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Conserved domains on  [gi|1601858065|gb|QBQ57510|]
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1-deoxy-D-xylulose-5-phosphate synthase [synthetic Caulobacter sp. 'ethensis']

Protein Classification

1-deoxy-D-xylulose-5-phosphate synthase( domain architecture ID 11439322)

1-deoxy-D-xylulose-5-phosphate synthase catalyzes the formation of 1-deoxy-D-xylulose 5-phosphate from pyruvate and D-glyceraldehyde-3-phosphate

CATH:  3.40.50.920|3.40.50.970
EC:  2.2.1.7
Gene Ontology:  GO:0008661|GO:0000287|GO:0030976|GO:0052865

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 4-627 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: 1092.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   4 KTPLLDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHK 83
Cdd:COG1154     1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  84 ILTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNA 163
Cdd:COG1154    81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 164 ATDTTKRLIVILNDNDMSIAPPVGGMSAYLANLVSGGAYRSVRKLGKTVVEKLP---TPMREAARKAEEYARGMVTGGTF 240
Cdd:COG1154   161 AGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPgigPPLYELARRAKEGLKGLVVPGTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 241 FEELGFYYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQKAAGGPPSY 320
Cdd:COG1154   241 FEELGFKYIGPIDGHDLDALVETLRNAKDL-KGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSY 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 321 TKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYD 400
Cdd:COG1154   320 TDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 401 QVVHDVAIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIdDRPSAFRYPRGEG 480
Cdd:COG1154   400 QVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIRYPRGNG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 481 LGLDMPAIAEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIIT 560
Cdd:COG1154   479 PGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVT 558

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1601858065 561 VEEGS-MGGFGAFVLQALAQHGALdrgLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILRGALSAMG 627
Cdd:COG1154   559 VEEGVlAGGFGSAVLEFLADAGLD---VPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
 
Name Accession Description Interval E-value
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 4-627 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: 1092.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   4 KTPLLDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHK 83
Cdd:COG1154     1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  84 ILTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNA 163
Cdd:COG1154    81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 164 ATDTTKRLIVILNDNDMSIAPPVGGMSAYLANLVSGGAYRSVRKLGKTVVEKLP---TPMREAARKAEEYARGMVTGGTF 240
Cdd:COG1154   161 AGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPgigPPLYELARRAKEGLKGLVVPGTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 241 FEELGFYYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQKAAGGPPSY 320
Cdd:COG1154   241 FEELGFKYIGPIDGHDLDALVETLRNAKDL-KGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSY 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 321 TKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYD 400
Cdd:COG1154   320 TDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 401 QVVHDVAIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIdDRPSAFRYPRGEG 480
Cdd:COG1154   400 QVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIRYPRGNG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 481 LGLDMPAIAEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIIT 560
Cdd:COG1154   479 PGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVT 558

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1601858065 561 VEEGS-MGGFGAFVLQALAQHGALdrgLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILRGALSAMG 627
Cdd:COG1154   559 VEEGVlAGGFGSAVLEFLADAGLD---VPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 2-620 0e+00

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 996.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   2 SSKTPLLDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYP 81
Cdd:PRK05444    1 IPKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  82 HKILTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKG-EDNSVIAVIGDGSLGAGMAYEA 160
Cdd:PRK05444   81 HKILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGgEDRKVVAVIGDGALTGGMAFEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 161 MNAATDTTKRLIVILNDNDMSIAPPVGGMSAYLANLVSGgayrsvrklgktvveklptpmreaarkaeeyargmvtggTF 240
Cdd:PRK05444  161 LNNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRSS---------------------------------------TL 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 241 FEELGFYYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQKAAG-GPPS 319
Cdd:PRK05444  202 FEELGFNYIGPIDGHDLDALIETLKNAKDL-KGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKSSKpGKPS 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 320 YTKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGY 399
Cdd:PRK05444  281 YTKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAY 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 400 DQVVHDVAIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPSAFRYPRGE 479
Cdd:PRK05444  361 DQVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGN 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 480 GLGLDMPAIaEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAarglSATVCDARFAKPLDLDLLLRLAREHEAII 559
Cdd:PRK05444  441 GVGVELPEL-EPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVV 515

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1601858065 560 TVEEGS-MGGFGAFVLQALAQHGALDrglKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILR 620
Cdd:PRK05444  516 TVEEGAiMGGFGSAVLEFLADHGLDV---PVLNLGLPDEFIDHGSREELLAELGLDAEGIAR 574
dxs TIGR00204
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ...
 8-627 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: 742.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   8 LDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHKILTG 87
Cdd:TIGR00204   1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  88 RRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNAATDT 167
Cdd:TIGR00204  81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 168 TKRLIVILNDNDMSIAPPVGGMSAYLANLVSGGAYRSVRKLGKTVVEKLPTPMREAARKAEEYARGMVTGGTFFEELGFY 247
Cdd:TIGR00204 161 KTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYLAKRTEESMKGLVVPGTFFEELGFN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 248 YIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQKAAGGPPSYTKVFAQE 327
Cdd:TIGR00204 241 YIGPVDGHDLLELIETLKNAKKL-KGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSALPSYSKIFSDT 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 328 LIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYDQVVHDVA 407
Cdd:TIGR00204 320 LCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVC 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 408 IQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPSAFRYPRGEGLGLDMPA 487
Cdd:TIGR00204 400 IQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVGVELTP 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 488 IAEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIITVEEGS-M 566
Cdd:TIGR00204 480 EPEKLPIGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVEENAiM 559

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1601858065 567 GGFGAFVLQALAQHGALdrgLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILRGALSAMG 627
Cdd:TIGR00204 560 GGAGSAVLEFLMDQNKL---VPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
DXP_synthase_N pfam13292
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ...
 8-281 3.35e-178

1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).


Pssm-ID: 463832 [Multi-domain]  Cd Length: 274  Bit Score: 506.17  E-value: 3.35e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   8 LDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHKILTG 87
Cdd:pfam13292   1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  88 RRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNAATDT 167
Cdd:pfam13292  81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 168 TKRLIVILNDNDMSIAPPVGGMSAYLANLVSGGAYRSVRKLGKTVVE-KLPTPMREAARKAEEYARGMVTGGTFFEELGF 246
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLKpKIGPPLYELARRAKESLKGLVVPGTLFEELGF 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1601858065 247 YYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVT 281
Cdd:pfam13292 241 KYIGPIDGHDLDALVKVLENAKDL-KGPVLLHVVT 274
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
 44-287 5.21e-114

Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).


Pssm-ID: 238965 [Multi-domain]  Cd Length: 195  Bit Score: 339.14  E-value: 5.21e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  44 GGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHKILTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATS 123
Cdd:cd02007     1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 124 ISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNAATDTTKRLIVILNDNDMSIAPPVGgmsaylanlvsggayr 203
Cdd:cd02007    81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 204 svrklgktvveklptpmreaarkaeeyargmvTGGTFFEELGFYYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQK 283
Cdd:cd02007   145 --------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDL-KGPVLLHVVTKK 191


                  ....
gi 1601858065 284 GKGY 287
Cdd:cd02007   192 GKGY 195
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 352-482 1.04e-41

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: 147.63  E-value: 1.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  352 DLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYDQVVHDVAIQGLPVRFAMDRAGLVGADGPTHA 431
Cdd:smart00861   7 KAFGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHH 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1601858065  432 GSFDIGFMGALPGMVLMAAADEVELARMVATAAEiDDRPSAFRYPRGEGLG 482
Cdd:smart00861  87 SIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSLYR 136
 
Name Accession Description Interval E-value
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 4-627 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: 1092.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   4 KTPLLDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHK 83
Cdd:COG1154     1 MTPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLASNLGVVELTVALHYVFDTPKDKLVWDVGHQAYPHK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  84 ILTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNA 163
Cdd:COG1154    81 ILTGRRDRFDTLRQYGGLSGFPKRSESEYDAFGAGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 164 ATDTTKRLIVILNDNDMSIAPPVGGMSAYLANLVSGGAYRSVRKLGKTVVEKLP---TPMREAARKAEEYARGMVTGGTF 240
Cdd:COG1154   161 AGHLKKDLIVILNDNEMSISPNVGALSNYLARLRTSPTYNKLREEVKKLLKKLPgigPPLYELARRAKEGLKGLVVPGTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 241 FEELGFYYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQKAAGGPPSY 320
Cdd:COG1154   241 FEELGFKYIGPIDGHDLDALVETLRNAKDL-KGPVLLHVVTKKGKGYAPAEKDPDKFHGVGPFDPETGEPKKSKSSAPSY 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 321 TKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYD 400
Cdd:COG1154   320 TDVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAYD 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 401 QVVHDVAIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIdDRPSAFRYPRGEG 480
Cdd:COG1154   400 QVIHDVALQNLPVTFAIDRAGLVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIRYPRGNG 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 481 LGLDMPAIAEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIIT 560
Cdd:COG1154   479 PGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVT 558

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1601858065 561 VEEGS-MGGFGAFVLQALAQHGALdrgLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILRGALSAMG 627
Cdd:COG1154   559 VEEGVlAGGFGSAVLEFLADAGLD---VPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 2-620 0e+00

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 996.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   2 SSKTPLLDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYP 81
Cdd:PRK05444    1 IPKYPLLDTINSPADLKKLSEEELPQLADEIREFLIDVVSKTGGHLGSNLGVVELTVALHYVFDTPKDRIIWDVGHQAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  82 HKILTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKG-EDNSVIAVIGDGSLGAGMAYEA 160
Cdd:PRK05444   81 HKILTGRRDRFDTLRQKGGLSGFPKRSESEYDTFGAGHSSTSISAALGMAKARDLKGgEDRKVVAVIGDGALTGGMAFEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 161 MNAATDTTKRLIVILNDNDMSIAPPVGGMSAYLANLVSGgayrsvrklgktvveklptpmreaarkaeeyargmvtggTF 240
Cdd:PRK05444  161 LNNAGDLKSDLIVILNDNEMSISPNVGALSNYLARLRSS---------------------------------------TL 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 241 FEELGFYYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQKAAG-GPPS 319
Cdd:PRK05444  202 FEELGFNYIGPIDGHDLDALIETLKNAKDL-KGPVLLHVVTKKGKGYAPAEADPIKYHGVGKFDPETGEQPKSSKpGKPS 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 320 YTKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGY 399
Cdd:PRK05444  281 YTKVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQRAY 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 400 DQVVHDVAIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPSAFRYPRGE 479
Cdd:PRK05444  361 DQVIHDVALQNLPVTFAIDRAGLVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGN 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 480 GLGLDMPAIaEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAarglSATVCDARFAKPLDLDLLLRLAREHEAII 559
Cdd:PRK05444  441 GVGVELPEL-EPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVV 515

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1601858065 560 TVEEGS-MGGFGAFVLQALAQHGALDrglKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILR 620
Cdd:PRK05444  516 TVEEGAiMGGFGSAVLEFLADHGLDV---PVLNLGLPDEFIDHGSREELLAELGLDAEGIAR 574
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 3-629 0e+00

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 952.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   3 SKTPLLDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPH 82
Cdd:PRK12571    4 PKTPLLDRIKGPADLRALSDAELEQLADELRAEVISAVSETGGHLGSSLGVVELTVALHAVFNTPKDKLVWDVGHQCYPH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  83 KILTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMN 162
Cdd:PRK12571   84 KILTGRRDRFRTLRQKGGLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYEALN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 163 AATDTTKRLIVILNDNDMSIAPPVGGMSAYLANLVSGGAYRSVRKLGKTVVEKLPTPMREAARKAEEYARGMVTGGTFFE 242
Cdd:PRK12571  164 NAGAADRRLIVILNDNEMSIAPPVGALAAYLSTLRSSDPFARLRAIAKGVEERLPGPLRDGARRARELVTGMIGGGTLFE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 243 ELGFYYIGPIDGHDMDALVSVLKNAKAFGDKPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQKAAGGPPSYTK 322
Cdd:PRK12571  244 ELGFTYVGPIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEADEDKYHAVGKFDVVTGLQKKSAPSAPSYTS 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 323 VFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYDQV 402
Cdd:PRK12571  324 VFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQRGYDQL 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 403 VHDVAIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPSAFRYPRGEGLG 482
Cdd:PRK12571  404 LHDVALQNLPVRFVLDRAGLVGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVG 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 483 LDMPAIAEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIITVE 562
Cdd:PRK12571  484 VEIPAEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHIVVIVEE 563

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601858065 563 EGSMGGFGAFVLQALAQHGALDRGLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILRGALSAMGMD 629
Cdd:PRK12571  564 QGAMGGFGAHVLHHLADTGLLDGGLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALARL 630
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 5-627 0e+00

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 777.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   5 TPLLDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHKI 84
Cdd:PLN02582   31 TPLLDTINYPIHMKNLSVKELKQLADELRSDVIFNVSKTGGHLGSSLGVVELTVALHYVFNAPQDKILWDVGHQSYPHKI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  85 LTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNAA 164
Cdd:PLN02582  111 LTGRRDKMHTMRQTNGLSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 165 TDTTKRLIVILNDN-DMSI--------APPVGGMSAYLANLVSGGAYRSVRKLGKTVVEKLPTPMREAARKAEEYARGMV 235
Cdd:PLN02582  191 GYLDSDMIVILNDNkQVSLptatldgpAPPVGALSSALSRLQSSRPLRELREVAKGVTKQIGGPMHELAAKVDEYARGMI 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 236 --TGGTFFEELGFYYIGPIDGHDMDALVSVLKNAKAFGDK-PVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQK 312
Cdd:PLN02582  271 sgSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKTTgPVLIHVVTEKGRGYPYAERAADKYHGVVKFDPATGKQFK 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 313 AAGGPPSYTKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYS 392
Cdd:PLN02582  351 VKAKTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYS 430

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 393 TFLQRGYDQVVHDVAIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPSA 472
Cdd:PLN02582  431 SFLQRGYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIDDRPSC 510

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 473 FRYPRGEGLGLDMPAIAE--PLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLR 550
Cdd:PLN02582  511 FRYPRGNGIGVQLPPNNKgiPIEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRS 590

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601858065 551 LAREHEAIITVEEGSMGGFGAFVLQALAQHGALDRGLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILRGALSAMG 627
Cdd:PLN02582  591 LAKSHEVLITVEEGSIGGFGSHVAQFMALDGLLDGKLKWRPLVLPDRYIDHGAPADQLAEAGLTPSHIAATVLNVLG 667
dxs TIGR00204
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ...
 8-627 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: 742.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   8 LDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHKILTG 87
Cdd:TIGR00204   1 LSLINSPQELRLLSIDELEKLCDELRRYLLESVSASGGHLASGLGTVELTVALHYVFNTPKDQFIWDVGHQAYPHKLLTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  88 RRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNAATDT 167
Cdd:TIGR00204  81 RREKFSTLRQKKGLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGADRKTVCVIGDGAITAGMAFEALNHAGDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 168 TKRLIVILNDNDMSIAPPVGGMSAYLANLVSGGAYRSVRKLGKTVVEKLPTPMREAARKAEEYARGMVTGGTFFEELGFY 247
Cdd:TIGR00204 161 KTDMIVILNDNEMSISENVGALSNHLAQLRSGSLYQSLRDGLKKIFSKLPPIKNYLAKRTEESMKGLVVPGTFFEELGFN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 248 YIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQKAAGGPPSYTKVFAQE 327
Cdd:TIGR00204 241 YIGPVDGHDLLELIETLKNAKKL-KGPVFLHIQTKKGKGYKPAEKDPIGWHGVGPFDLSTGCLPKSKSALPSYSKIFSDT 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 328 LIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYDQVVHDVA 407
Cdd:TIGR00204 320 LCELAKKDNKIVGITPAMPEGSGLDKFSRKFPDRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYSTFLQRAYDQVVHDVC 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 408 IQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPSAFRYPRGEGLGLDMPA 487
Cdd:TIGR00204 400 IQKLPVLFAIDRAGIVGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVGVELTP 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 488 IAEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIITVEEGS-M 566
Cdd:TIGR00204 480 EPEKLPIGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVEENAiM 559

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1601858065 567 GGFGAFVLQALAQHGALdrgLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILRGALSAMG 627
Cdd:TIGR00204 560 GGAGSAVLEFLMDQNKL---VPVKRLGIPDFFIPHGTQEEVLAELGLDTAGMEAKILAWLA 617
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 5-589 0e+00

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 614.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   5 TPLLDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHKI 84
Cdd:PLN02234   64 TPLLDTINHPMHMKNLSIKELKVLSDELRSDVIFNVSKTGGHLGSNLGVVELTVALHYIFNTPHDKILWDVGHQSYPHKI 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  85 LTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNAA 164
Cdd:PLN02234  144 LTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNA 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 165 TDTTKRLIVILNDNDM---------SIAPPVGGMSAYLANLVSGGAYRSVrklgktvveklptpmreaarkaeeyargmv 235
Cdd:PLN02234  224 GYLHSNMIVILNDNKQvslptanldGPTQPVGALSCALSRLQSNCGMIRE------------------------------ 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 236 TGGTFFEELGFYYIGPIDGHDMDALVSVL---KNAKAFGdkPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQK 312
Cdd:PLN02234  274 TSSTLFEELGFHYVGPVDGHNIDDLVSILetlKSTKTIG--PVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQFK 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 313 AAGGPPSYTKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYS 392
Cdd:PLN02234  352 NISKTQSYTSCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 393 TFLQRGYDQVVHDVAIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPSA 472
Cdd:PLN02234  432 SFMQRAYDQVVHDVDLQKLPVRFAIDRAGLMGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSC 511

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 473 FRYPRGEGLGLDMPAIAE--PLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLR 550
Cdd:PLN02234  512 FRYHRGNGIGVSLPPGNKgvPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRS 591

                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 1601858065 551 LAREHEAIITVEEGSMGGFGAFVLQALAQHGALDRGLKI 589
Cdd:PLN02234  592 LAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKV 630
DXP_synthase_N pfam13292
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ...
 8-281 3.35e-178

1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).


Pssm-ID: 463832 [Multi-domain]  Cd Length: 274  Bit Score: 506.17  E-value: 3.35e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   8 LDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHKILTG 87
Cdd:pfam13292   1 LDKINSPADLKKLSEEELPQLAEEIREFLIESVSKTGGHLASNLGVVELTLALHYVFDTPKDKIVWDVGHQAYVHKILTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  88 RRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNAATDT 167
Cdd:pfam13292  81 RRDRFHTLRQYGGLSGFPKRSESEYDAFGTGHSSTSISAALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 168 TKRLIVILNDNDMSIAPPVGGMSAYLANLVSGGAYRSVRKLGKTVVE-KLPTPMREAARKAEEYARGMVTGGTFFEELGF 246
Cdd:pfam13292 161 KKDLIVILNDNEMSISPNVGALSNYLSRLRTSPTYNRLKEEVKKLLKpKIGPPLYELARRAKESLKGLVVPGTLFEELGF 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1601858065 247 YYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVT 281
Cdd:pfam13292 241 KYIGPIDGHDLDALVKVLENAKDL-KGPVLLHVVT 274
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
 4-627 7.06e-165

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 488.46  E-value: 7.06e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   4 KTPLLDTIASPADTRGLSLAELKQLAAEVRAETIDAV-SVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPH 82
Cdd:PLN02225   75 ETPILDSIETPLQLKNLSVKELKLLADEIRTELHSVLwKKTQKSMNPSFAAIELTLALHYVFRAPVDNILWDAVEQTYAH 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  83 KILTGRRDRIRTlRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMN 162
Cdd:PLN02225  155 KVLTRRWSAIPS-RQKNGISGVTSQLESEYDSFGTGHGCNSISAGLGLAVARDIKGKRDRVVAVIDNATITAGQAYEAMS 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 163 AATDTTKRLIVILNDNDMSIAP--------PVGGMSAYLANLVSGGAYRSVRKLGKTVVEKLPTPMREAARKAEEYARGM 234
Cdd:PLN02225  234 NAGYLDSNMIVILNDSRHSLHPnmeegskaSISALSSIMSKIQSSKIFRKFRELAKAMTKRIGKGMYEWAAKVDEYARGM 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 235 V--TGGTFFEELGFYYIGPIDGHDMDALVSVLKNAKAFGDK-PVLVHCVTQKGKgyapaegaadklhavvkfDVVTGQQQ 311
Cdd:PLN02225  314 VgpTGSTLFEELGLYYIGPVDGHNIEDLVCVLREVSSLDSMgPVLVHVITEENR------------------DAETGKNI 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 312 KAAGgPPSYTKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIY 391
Cdd:PLN02225  376 MVKD-RRTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIP 454

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 392 STFLQRGYDQVVHDVAIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPS 471
Cdd:PLN02225  455 SAFLQRAYDQVVHDVDRQRKAVRFVITSAGLVGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDRPV 534

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 472 AFRYPRGEGLGLD-MPAIAEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLR 550
Cdd:PLN02225  535 CFRFPRGSIVNMNyLVPTGLPIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRD 614

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601858065 551 LAREHEAIITVEEGSMGGFGAFVLQALAQHGALDRGLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILRGALSAMG 627
Cdd:PLN02225  615 LCQNHKFLITVEEGCVGGFGSHVAQFIALDGQLDGNIKWRPIVLPDGYIEEASPREQLALAGLTGHHIAATALSLLG 691
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 6-618 4.04e-161

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 474.49  E-value: 4.04e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065   6 PLLDTIASPADTRGLSLAELKQLAAEVRAETIDAVSVTGGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHKIL 85
Cdd:PRK12315    1 MYLEKINSPADLKKLSLDELEQLASEIRTALLEKDSAHGGHVGPNLGVVELTIALHYVFNSPKDKIVWDVSHQSYPHKML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  86 TGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATSISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNAAT 165
Cdd:PRK12315   81 TGRKEAFLDPDHYDDVTGYTNPEESEHDFFTVGHTSTSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 166 DTTKRLIVILNDNDMSIAPPVGGMsaylanlvsggaYRSVRKLgktvveklptpmREAARKAEEyargmvtggTFFEELG 245
Cdd:PRK12315  161 ELKSNLIIIVNDNQMSIAENHGGL------------YKNLKEL------------RDTNGQSEN---------NLFKAMG 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 246 FYYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQKGKGYAPAEGAADKLHAVVKFDVVTGQQQKAAGGPpSYTKVFA 325
Cdd:PRK12315  208 LDYRYVEDGNDIESLIEAFKEVKDI-DHPIVLHIHTLKGKGYQPAEENKEAFHWHMPFDLETGQSKVPASGE-SYSSVTL 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 326 QELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYDQVVHD 405
Cdd:PRK12315  286 DYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQRAYDQLSHD 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 406 VAIQGLPVRFaMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPSAFRYPrgeglglDM 485
Cdd:PRK12315  366 LAINNNPAVM-IVFGGSISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAIRVP-------EH 437

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 486 PAIAEPLEIG-----KGRIVREGTSVAIVSFGTRLSESLKAADLLAAR-GLSATVCDARFAKPLDLDLLLRLAREHEAII 559
Cdd:PRK12315  438 GVESGPTVDTdystlKYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEELLEKLKEDHELVV 517

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 560 TVEEGSM-GGFGAFVLQALAqhgalDRGLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGI 618
Cdd:PRK12315  518 TLEDGILdGGFGEKIARYYG-----NSDMKVLNYGAKKEFNDRVPVEELYKRNHLTPEQI 572
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
 44-287 5.21e-114

Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).


Pssm-ID: 238965 [Multi-domain]  Cd Length: 195  Bit Score: 339.14  E-value: 5.21e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  44 GGHLGAGLGVVELTVALHHVFETPKDIVIWDVGHQAYPHKILTGRRDRIRTLRQGGGLSGFTKRAESEYDPFGAAHAATS 123
Cdd:cd02007     1 GGHLGSNLGVVELTLALHYVFDSPKDKIIWDVGHQAYPHKILTGRRDQFHTLRQYGGLSGFTKRSESEYDAFGTGHSSTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 124 ISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEAMNAATDTTKRLIVILNDNDMSIAPPVGgmsaylanlvsggayr 203
Cdd:cd02007    81 ISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNEMSISPNVG---------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 204 svrklgktvveklptpmreaarkaeeyargmvTGGTFFEELGFYYIGPIDGHDMDALVSVLKNAKAFgDKPVLVHCVTQK 283
Cdd:cd02007   145 --------------------------------TPGNLFEELGFRYIGPVDGHNIEALIKVLKEVKDL-KGPVLLHVVTKK 191


                  ....
gi 1601858065 284 GKGY 287
Cdd:cd02007   192 GKGY 195
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
322-626 2.90e-72

Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 235.37  E-value: 2.90e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 322 KVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFL-QRGYD 400
Cdd:COG3958     8 DAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLtGRAYE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 401 QVVHDVAIQGLPVRFAMDRAGL-VGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDrPSAFRYPRGE 479
Cdd:COG3958    88 QIRNDIAYPNLNVKIVGSHAGLsYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDG-PVYLRLGRGA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 480 glgldMPAI---AEPLEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHE 556
Cdd:COG3958   167 -----VPVVydeDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTG 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1601858065 557 AIITVEEGS-MGGFGAFVLQALAQHGAldrgLKIRTLCLPDVFQDQDKPDAMYAQAGLDAEGILRGALSAM 626
Cdd:COG3958   242 AVVTAEEHSiIGGLGSAVAEVLAENYP----VPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
 322-477 7.03e-70

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: 223.47  E-value: 7.03e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 322 KVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYDQ 401
Cdd:cd07033     1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFFLQRAYDQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601858065 402 VVHDVAIQGLPVRFAMDRAGL-VGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDrPSAFRYPR 477
Cdd:cd07033    81 IRHDVALQNLPVKFVGTHAGIsVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDG-PVYIRLPR 156
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
 317-479 4.73e-45

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: 158.10  E-value: 4.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 317 PPSYTKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPE---RTFDVGIAEQHAVTFAAGMAADG--MKPFAAIY 391
Cdd:pfam02779   2 KIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEATF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 392 STFLQRGYDQVVHDVAIQGLPVRFAMDRAGL-VGADGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDR- 469
Cdd:pfam02779  82 SDFLNRADDAIRHGAALGKLPVPFVVTRDPIgVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGRk 161

                         170
                  ....*....|
gi 1601858065 470 PSAFRYPRGE 479
Cdd:pfam02779 162 PVVLRLPRQL 171
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
 352-482 1.04e-41

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: 147.63  E-value: 1.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  352 DLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYSTFLQRGYDQVVHDVAIQGLPVRFAMDRAGLVGADGPTHA 431
Cdd:smart00861   7 KAFGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHH 86

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1601858065  432 GSFDIGFMGALPGMVLMAAADEVELARMVATAAEiDDRPSAFRYPRGEGLG 482
Cdd:smart00861  87 SIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSLYR 136
PRK05899 PRK05899
transketolase; Reviewed
 21-624 8.40e-34

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 136.42  E-value: 8.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  21 SLAELKQLAAEVRAETIDAVSVTG-GHLGAGLGVVELTVAL-----HHVFETPKDI----VIWDVGHQA---YPHKILTG 87
Cdd:PRK05899    4 DMELLQLLANAIRVLSIDAVQKANsGHPGMPMGAADIAYVLwtrflRHDPKNPKWPnrdrFVLSAGHGSmllYSLLHLAG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  88 ---RRDRIRTLRQGGglsgftkraeS------EYDPFGAAHAATS-----ISAALGFC-AARDAKGEDNSVIAVI----- 147
Cdd:PRK05899   84 ydlSIDDLKNFRQLG----------SktpghpEYGHTPGVETTTGplgqgLANAVGMAlAEKYLAALFNRPGLDIvdhyt 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 148 ----GDGSLGAGMAYEAMN-AATDTTKRLIVILNDNDMSIAPPVGGmsAYLANLvsggayrsvrklgktvveklptpmre 222
Cdd:PRK05899  154 yvlcGDGDLMEGISHEACSlAGHLKLGNLIVIYDDNRISIDGPTEG--WFTEDV-------------------------- 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 223 AARkaeeyargmvtggtfFEELGFYYIgPIDGHDMDALVSVLKNAKAfGDKPVLVHCVTQKGKGYAPAEGAAdKLH-AVV 301
Cdd:PRK05899  206 KKR---------------FEAYGWHVI-EVDGHDVEAIDAAIEEAKA-STKPTLIIAKTIIGKGAPNKEGTH-KVHgAPL 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 302 KFDVVTgQQQKAAGGPPSytKVFAQELIKQAEKDDKIVAITAAMPSGTGLDLFG------KAFPERTFDVGIAEQHAVTF 375
Cdd:PRK05899  268 GAEEIA-AAKKELGWDYR--KASGKALNALAKALPELVGGSADLAGSNNTKIKGskdfapEDYSGRYIHYGVREFAMAAI 344

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 376 AAGMAADGM-KPFAAIYSTFLQRGYDQvVHDVAIQGLPVRFAMDRAGL-VGADGPTHAGSFDIGFMGALPGMVLMAAADE 453
Cdd:PRK05899  345 ANGLALHGGfIPFGGTFLVFSDYARNA-IRLAALMKLPVIYVFTHDSIgVGEDGPTHQPVEQLASLRAIPNLTVIRPADA 423

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 454 VELARMVATAAEIDDRPSAFRYPRGeglglDMPAIAEPLEIGK----GRIVREGTSVAIVSFGTRLSESLKAADLLAARG 529
Cdd:PRK05899  424 NETAAAWKYALERKDGPSALVLTRQ-----NLPVLERTAQEEGvakgGYVLRDDPDVILIATGSEVHLALEAADELEAEG 498

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 530 LSATV----CDARFAKPLDLDLLLRLAREHEAIITVEEGSMGGFGAFVlqalaqhgaldrGLKIRTLCLpDVFQDQDKPD 605
Cdd:PRK05899  499 IKVRVvsmpSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYV------------GLDGKVLGI-DTFGASAPAD 565

                         650
                  ....*....|....*....
gi 1601858065 606 AMYAQAGLDAEGILRGALS 624
Cdd:PRK05899  566 ELFKEFGFTVENIVAAAKE 584
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 495-618 1.53e-26

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: 104.60  E-value: 1.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 495 GKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIITVEEGS-MGGFGAFV 573
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVpRGGFGSEV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1601858065 574 LQALAQHGALDRGLKIRTLCLPDvFQDQDKPDAMYAQAGLDAEGI 618
Cdd:pfam02780  81 AAALAEEAFDGLDAPVLRVGGPD-FPEPGSADELEKLYGLTPEKI 124
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
 351-571 1.51e-19

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 90.43  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 351 LDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAI-YSTFLQRGYDQVVHDVA--------IQGLPVRFamdRA- 420
Cdd:PTZ00182   73 KGLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFmFADFIFPAFDQIVNEAAkyrymsggQFDCPIVI---RGp 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 421 -GLVGADGPTHAGSFDIGFMGAlPGMVLMAAADEVElARMVATAAEIDDRPSAFRYPRG-EGLGLDMPAIAE-PLEIGKG 497
Cdd:PTZ00182  150 nGAVGHGGAYHSQSFEAYFAHV-PGLKVVAPSDPED-AKGLLKAAIRDPNPVVFFEPKLlYRESVEVVPEADyTLPLGKA 227

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1601858065 498 RIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIITVEEGSM-GGFGA 571
Cdd:PTZ00182  228 KVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPtCGIGA 302
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
 328-477 1.75e-18

Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.


Pssm-ID: 132915 [Multi-domain]  Cd Length: 154  Bit Score: 82.78  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 328 LIKQAEKDDKIVAITAAMPSGTGLDLFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIY-STFLQRGYDQVVhDV 406
Cdd:cd06586     3 FAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTsGTGLLNAINGLA-DA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1601858065 407 AIQGLPVRFAMDRAGLVGADGPTHAGSFDIGFMGALPGMVLMAAADEvELARMVATAAEIDD---RPSAFRYPR 477
Cdd:cd06586    82 AAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPA-ELPAGIDHAIRTAYasqGPVVVRLPR 154
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
 351-584 6.00e-16

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 79.38  E-value: 6.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 351 LDLFGkafPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYS-TFLQRGYDQVVHDVAIQ--------GLPVRF--AMDR 419
Cdd:PRK09212   45 LEQFG---PKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFMTfNFSMQAIDQIVNSAAKTnymsggqlKCPIVFrgPNGA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 420 AGLVGADgptHAGSFDiGFMGALPGMVLMA---AADevelARMVATAAEIDDRPSAF-RYPRGEGLGLDMPAIAEPLEIG 495
Cdd:PRK09212  122 AARVAAQ---HSQCYA-AWYSHIPGLKVVApyfAAD----CKGLLKTAIRDPNPVIFlENEILYGHSHEVPEEEESIPIG 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 496 KGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIITVEEG-SMGGFGAFVl 574
Cdd:PRK09212  194 KAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKTNRLVVVEEGwPFAGVGAEI- 272

                         250
                  ....*....|
gi 1601858065 575 QALAQHGALD 584
Cdd:PRK09212  273 AALIMKEAFD 282
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
 31-292 1.55e-15

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: 76.77  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  31 EVRAETIDAVSVTG-GHLGAGLGVVELTVAL-----HHVFETPK----DIVIWDVGHQA---YPHKILTG--RRDRIRTL 95
Cdd:cd02012     2 RIRRLSIDMVQKAGsGHPGGSLSAADILAVLyfkvlKYDPADPKwpnrDRFVLSKGHASpalYAVLALAGylPEEDLKTF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  96 RQGGG-LSGFTkraesEYDPFGAAHAATS-----ISAALGFCAARDAKGEDNSVIAVIGDGSLGAGMAYEA-MNAATDTT 168
Cdd:cd02012    82 RQLGSrLPGHP-----EYGLTPGVEVTTGslgqgLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAaSFAGHYKL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 169 KRLIVILNDNDMSIappvGGMSAYLANLVsggayrsvrklgktvveklPTPMReaarkaeeyargmvtggtfFEELGFYY 248
Cdd:cd02012   157 DNLIAIVDSNRIQI----DGPTDDILFTE-------------------DLAKK-------------------FEAFGWNV 194

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1601858065 249 IgPIDGHDMDALVSVLKNAKAFGDKPVLVHCVTQKGKGYAPAEG 292
Cdd:cd02012   195 I-EVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMEN 237
TktA1 COG3959
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
21-286 3.29e-13

Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443159 [Multi-domain]  Cd Length: 277  Bit Score: 70.49  E-value: 3.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  21 SLAELKQLAAEVRAETIDAVSVTG-GHLGAGLGVVELTVAL-HHVF----ETPK----DIVIWDVGHQA---YPHKILTG 87
Cdd:COG3959     4 DIKELEEKARQIRRDILRMIYAAGsGHPGGSLSAADILAALyFKVMnidpKNPDwpdrDRFILSKGHAApalYAVLAEKG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  88 R--RDRIRTLRQGGG-LSGftkraeseydpfgaaHAATS---------------ISAALGFCAARDAKGEDNSVIAVIGD 149
Cdd:COG3959    84 YfpKEELATFRKLGSrLQG---------------HPDMKktpgvemstgslgqgLSVAVGMALAAKLDGKDYRVYVLLGD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 150 GSLGAGMAYEAMNAAT----DttkRLIVILNDNDMSIappvggmsaylanlvsGGAYRSVRKLGktvveklptPMREaar 225
Cdd:COG3959   149 GELQEGQVWEAAMAAAhyklD---NLIAIVDRNGLQI----------------DGPTEDVMSLE---------PLAE--- 197

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1601858065 226 KaeeyargmvtggtfFEELGFYYIgPIDGHDMDALVSVLKNAKAFGDKPVLVHCVTQKGKG 286
Cdd:COG3959   198 K--------------WEAFGWHVI-EVDGHDIEALLAALDEAKAVKGKPTVIIAHTVKGKG 243
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
 353-604 1.25e-12

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 69.46  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 353 LFGKAFPERTFDVGIAEQHAVTFAAGMAADGMKPFAAIYS-TFLQRGYDQVVHDVAIQ--------GLPVRFAMDRAGLV 423
Cdd:PLN02683   67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTfNFSMQAIDHIINSAAKTnymsagqiSVPIVFRGPNGAAA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 424 GAdGPTHAGSFdIGFMGALPGMVLMAAADEvELARMVATAAEIDDRPSAFRypRGEGL-GLDMPAIAEPLE------IGK 496
Cdd:PLN02683  147 GV-GAQHSQCF-AAWYSSVPGLKVLAPYSS-EDARGLLKAAIRDPDPVVFL--ENELLyGESFPVSAEVLDssfvlpIGK 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 497 GRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIITVEEGsmggfgafvlqa 576
Cdd:PLN02683  222 AKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEG------------ 289

                         250       260
                  ....*....|....*....|....*...
gi 1601858065 577 LAQHGAldrGLKIRTLCLPDVFQDQDKP 604
Cdd:PLN02683  290 WPQHGV---GAEICASVVEESFDYLDAP 314
PLN02790 PLN02790
transketolase
 124-573 3.40e-10

transketolase


Pssm-ID: 215424 [Multi-domain]  Cd Length: 654  Bit Score: 63.12  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 124 ISAALGFC------AAR----DAKGEDNSVIAVIGDGSLGAGMAYEAMN-AATDTTKRLIVILNDNDMSIappvGGMSAY 192
Cdd:PLN02790  111 IANAVGLAlaekhlAARfnkpDHKIVDHYTYCILGDGCQMEGISNEAASlAGHWGLGKLIVLYDDNHISI----DGDTEI 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 193 lanlvsggayrsvrklgkTVVEKLptpmreAARkaeeyargmvtggtfFEELGFYYIGPIDG-HDMDALVSVLKNAKAFG 271
Cdd:PLN02790  187 ------------------AFTEDV------DKR---------------YEALGWHTIWVKNGnTDYDEIRAAIKEAKAVT 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 272 DKPVLVHCVTQKGKG-------YApAEGAA------DKLHAVVK-----FDVV-------TGQQQKAAGGPPSYTKVFAQ 326
Cdd:PLN02790  228 DKPTLIKVTTTIGYGspnkansYS-VHGAAlgekevDATRKNLGwpyepFHVPedvkshwSKHTKEGAALEAEWNAKFAE 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 327 ------------------ELIKQAEK-------DDKIVA-----------ITAAMPS--GTGLDL-------------FG 355
Cdd:PLN02790  307 ykkkypeeaaelkslisgELPSGWEKalptftpEDPADAtrnlsqkclnaLAKVLPGliGGSADLassnmtllkdfgdFQ 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 356 KAFP-ERTFDVGIAEQHAVTFAAGMAA--DGMKPFAAiysTFLQ-----RGYDQVVhdvAIQGLPVRFAM--DRAGLvGA 425
Cdd:PLN02790  387 KDTPeERNVRFGVREHGMGAICNGIALhsSGLIPYCA---TFFVftdymRAAMRLS---ALSEAGVIYVMthDSIGL-GE 459

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 426 DGPTHAGSFDIGFMGALPGMVLMAAADEVELARMVATAAEIDDRPSAFRYPRGEGLGLDMPAIAeplEIGKGRIVREGTS 505
Cdd:PLN02790  460 DGPTHQPIEHLASLRAMPNILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGTSIE---GVEKGGYVISDNS 536

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1601858065 506 ------VAIVSFGTRLSESLKAADLLAARGLSATV----CDARFAKPLDLDLLLRLAREHEAIITVEEGSMGGFGAFV 573
Cdd:PLN02790  537 sgnkpdLILIGTGSELEIAAKAAKELRKEGKKVRVvsmvCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYV 614
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
 492-581 3.92e-09

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 59.16  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 492 LEIGKGRIVREGTSVAIVSFGTRLSESLKAADLLAARGLSATVCDARFAKPLDLDLLLRLAREHEAIITVEEG-SMGGFG 570
Cdd:PRK11892  329 LPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEEGwPQSGVG 408

                          90
                  ....*....|.
gi 1601858065 571 AFVLQALAQHG 581
Cdd:PRK11892  409 AEIAARVMEQA 419
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
 26-295 2.05e-08

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: 56.24  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  26 KQLAAEVRAETIDAV-SVTGGHLGAGLGVVELTVAL-----HHVFETPK----DIVIWDVGHQA---YPHKILTG---RR 89
Cdd:pfam00456   3 KRAVNAIRALAMDAVeKANSGHPGAPMGMAPIAEVLfkrflKHNPNDPKwinrDRFVLSNGHGSmllYSLLHLTGydlSM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065  90 DRIRTLRQGGGLS------GFTKRAESEYDPFGAAHA-ATSISAALGFCAARDAKGE----DNSVIAVIGDGSLGAGMAY 158
Cdd:pfam00456  83 EDLKSFRQLGSKTpghpefGHTAGVEVTTGPLGQGIAnAVGMAIAERNLAATYNRPGfdivDHYTYVFLGDGCLMEGVSS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 159 EAMN-AATDTTKRLIVILNDNDMSIAPPVGGmsaylanlvsggayrsvrklgkTVVEKlpTPMReaarkaeeyargmvtg 237
Cdd:pfam00456 163 EASSlAGHLGLGNLIVFYDDNQISIDGETKI----------------------SFTED--TAAR---------------- 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1601858065 238 gtfFEELGFYYIGPIDGHDMDALVSVLKNAKAFGDKPVLVHCVTQKGKGYAPAEGAAD 295
Cdd:pfam00456 203 ---FEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLIKCRTVIGYGSPNKQGTHD 257
TktA COG0021
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ...
 241-534 5.12e-06

Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439792 [Multi-domain]  Cd Length: 661  Bit Score: 49.62  E-value: 5.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 241 FEELGFYYIGPIDGHDMDALVSVLKNAKAFGDKPVLVHCVTQKGKGyAP-------AEGA---ADKLHAVVKF------- 303
Cdd:COG0021   205 FEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPTLIICKTIIGYG-SPnkqgtakAHGAplgAEEIAATKEAlgwppep 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 304 -----DVVT--------GQQQKAAggppsYTKVFAQ-------------------------ELIKQAEKDDKIVAITAAm 345
Cdd:COG0021   284 fevpdEVYAhwraagerGAAAEAE-----WNERFAAyaaaypelaaelerrlagelpedwdAALPAFEADAKGVATRKA- 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 346 pSGTGLDLFGKAFPE-----------------------------RTFDVGIAEqHAVTFAA-GMAADGM-KPFAAiysTF 394
Cdd:COG0021   358 -SGKVLNALAPVLPEliggsadlagsnkttikgagsfspedpsgRNIHFGVRE-HAMGAIMnGIALHGGlRPYGG---TF 432

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 395 LqrgydqvvhdV------------AIQGLPVRFAM--DRAGlVGADGPTH------AGsfdigfMGALPGMVLMAAADEV 454
Cdd:COG0021   433 L----------VfsdymrpairlaALMKLPVIYVFthDSIG-LGEDGPTHqpveqlAS------LRAIPNLDVIRPADAN 495

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 455 ELARMVATAAEIDDRPSAfryprgegLGL---DMPAI----AEPLEIGKG-RIVREGTS---VAIVSFGTRLSESLKAAD 523
Cdd:COG0021   496 ETAAAWKLALERKDGPTA--------LILsrqNLPTLdrtaAAAEGVAKGaYVLADAEGtpdVILIATGSEVSLAVEAAE 567

                         410
                  ....*....|.
gi 1601858065 524 LLAARGLSATV 534
Cdd:COG0021   568 LLAAEGIKVRV 578
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
 351-473 1.83e-05

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: 45.55  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 351 LDLFGkafPERTFDVGIAEQHAVTFAAGMAADGMKPFAAI-YSTFLQRGYDQVVHDVAIQ----------GLPVRFAMdr 419
Cdd:cd07036    38 LDKFG---PDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEImFADFALPAFDQIVNEAAKLrymsggqfkvPIVIRGPN-- 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1601858065 420 aGLVGADGPTHAGSFDiGFMGALPGMVLMAAADeVELARMVATAAEIDDRPSAF 473
Cdd:cd07036   113 -GGGIGGGAQHSQSLE-AWFAHIPGLKVVAPST-PYDAKGLLKAAIRDDDPVIF 163
PTZ00089 PTZ00089
transketolase; Provisional
 140-527 4.05e-05

transketolase; Provisional


Pssm-ID: 173383 [Multi-domain]  Cd Length: 661  Bit Score: 46.59  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 140 DNSVIAVIGDGSLGAGMAYEAMNAATD-TTKRLIVILNDNDMSIAppvggmsaylanlvsggayrsvrklGKTVVeklpT 218
Cdd:PTZ00089  148 DNYVYVICGDGCLQEGVSQEALSLAGHlGLEKLIVLYDDNKITID-------------------------GNTDL----S 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 219 PMREAARKaeeyargmvtggtfFEELGFYYIGPIDGH-DMDALVSVLKNAKAFGDKPVLVHCVTQKGKGyaPAEGAADKL 297
Cdd:PTZ00089  199 FTEDVEKK--------------YEAYGWHVIEVDNGNtDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYG--SSKAGTEKV 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 298 HAVVKFDVVTGQQQKAAGGPPS---------------------------------YTKVF---AQELIKQAEKD------ 335
Cdd:PTZ00089  263 HGAPLGDEDIAQVKELFGLDPEkkfhvseevrqffeqhvekkkenyeawkkrfakYTAAFpkeAQAIERRFKGElppgwe 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 336 -----------------------DKIVAITAAMPSGT------------GLDLFGKAFPE-RTFDVGIAEQHAVTFAAGM 379
Cdd:PTZ00089  343 kklpkyttndkaiatrkasenvlNPLFQILPELIGGSadltpsnltrpkEANDFTKASPEgRYIRFGVREHAMCAIMNGI 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601858065 380 AADG-MKPFAAiysTFLQ-RGYD-QVVHDVAIQGLPVRFAM--DRAGLvGADGPTHAGSFDIGFMGALPGMVLMAAADEV 454
Cdd:PTZ00089  423 AAHGgFIPFGA---TFLNfYGYAlGAVRLAALSHHPVIYVAthDSIGL-GEDGPTHQPVETLALLRATPNLLVIRPADGT 498

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601858065 455 ELARMVATAAEIDDRPSAFRYPRGeglGLDMPAIAEPLEIGKGR-IVREGT---SVAIVSFGTRLSESLKAADLLAA 527
Cdd:PTZ00089  499 ETSGAYALALANAKTPTILCLSRQ---NTPPLPGSSIEGVLKGAyIVVDFTnspQLILVASGSEVSLCVEAAKALSK 572
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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