPFASMALTVAERLRKqgigVTVVDPRWVLPVP-EVLTEFAAAHKL 553
Cdd:PRK05444 443 GVELPELEPLPigKGEVLRE-----GEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDeELLLELAAKHDL 513
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123369359 554 VVTVEDNGLHGGIGSSVSAALRHAEVDVPCRDVGLPQQFFDHASRGEVLADVGVTDRNISRQITGWV 620
Cdd:PRK05444 514 VVTVEEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
2-621 |
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: 586.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 2 LEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLTG 81
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 82 RSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALNNIAA 161
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKG-ADRKTVCVIGDGAITAGMAFEALNHAGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 162 ARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQPGYERVLEEGRKAVRGLPVIGEFCyqcMHSVKAGIKDALSPQVMFTD 241
Cdd:TIGR00204 160 LKTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYL---AKRTEESMKGLVVPGTFFEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 242 LGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVVTRKGMGYAPAENDEaEQMHACGVIDVATG--RATKVAAPGWTSS 319
Cdd:TIGR00204 237 LGFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDP-IGWHGVGPFDLSTGclPKSKSALPSYSKI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 320 FSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQLM 399
Cdd:TIGR00204 316 FSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 400 MDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDAPTAIRFPKGDvGED 479
Cdd:TIGR00204 396 HDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGN-AVG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 480 IPAVRRHRGVDVLAEPADGLSDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPV-PEVLTEFAAAHKLVVTVE 558
Cdd:TIGR00204 475 VELTPEPEKLPIGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLdEELILEIAASHEKLVTVE 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123369359 559 DNGLHGGIGSSVSAALRHAEVDVPCRDVGLPQQFFDHASRGEVLADVGVTDRNISRQITGWVA 621
Cdd:TIGR00204 555 ENAIMGGAGSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
2-278 |
3.58e-158 |
|
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: 454.94 E-value: 3.58e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 2 LEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLTG 81
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 82 RSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALNNIAA 161
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKG-EDRKVVAVIGDGALTGGMAFEALNNAGH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 162 ARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQPGYERVLEEGRKAVRglPVIGEFCYQCMHSVKAGIKDALSPQVMFTD 241
Cdd:pfam13292 160 LKKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLK--PKIGPPLYELARRAKESLKGLVVPGTLFEE 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 123369359 242 LGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVVT 278
Cdd:pfam13292 238 LGFKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
38-284 |
3.07e-97 |
|
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: 296.00 E-value: 3.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 38 GGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLTGRSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAA 117
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 118 LSYADGLAKAFELTGHrNRHVVAVVGDGALTGGMCWEALNNIAAARRPVVIVVNDNGRSYAPTIGgfadhlaalrlqpgy 197
Cdd:cd02007 81 ISAALGMAVARDLKGK-KRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 198 ervleegrkavrglpvigefcyqcmhsvkagikdalSPQVMFTDLGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVV 277
Cdd:cd02007 145 ------------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVV 188
|
....*..
gi 123369359 278 TRKGMGY 284
Cdd:cd02007 189 TKKGKGY 195
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
349-474 |
4.03e-36 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 132.22 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 349 AFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQLMMDVALHKLPVTLVLDRSGVTGPDGASHNG 428
Cdd:smart00861 8 AFGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHS 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 123369359 429 MWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDaPTAIRFPKG 474
Cdd:smart00861 88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDG-PVVIRLERK 132
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
1-621 |
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: 964.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 1 MLEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLT 80
Cdd:COG1154 4 LLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHKILT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 81 GRSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALNNIA 160
Cdd:COG1154 84 GRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKG-EDRKVVAVIGDGALTGGMAFEALNNAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 161 AARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQPGYERVLEEGRKAVRGLPVIGEFCYQCMHSVKAGIKDALSPQVMFT 240
Cdd:COG1154 163 HLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPGIGPPLYELARRAKEGLKGLVVPGTLFE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 241 DLGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVVTRKGMGYAPAENDEaEQMHACGVIDVATGRATKVA--APGWTS 318
Cdd:COG1154 243 ELGFKYIGPIDGHDLDALVETLRNAKDLKGPVLLHVVTKKGKGYAPAEKDP-DKFHGVGPFDPETGEPKKSKssAPSYTD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 319 SFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQL 398
Cdd:COG1154 322 VFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 399 MMDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVnDAPTAIRFPKGD-VG 477
Cdd:COG1154 402 IHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIRYPRGNgPG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 478 EDIPAVRRHR---GVDVLAEpadglSDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPVP-EVLTEFAAAHKL 553
Cdd:COG1154 481 VELPAELEPLpigKGEVLRE-----GKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDeELILELAREHDL 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123369359 554 VVTVEDNGLHGGIGSSVSAALRHAEVDVPCRDVGLPQQFFDHASRGEVLADVGVTDRNISRQITGWVA 621
Cdd:COG1154 556 VVTVEEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-620 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 896.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 1 MLEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLT 80
Cdd:PRK05444 6 LLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYPHKILT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 81 GRSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGHRNRHVVAVVGDGALTGGMCWEALNNIA 160
Cdd:PRK05444 86 GRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEALNNAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 161 AARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQpgyervleegrkavrglpvigefcyqcmhsvkagikdalspqVMFT 240
Cdd:PRK05444 166 DLKSDLIVILNDNEMSISPNVGALSNYLARLRSS------------------------------------------TLFE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 241 DLGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVVTRKGMGYAPAENDEAEqMHACGVIDVATGRATKVA---APGWT 317
Cdd:PRK05444 204 ELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIK-YHGVGKFDPETGEQPKSSkpgKPSYT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 318 SSFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQ 397
Cdd:PRK05444 283 KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYDQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 398 LMMDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDAPTAIRFPKGD-V 476
Cdd:PRK05444 363 VIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNgV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 477 GEDIPAVRRHR--GVDVLAEpadglSDDVLLVAVGPFASMALTVAERLRKqgigVTVVDPRWVLPVP-EVLTEFAAAHKL 553
Cdd:PRK05444 443 GVELPELEPLPigKGEVLRE-----GEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDeELLLELAAKHDL 513
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123369359 554 VVTVEDNGLHGGIGSSVSAALRHAEVDVPCRDVGLPQQFFDHASRGEVLADVGVTDRNISRQITGWV 620
Cdd:PRK05444 514 VVTVEEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-632 |
0e+00 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 794.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 1 MLEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLT 80
Cdd:PRK12571 8 LLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCYPHKILT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 81 GRSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELtGHRNRHVVAVVGDGALTGGMCWEALNNIA 160
Cdd:PRK12571 88 GRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARAL-GQPDGDVVAVIGDGSLTAGMAYEALNNAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 161 AARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQPGYERVLEEGRKAVRGLPvigEFCYQCMHSVKAGIKDALSPQVMFT 240
Cdd:PRK12571 167 AADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIAKGVEERLP---GPLRDGARRARELVTGMIGGGTLFE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 241 DLGLKYVGPIDGHDEHAVESALRHAR-GFNAPVIVHVVTRKGMGYAPAENDEaEQMHACGVIDVATGRATKVA--APGWT 317
Cdd:PRK12571 244 ELGFTYVGPIDGHDMEALLSVLRAARaRADGPVLVHVVTEKGRGYAPAEADE-DKYHAVGKFDVVTGLQKKSApsAPSYT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 318 SSFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQ 397
Cdd:PRK12571 323 SVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQRGYDQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 398 LMMDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDAPTAIRFPKGD-V 476
Cdd:PRK12571 403 LLHDVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEgV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 477 GEDIPAVRRHRGVDVLAEPADGlsDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPVPEVLTEFAAAHKLVVT 556
Cdd:PRK12571 483 GVEIPAEGTILGIGKGRVPREG--PDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHIVVI 560
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123369359 557 VEDNGLHGGIGSSVSAALRHA---EVDVPCRDVGLPQQFFDHASRGEVLADVGVTDRNISRQITGWVAALGATPADADE 632
Cdd:PRK12571 561 VEEQGAMGGFGAHVLHHLADTgllDGGLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALARLSGVPERETA 639
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
2-621 |
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: 586.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 2 LEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLTG 81
Cdd:TIGR00204 1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 82 RSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALNNIAA 161
Cdd:TIGR00204 81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKG-ADRKTVCVIGDGAITAGMAFEALNHAGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 162 ARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQPGYERVLEEGRKAVRGLPVIGEFCyqcMHSVKAGIKDALSPQVMFTD 241
Cdd:TIGR00204 160 LKTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYL---AKRTEESMKGLVVPGTFFEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 242 LGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVVTRKGMGYAPAENDEaEQMHACGVIDVATG--RATKVAAPGWTSS 319
Cdd:TIGR00204 237 LGFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGYKPAEKDP-IGWHGVGPFDLSTGclPKSKSALPSYSKI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 320 FSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQLM 399
Cdd:TIGR00204 316 FSDTLCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 400 MDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDAPTAIRFPKGDvGED 479
Cdd:TIGR00204 396 HDVCIQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGN-AVG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 480 IPAVRRHRGVDVLAEPADGLSDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPV-PEVLTEFAAAHKLVVTVE 558
Cdd:TIGR00204 475 VELTPEPEKLPIGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLdEELILEIAASHEKLVTVE 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123369359 559 DNGLHGGIGSSVSAALRHAEVDVPCRDVGLPQQFFDHASRGEVLADVGVTDRNISRQITGWVA 621
Cdd:TIGR00204 555 ENAIMGGAGSAVLEFLMDQNKLVPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
2-278 |
3.58e-158 |
|
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: 454.94 E-value: 3.58e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 2 LEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLTG 81
Cdd:pfam13292 1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 82 RSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALNNIAA 161
Cdd:pfam13292 81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKG-EDRKVVAVIGDGALTGGMAFEALNNAGH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 162 ARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQPGYERVLEEGRKAVRglPVIGEFCYQCMHSVKAGIKDALSPQVMFTD 241
Cdd:pfam13292 160 LKKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLK--PKIGPPLYELARRAKESLKGLVVPGTLFEE 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 123369359 242 LGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVVT 278
Cdd:pfam13292 238 LGFKYIGPIDGHDLDALVKVLENAKDLKGPVLLHVVT 274
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
2-618 |
8.47e-154 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 455.62 E-value: 8.47e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 2 LEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLTG 81
Cdd:PRK12315 3 LEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKMLTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 82 RSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALNNIAA 161
Cdd:PRK12315 83 RKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKG-EKGNIIAVIGDGSLSGGLALEGLNNAAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 162 ARRPVVIVVNDNGRSYAPTIGGFADHLAALRLQpgyervleEGRkavrglpvigefcyqcmhsvkagikdalSPQVMFTD 241
Cdd:PRK12315 162 LKSNLIIIVNDNQMSIAENHGGLYKNLKELRDT--------NGQ----------------------------SENNLFKA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 242 LGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVVTRKGMGYAPAENDEaEQMHACGVIDVATGrATKVAAPGWTSS-- 319
Cdd:PRK12315 206 MGLDYRYVEDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKGYQPAEENK-EAFHWHMPFDLETG-QSKVPASGESYSsv 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 320 FSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQLM 399
Cdd:PRK12315 284 TLDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQRAYDQLS 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 400 MDVALHKLPVTLVLDRSGVTGPDgASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDAPTAIRFPKGDVGED 479
Cdd:PRK12315 364 HDLAINNNPAVMIVFGGSISGND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAIRVPEHGVESG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 480 IPAVR---------RHRGvdvlaepadglsDDVLLVAVGPFASMALTVAERLRKQ-GIGVTVVDPRWV-LPVPEVLTEFA 548
Cdd:PRK12315 443 PTVDTdystlkyevTKAG------------EKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFItGLDEELLEKLK 510
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 549 AAHKLVVTVEDNGLHGGIGSSVSAALRHAEVDVpcRDVGLPQQFFDHASRGEVLADVGVTDRNISRQITG 618
Cdd:PRK12315 511 EDHELVVTLEDGILDGGFGEKIARYYGNSDMKV--LNYGAKKEFNDRVPVEELYKRNHLTPEQIVEDILS 578
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
1-613 |
2.65e-138 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 419.31 E-value: 2.65e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 1 MLEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLT 80
Cdd:PLN02582 33 LLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQSYPHKILT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 81 GRSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGHRNrHVVAVVGDGALTGGMCWEALNNIA 160
Cdd:PLN02582 113 GRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKN-NVVAVIGDGAMTAGQAYEAMNNAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 161 AARRPVVIVVNDNGRSYAPT--IGGFADHLAAL-----RLQPgyERVLEEGRKAVRGL-PVIGefcyQCMHSVKAGIKD- 231
Cdd:PLN02582 192 YLDSDMIVILNDNKQVSLPTatLDGPAPPVGALssalsRLQS--SRPLRELREVAKGVtKQIG----GPMHELAAKVDEy 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 232 -----ALSPQVMFTDLGLKYVGPIDGHDEHAVESALRHARGF--NAPVIVHVVTRKGMGYAPAENdEAEQMHACGVIDVA 304
Cdd:PLN02582 266 argmiSGSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTktTGPVLIHVVTEKGRGYPYAER-AADKYHGVVKFDPA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 305 TGRATKVAAP--GWTSSFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHP 382
Cdd:PLN02582 345 TGKQFKVKAKtqSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 383 VVAIYSTFLNRAFDQLMMDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDV 462
Cdd:PLN02582 425 FCAIYSSFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAI 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 463 NDAPTAIRFPKGD-VGEDIPAvrRHRGVDVlaEPADGL----SDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWV 537
Cdd:PLN02582 505 DDRPSCFRYPRGNgIGVQLPP--NNKGIPI--EVGKGRilleGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFC 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 538 LPVPEVLT-EFAAAHKLVVTVEDNGLhGGIGSSVSAALRHAEV---DVPCRDVGLPQQFFDHASRGEVLADVGVTDRNIS 613
Cdd:PLN02582 581 KPLDRALIrSLAKSHEVLITVEEGSI-GGFGSHVAQFMALDGLldgKLKWRPLVLPDRYIDHGAPADQLAEAGLTPSHIA 659
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
1-570 |
2.14e-116 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 361.34 E-value: 2.14e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 1 MLEQIRGPADLQHLSQSALSELAGEIRQFLIHKVAATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLT 80
Cdd:PLN02234 66 LLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKILT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 81 GRSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALNNIA 160
Cdd:PLN02234 146 GRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKG-MNNSVVSVIGDGAMTAGQAYEAMNNAG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 161 AARRPVVIVVNDNGRSYAPT--IGGFADHLAALRlqpgyervleegrkavrglpvigefCYQCMHSVKAGIKDALSpQVM 238
Cdd:PLN02234 225 YLHSNMIVILNDNKQVSLPTanLDGPTQPVGALS-------------------------CALSRLQSNCGMIRETS-STL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 239 FTDLGLKYVGPIDGHDEHAVESALRHARGFN--APVIVHVVTRKGMGYAPAENDEaEQMHACGVIDVATGRATK--VAAP 314
Cdd:PLN02234 279 FEELGFHYVGPVDGHNIDDLVSILETLKSTKtiGPVLIHVVTEKGRGYPYAERAD-DKYHGVLKFDPETGKQFKniSKTQ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 315 GWTSSFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRA 394
Cdd:PLN02234 358 SYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQRA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 395 FDQLMMDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDAPTAIRFPKG 474
Cdd:PLN02234 438 YDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRG 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 475 D-VGEDIPAvrRHRGVDVLAEPADGLSDD--VLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPVPEVLTE-FAAA 550
Cdd:PLN02234 518 NgIGVSLPP--GNKGVPLQIGRGRILRDGerVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRsLAKS 595
|
570 580
....*....|....*....|
gi 123369359 551 HKLVVTVEDNGLhGGIGSSV 570
Cdd:PLN02234 596 HEVLITVEEGSI-GGFGSHV 614
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
38-284 |
3.07e-97 |
|
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: 296.00 E-value: 3.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 38 GGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKMLTGRSHEFDSLRKKDGLSGYPSRSESEHDWVESSHASAA 117
Cdd:cd02007 1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 118 LSYADGLAKAFELTGHrNRHVVAVVGDGALTGGMCWEALNNIAAARRPVVIVVNDNGRSYAPTIGgfadhlaalrlqpgy 197
Cdd:cd02007 81 ISAALGMAVARDLKGK-KRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 198 ervleegrkavrglpvigefcyqcmhsvkagikdalSPQVMFTDLGLKYVGPIDGHDEHAVESALRHARGFNAPVIVHVV 277
Cdd:cd02007 145 ------------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVV 188
|
....*..
gi 123369359 278 TRKGMGY 284
Cdd:cd02007 189 TKKGKGY 195
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
1-613 |
1.59e-88 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 290.08 E-value: 1.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 1 MLEQIRGPADLQHLSQSALSELAGEIRQFLiHKV--AATGGHLGPNLGVVELTLALHRVFDSPHDPLIFDTGHQAYVHKM 78
Cdd:PLN02225 78 ILDSIETPLQLKNLSVKELKLLADEIRTEL-HSVlwKKTQKSMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAHKV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 79 LTGRSHEFDSlRKKDGLSGYPSRSESEHDWVESSHASAALSYADGLAKAFELTGHRNRhVVAVVGDGALTGGMCWEALNN 158
Cdd:PLN02225 157 LTRRWSAIPS-RQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGKRDR-VVAVIDNATITAGQAYEAMSN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 159 IAAARRPVVIVVNDNGRSYAPTI--GGFAD--HLAALRLQPGYERVLEEGRKAVRGLPV-IGEFCYQCMHSVKAGIKDAL 233
Cdd:PLN02225 235 AGYLDSNMIVILNDSRHSLHPNMeeGSKASisALSSIMSKIQSSKIFRKFRELAKAMTKrIGKGMYEWAAKVDEYARGMV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 234 SP--QVMFTDLGLKYVGPIDGHDEHAVESALRHARGFNA--PVIVHVVTRkgmgyapaENDEAEQMHACGVIDVATgrat 309
Cdd:PLN02225 315 GPtgSTLFEELGLYYIGPVDGHNIEDLVCVLREVSSLDSmgPVLVHVITE--------ENRDAETGKNIMVKDRRT---- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 310 kvaapgWTSSFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYST 389
Cdd:PLN02225 383 ------YSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 390 FLNRAFDQLMMDVALHKLPVTLVLDRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDAPTAI 469
Cdd:PLN02225 457 FLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDRPVCF 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 470 RFPKGDVGED---IPA---VRRHRGvDVLAEpadglSDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPVP-E 542
Cdd:PLN02225 537 RFPRGSIVNMnylVPTglpIEIGRG-RVLVE-----GQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDiK 610
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123369359 543 VLTEFAAAHKLVVTVEDnGLHGGIGSSVSAALR---HAEVDVPCRDVGLPQQFFDHASRGEVLADVGVTDRNIS 613
Cdd:PLN02225 611 LVRDLCQNHKFLITVEE-GCVGGFGSHVAQFIAldgQLDGNIKWRPIVLPDGYIEEASPREQLALAGLTGHHIA 683
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
320-620 |
6.63e-62 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 208.02 E-value: 6.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 320 FSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFL-NRAFDQL 398
Cdd:COG3958 10 FGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLtGRAYEQI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 399 MMDVALHKLPVTLVLDRSGVT-GPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDaPTAIRFPKGDV- 476
Cdd:COG3958 90 RNDIAYPNLNVKIVGSHAGLSyGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDG-PVYLRLGRGAVp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 477 ---GEDIP-----AVRRHRGvdvlaepadglsDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPVP-EVLTEF 547
Cdd:COG3958 169 vvyDEDYEfeigkARVLREG------------KDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDeEAILKA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123369359 548 AAAHKLVVTVEDNGLHGGIGSSVSAALrhAE-VDVPCRDVGLPQQFFDHASRGEVLADVGVTDRNISRQITGWV 620
Cdd:COG3958 237 ARKTGAVVTAEEHSIIGGLGSAVAEVL--AEnYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
319-473 |
1.02e-56 |
|
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: 188.80 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 319 SFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQL 398
Cdd:cd07033 2 AFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123369359 399 MMDVALHKLPVTLVLDRSGVT-GPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDvNDAPTAIRFPK 473
Cdd:cd07033 82 RHDVALQNLPVKFVGTHAGISvGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALE-YDGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
312-477 |
8.44e-42 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 149.24 E-value: 8.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 312 AAPGWTSSFSEALIDYGAKRRDIVAITAAMPGPTGLSAFRDRFPD---RFFDVGIAEQHAMTSAAGLAMGG--LHPVVAI 386
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 387 YSTFLNRAFDQLMMDVALHKLPVTLVLDRSGV-TGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVND- 464
Cdd:pfam02779 81 FSDFLNRADDAIRHGAALGKLPVPFVVTRDPIgVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|...
gi 123369359 465 APTAIRFPKGDVG 477
Cdd:pfam02779 161 KPVVLRLPRQLLR 173
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
349-474 |
4.03e-36 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 132.22 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 349 AFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIYSTFLNRAFDQLMMDVALHKLPVTLVLDRSGVTGPDGASHNG 428
Cdd:smart00861 8 AFGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHS 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 123369359 429 MWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDaPTAIRFPKG 474
Cdd:smart00861 88 IEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDG-PVVIRLERK 132
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
501-612 |
9.97e-23 |
|
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: 93.81 E-value: 9.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 501 DDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPV-PEVLTEFAAAHKLVVTVEDNGLHGGIGSSVSAAL---RH 576
Cdd:pfam02780 10 DDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLdKETILESVKKTGRLVTVEEAVPRGGFGSEVAAALaeeAF 89
|
90 100 110
....*....|....*....|....*....|....*.
gi 123369359 577 AEVDVPCRDVGLPqQFFDHASRGEVLADVGVTDRNI 612
Cdd:pfam02780 90 DGLDAPVLRVGGP-DFPEPGSADELEKLYGLTPEKI 124
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
250-574 |
1.00e-22 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 102.52 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 250 IDGHDEHAVESALRHARGFNAPVIVHVVTRKGMGYAPAENDEAeqMH--ACGVIDVAtgrATKvAAPGWT--SSFSEALI 325
Cdd:PRK05899 219 VDGHDVEAIDAAIEEAKASTKPTLIIAKTIIGKGAPNKEGTHK--VHgaPLGAEEIA---AAK-KELGWDyrKASGKALN 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 326 DYGAKRRDIVAITAAMPGPT-----GLSAFRDR-FPDRFFDVGIAEqHAMTSAA-GLAM-GGLHPVVAIYSTFLNRAFDQ 397
Cdd:PRK05899 293 ALAKALPELVGGSADLAGSNntkikGSKDFAPEdYSGRYIHYGVRE-FAMAAIAnGLALhGGFIPFGGTFLVFSDYARNA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 398 LMMDvALHKLPVTLVL--DRSGVtGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLREELGEALDVNDAPTAIRFPKGD 475
Cdd:PRK05899 372 IRLA-ALMKLPVIYVFthDSIGV-GEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQN 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 476 VgediPAVRRHRGVD-------VLAEpadglSDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDprwvLPVPEVLTEFA 548
Cdd:PRK05899 450 L----PVLERTAQEEgvakggyVLRD-----DPDVILIATGSEVHLALEAADELEAEGIKVRVVS----MPSTELFDEQD 516
|
330 340
....*....|....*....|....*.
gi 123369359 549 AAHKlvvtvednglHGGIGSSVSAAL 574
Cdd:PRK05899 517 AAYK----------ESVLPAAVTARV 532
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
335-473 |
4.81e-16 |
|
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: 75.84 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 335 VAITAAMPGPTGLSAFRDRFPDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAIY-STFLNRAFDQlMMDVALHKLPVTLVL 413
Cdd:cd06586 14 HVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTsGTGLLNAING-LADAAAEHLPVVFLI 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123369359 414 DRSGVTGPDGASHNGMWDLSVLGIVPGMRVAAPRDGARLRE--ELGEALDVNDAPTAIRFPK 473
Cdd:cd06586 93 GARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGidHAIRTAYASQGPVVVRLPR 154
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
350-572 |
2.37e-09 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 59.61 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 350 FRDRF-PDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAI-YSTFLNRAFDQLMMDVALHK------LPVTLVLdRS--GVT 419
Cdd:PTZ00182 75 LLDKYgPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFmFADFIFPAFDQIVNEAAKYRymsggqFDCPIVI-RGpnGAV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 420 GPDGASHN---GMWdlsvLGIVPGMRVAAPRDG--------ARLREE-----------LGEALDVNDAPT-AIRFPKGDV 476
Cdd:PTZ00182 154 GHGGAYHSqsfEAY----FAHVPGLKVVAPSDPedakgllkAAIRDPnpvvffepkllYRESVEVVPEADyTLPLGKAKV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 477 gedipaVRRhrgvdvlaepadglSDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLP--VPEVLTEFAAAHKLv 554
Cdd:PTZ00182 230 ------VRE--------------GKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPwdRETIVKSVKKTGRC- 288
|
250
....*....|....*...
gi 123369359 555 VTVEDNGLHGGIGSSVSA 572
Cdd:PTZ00182 289 VIVHEAPPTCGIGAEIAA 306
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
352-450 |
5.49e-08 |
|
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132919 [Multi-domain] Cd Length: 167 Bit Score: 52.87 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 352 DRF-PDRFFDVGIAEQHAMTSAAGLAMGGLHPVVAI-YSTFLNRAFDQLMMDVA-LH-----KLPVTLVLdR--SGVTGP 421
Cdd:cd07036 39 DKFgPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFALPAFDQIVNEAAkLRymsggQFKVPIVI-RgpNGGGIG 117
|
90 100 110
....*....|....*....|....*....|
gi 123369359 422 DGASHNGmwDL-SVLGIVPGMRVAAPRDGA 450
Cdd:cd07036 118 GGAQHSQ--SLeAWFAHIPGLKVVAPSTPY 145
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
352-572 |
8.05e-08 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 54.34 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 352 DRF-PDRFFDVGIAEqHAMTS-AAGLAMGGLHPVVAIYS-TFLNRAFDQLMMDVA-LH-----KLPVTLVLdrsgvTGPD 422
Cdd:PRK09212 46 EQFgPKRVIDTPITE-HGFAGlAVGAAFAGLRPIVEFMTfNFSMQAIDQIVNSAAkTNymsggQLKCPIVF-----RGPN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 423 GAS------HNGMWDlSVLGIVPGMRVAAPRDGARLREELgealdvndaPTAIRFP--------------KGDVGEDIPA 482
Cdd:PRK09212 120 GAAarvaaqHSQCYA-AWYSHIPGLKVVAPYFAADCKGLL---------KTAIRDPnpvifleneilyghSHEVPEEEES 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 483 VRRHRGvDVLAEpadglSDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPVPE--VLTEFAAAHKLVVtVEDN 560
Cdd:PRK09212 190 IPIGKA-AILRE-----GSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTetIIESVKKTNRLVV-VEEG 262
|
250
....*....|..
gi 123369359 561 GLHGGIGSSVSA 572
Cdd:PRK09212 263 WPFAGVGAEIAA 274
|
|
| PFOR_II |
pfam17147 |
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ... |
502-574 |
2.84e-06 |
|
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic enzyme pyruvate:ferredoxin oxidoreductase and is necessary for inter subunit contacts in conjunction with domains I and IV.
Pssm-ID: 407280 [Multi-domain] Cd Length: 102 Bit Score: 46.10 E-value: 2.84e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123369359 502 DVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLPVP-EVLTEFAAAHKLVVTVEDN---GLHGGIGSSVSAAL 574
Cdd:pfam17147 2 EVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPeEELKELLAGVKKVVVLDRNisfGSPGQLGTEVKAAL 78
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
35-174 |
4.98e-05 |
|
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: 45.19 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 35 AATGGHLGPNLGVVELTLAL------HRVFDsPHDP----LIFDTGHQA---YVHKMLTGRSHEFD--SLRKKDG-LSGY 98
Cdd:cd02012 13 KAGSGHPGGSLSAADILAVLyfkvlkYDPAD-PKWPnrdrFVLSKGHASpalYAVLALAGYLPEEDlkTFRQLGSrLPGH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 99 PSRSESehDWVESSHAS--AALSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEA--------LNNIaaarrpvVI 168
Cdd:cd02012 92 PEYGLT--PGVEVTTGSlgQGLSVAVGMALAEKLLG-FDYRVYVLLGDGELQEGSVWEAasfaghykLDNL-------IA 161
|
....*.
gi 123369359 169 VVNDNG 174
Cdd:cd02012 162 IVDSNR 167
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
117-174 |
1.63e-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: 42.63 E-value: 1.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 123369359 117 ALSYADGLAKAfeltgHRNRHVVAVVGDGALtgGMCWEALNNIAAARRPVVIVVNDNG 174
Cdd:cd00568 51 GLPAAIGAALA-----APDRPVVCIAGDGGF--MMTGQELATAVRYGLPVIVVVFNNG 101
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
121-178 |
2.44e-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: 43.59 E-value: 2.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 123369359 121 ADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALnNIAAARR-PVVIVVNDNGrsYA 178
Cdd:COG1071 136 AVGAALAAKLRG-EDEVAVAFFGDGATSEGDFHEAL-NFAAVWKlPVVFVCENNG--YA 190
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
19-169 |
5.98e-04 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 41.99 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 19 LSELAGEIRQFLIHKVAATG-GHLGPNLGVVELTLALHrvFD----SPHDP-------LIFDTGHQA---YVHKMLTGR- 82
Cdd:COG3959 8 LEEKARQIRRDILRMIYAAGsGHPGGSLSAADILAALY--FKvmniDPKNPdwpdrdrFILSKGHAApalYAVLAEKGYf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 83 -SHEFDSLRKKDG-LSGYPSRSESEHdwVESS-----HAsaaLSYADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEA 155
Cdd:COG3959 86 pKEELATFRKLGSrLQGHPDMKKTPG--VEMStgslgQG---LSVAVGMALAAKLDG-KDYRVYVLLGDGELQEGQVWEA 159
|
170 180
....*....|....*....|..
gi 123369359 156 --------LNNIaaarrpVVIV 169
Cdd:COG3959 160 amaaahykLDNL------IAIV 175
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
121-178 |
6.09e-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: 42.10 E-value: 6.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 123369359 121 ADGLAKAFELTGhRNRHVVAVVGDGALTGGMCWEALNnIAAARR-PVVIVVNDNGrsYA 178
Cdd:cd02000 113 AAGAALALKYRG-EDRVAVCFFGDGATNEGDFHEALN-FAALWKlPVIFVCENNG--YA 167
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
347-589 |
1.21e-03 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 41.83 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 347 LSAFRDRfpdRFFDVGIAEQHAMTSAAGLAMGGLHPVVAiYSTFlN---RAFDQLMMDVAlhKlpvTLVLdrSG------ 417
Cdd:PRK11892 183 LQEFGAR---RVIDTPITEHGFAGIGVGAAFAGLKPIVE-FMTF-NfamQAIDQIINSAA--K---TLYM--SGgqmgcp 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 418 --VTGPDGA--------SHN-GMWdlsvLGIVPGMRVAAPRDGArlreelgealdvnDAP----TAIRFP---------- 472
Cdd:PRK11892 251 ivFRGPNGAaarvaaqhSQDyAAW----YSHIPGLKVVAPYSAA-------------DAKgllkAAIRDPnpviflenei 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123369359 473 ----KGDVGED------IPAVRRHRGvdvlaepadglSDDVLLVAVGPFASMALTVAERLRKQGIGVTVVDPRWVLP--V 540
Cdd:PRK11892 314 lygqSFDVPKLddfvlpIGKARIHRE-----------GKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPmdT 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 123369359 541 PEVLTEFAAAHKLvVTVEDNGLHGGIGSSVSA-ALRHA--EVDVPC-----RDVGLP 589
Cdd:PRK11892 383 ETIVESVKKTNRL-VTVEEGWPQSGVGAEIAArVMEQAfdYLDAPVlrvtgKDVPMP 438
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
117-174 |
2.06e-03 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 39.11 E-value: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 123369359 117 ALSYADGLAKAfeltgHRNRHVVAVVGDGALtgGMCWEALNNIAAARRPVVIVVNDNG 174
Cdd:pfam02775 33 GLPAAIGAKLA-----RPDRPVVAIAGDGGF--QMNLQELATAVRYNLPITVVVLNNG 83
|
|
| |
