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Conserved domains on  [gi|488978457|ref|WP_002889310|]
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MULTISPECIES: 1-deoxy-D-xylulose-5-phosphate reductoisomerase [Klebsiella]

Protein Classification

1-deoxy-D-xylulose-5-phosphate reductoisomerase( domain architecture ID 11432909)

1-deoxy-D-xylulose-5-phosphate reductoisomerase catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dxr COG0743
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
1-396 0e+00

1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; 1-deoxy-D-xylulose 5-phosphate reductoisomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


:

Pssm-ID: 440506  Cd Length: 385  Bit Score: 691.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457   1 MKQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHehGSRTEVLS 80
Cdd:COG0743    1 MKRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREALA--GSGIEVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  81 GQQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSM 160
Cdd:COG0743   79 GEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEHGAQLLPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 161 PETiqqhlgyadlARNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFN 240
Cdd:COG0743  159 PGE----------DREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDSATMMNKGLEVIEAHWLFD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 241 ASAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKL 320
Cdd:COG0743  229 VPPDQIEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDLAKLGTLTFEPPDEERFPCLRL 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488978457 321 AMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDLQEPQSIDDVLVIDAEARAIAHQQLQRL 396
Cdd:COG0743  309 AYEALRAGGTAPAVLNAANEVAVAAFLAGRIGFLDIADVVEKVLERHPPIAPPSLEDVLEADAWARRRARELIARL 384
 
Name Accession Description Interval E-value
Dxr COG0743
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
1-396 0e+00

1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; 1-deoxy-D-xylulose 5-phosphate reductoisomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440506  Cd Length: 385  Bit Score: 691.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457   1 MKQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHehGSRTEVLS 80
Cdd:COG0743    1 MKRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREALA--GSGIEVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  81 GQQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSM 160
Cdd:COG0743   79 GEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEHGAQLLPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 161 PETiqqhlgyadlARNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFN 240
Cdd:COG0743  159 PGE----------DREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDSATMMNKGLEVIEAHWLFD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 241 ASAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKL 320
Cdd:COG0743  229 VPPDQIEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDLAKLGTLTFEPPDEERFPCLRL 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488978457 321 AMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDLQEPQSIDDVLVIDAEARAIAHQQLQRL 396
Cdd:COG0743  309 AYEALRAGGTAPAVLNAANEVAVAAFLAGRIGFLDIADVVEKVLERHPPIAPPSLEDVLEADAWARRRARELIARL 384
PRK05447 PRK05447
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
1-398 0e+00

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


Pssm-ID: 235472  Cd Length: 385  Bit Score: 686.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457   1 MKQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGsrTEVLS 80
Cdd:PRK05447   1 MKRITILGSTGSIGTQTLDVIRRNPDRFRVVALSAGKNVELLAEQAREFRPKYVVVADEEAAKELKEALAAAG--IEVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  81 GQQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSM 160
Cdd:PRK05447  79 GEEGLCELAALPEADVVVAAIVGAAGLLPTLAAIRAGKRIALANKESLVCAGELVMDAAKKSGAQILPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 161 PETIQqhlgyadlarNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFN 240
Cdd:PRK05447 159 PGEKQ----------EGVEKIILTASGGPFRDWPLEELANVTPEQALKHPNWSMGRKITIDSATMMNKGLEVIEAHWLFG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 241 ASAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKL 320
Cdd:PRK05447 229 LPYEQIEVVIHPQSIIHSMVEYVDGSVLAQLGPPDMRLPIAYALAYPERVPSGVKPLDLTKLGTLTFEPPDFERFPCLKL 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488978457 321 AMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDlQEPQSIDDVLVIDAEARAIAHQQLQRLVA 398
Cdd:PRK05447 309 AYEALKAGGTAPAVLNAANEVAVAAFLAGKIGFLDIADLIEKVLERHN-PEPPSLEDVLEADAEARERARELIARLAA 385
Dxr TIGR00243
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
1-397 0e+00

1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted to 2-C-methyl-D-erythritol 4-phosphate in the presence of NADPH. It is involved in the synthesis of isopentenyl diphosphate (IPP), a basic building block in isoprenoid, thiamin, and pyridoxal biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 161787 [Multi-domain]  Cd Length: 389  Bit Score: 614.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457    1 MKQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGSRTEVLS 80
Cdd:TIGR00243   1 MKQIVILGSTGSIGKSTLDVVRHNPDHFQVVALSAGKNVALMVEQILEFRPKFVAIDDEASLKDLKTMLQQQGSRTEVLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457   81 GQQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSM 160
Cdd:TIGR00243  81 GEEGICEMAALEDVDQVMNAIVGAAGLLPTLAAIRAGKTIALANKESLVTAGHLFLDAVKKYGVQLLPVDSEHNAIFQSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  161 PETIQQhlgyadlarNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFN 240
Cdd:TIGR00243 161 QHGLEE---------LGVVSIILTASGGAFRDTPLEDLPTVTPQQALKHPNWSMGRKITIDSATMMNKGLEYIEARWLFG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  241 ASAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKL 320
Cdd:TIGR00243 232 ASAEQIDVLIHPQSIIHSMVEFQDGSVIAQLGEPDMRLPIAYAMAWPNRVNSGVKPLDLCKLSALTFEEPDFDRYPCLKL 311
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488978457  321 AMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDLQEPQSIDDVLVIDAEARAIAHQQLQRLV 397
Cdd:TIGR00243 312 AMEAFKAGQAATTVLNAANEVAVAAFLAQQIRFLDIAALISKVLYRMQPRKPQSLEDVLEVDKNARETARKNVARVA 388
DXP_reductoisom pfam02670
1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose ...
4-132 1.88e-68

1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose 5-phosphate reductoisomerases. This enzyme catalyzes the formation of 2-C-methyl-D-erythritol 4-phosphate from 1-deoxy-D-xylulose-5-phosphate in the presence of NADPH. This reaction is part of the terpenoid biosynthesis pathway.


Pssm-ID: 460644 [Multi-domain]  Cd Length: 127  Bit Score: 212.34  E-value: 1.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457    4 LTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGsrTEVLSGQQ 83
Cdd:pfam02670   1 ITILGSTGSIGTQTLDVIRRHPDRFEVVALAAGRNVELLAEQIKEFKPKYVAVADEEAAEELKAALAGTG--TEVLAGEE 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 488978457   84 AAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCG 132
Cdd:pfam02670  79 GLCEVAALPEADIVMAAIVGAAGLLPTLAAIKAGKRIALANKESLVAAG 127
 
Name Accession Description Interval E-value
Dxr COG0743
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
1-396 0e+00

1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; 1-deoxy-D-xylulose 5-phosphate reductoisomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440506  Cd Length: 385  Bit Score: 691.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457   1 MKQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHehGSRTEVLS 80
Cdd:COG0743    1 MKRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREALA--GSGIEVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  81 GQQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSM 160
Cdd:COG0743   79 GEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEHGAQLLPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 161 PETiqqhlgyadlARNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFN 240
Cdd:COG0743  159 PGE----------DREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDSATMMNKGLEVIEAHWLFD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 241 ASAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKL 320
Cdd:COG0743  229 VPPDQIEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDLAKLGTLTFEPPDEERFPCLRL 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488978457 321 AMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDLQEPQSIDDVLVIDAEARAIAHQQLQRL 396
Cdd:COG0743  309 AYEALRAGGTAPAVLNAANEVAVAAFLAGRIGFLDIADVVEKVLERHPPIAPPSLEDVLEADAWARRRARELIARL 384
PRK05447 PRK05447
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
1-398 0e+00

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


Pssm-ID: 235472  Cd Length: 385  Bit Score: 686.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457   1 MKQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGsrTEVLS 80
Cdd:PRK05447   1 MKRITILGSTGSIGTQTLDVIRRNPDRFRVVALSAGKNVELLAEQAREFRPKYVVVADEEAAKELKEALAAAG--IEVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  81 GQQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSM 160
Cdd:PRK05447  79 GEEGLCELAALPEADVVVAAIVGAAGLLPTLAAIRAGKRIALANKESLVCAGELVMDAAKKSGAQILPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 161 PETIQqhlgyadlarNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFN 240
Cdd:PRK05447 159 PGEKQ----------EGVEKIILTASGGPFRDWPLEELANVTPEQALKHPNWSMGRKITIDSATMMNKGLEVIEAHWLFG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 241 ASAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKL 320
Cdd:PRK05447 229 LPYEQIEVVIHPQSIIHSMVEYVDGSVLAQLGPPDMRLPIAYALAYPERVPSGVKPLDLTKLGTLTFEPPDFERFPCLKL 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488978457 321 AMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDlQEPQSIDDVLVIDAEARAIAHQQLQRLVA 398
Cdd:PRK05447 309 AYEALKAGGTAPAVLNAANEVAVAAFLAGKIGFLDIADLIEKVLERHN-PEPPSLEDVLEADAEARERARELIARLAA 385
Dxr TIGR00243
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
1-397 0e+00

1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted to 2-C-methyl-D-erythritol 4-phosphate in the presence of NADPH. It is involved in the synthesis of isopentenyl diphosphate (IPP), a basic building block in isoprenoid, thiamin, and pyridoxal biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 161787 [Multi-domain]  Cd Length: 389  Bit Score: 614.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457    1 MKQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGSRTEVLS 80
Cdd:TIGR00243   1 MKQIVILGSTGSIGKSTLDVVRHNPDHFQVVALSAGKNVALMVEQILEFRPKFVAIDDEASLKDLKTMLQQQGSRTEVLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457   81 GQQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSM 160
Cdd:TIGR00243  81 GEEGICEMAALEDVDQVMNAIVGAAGLLPTLAAIRAGKTIALANKESLVTAGHLFLDAVKKYGVQLLPVDSEHNAIFQSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  161 PETIQQhlgyadlarNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFN 240
Cdd:TIGR00243 161 QHGLEE---------LGVVSIILTASGGAFRDTPLEDLPTVTPQQALKHPNWSMGRKITIDSATMMNKGLEYIEARWLFG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  241 ASAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKL 320
Cdd:TIGR00243 232 ASAEQIDVLIHPQSIIHSMVEFQDGSVIAQLGEPDMRLPIAYAMAWPNRVNSGVKPLDLCKLSALTFEEPDFDRYPCLKL 311
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488978457  321 AMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDLQEPQSIDDVLVIDAEARAIAHQQLQRLV 397
Cdd:TIGR00243 312 AMEAFKAGQAATTVLNAANEVAVAAFLAQQIRFLDIAALISKVLYRMQPRKPQSLEDVLEVDKNARETARKNVARVA 388
PRK12464 PRK12464
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
6-398 7.90e-176

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


Pssm-ID: 237107  Cd Length: 383  Bit Score: 495.07  E-value: 7.90e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457   6 VLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGSRteVLSGQQAA 85
Cdd:PRK12464   1 ILGSTGSIGTSALDVVSAHPEHFKVVGLTANYNIELLEQQIKRFQPRIVSVADKELADTLRTRLSANTSK--ITYGTDGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  86 AEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQSMPETIQ 165
Cdd:PRK12464  79 IAVATHPGSDLVLSSVVGAAGLLPTIEALKAKKDIALANKETLVAAGHIVTDLAKQNGCRLIPVDSEHSAIFQCLNGENN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 166 QHLgyadlarngvSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASAQQ 245
Cdd:PRK12464 159 KEI----------DKLIVTASGGAFRDKTREEMATLTAKDALKHPNWLMGAKLTIDSATLMNKGFEVIEAHWLFDIPYEK 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 246 MEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSGVKPLDFCQLSNLSFSAPDYTRYPCLKLAMDAF 325
Cdd:PRK12464 229 IDVLIHKESIIHSLVEFIDGSVLAQLGAPDMRMPIQYAFHYPTRLPSSYEKLNLLEIGSLHFEKPDLEKFPCLQYAYEAG 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488978457 326 DVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLDKMDLQEPQSIDDVLVIDAEARAIAHQQLQRLVA 398
Cdd:PRK12464 309 KIGGTTPAVLNAANEIANALFLKNRIAFFDIEKTIYATLEAHHNVKDPSLDDILEADAWARRYANQLLIKKSA 381
PLN02696 PLN02696
1-deoxy-D-xylulose-5-phosphate reductoisomerase
2-400 1.73e-138

1-deoxy-D-xylulose-5-phosphate reductoisomerase


Pssm-ID: 215374  Cd Length: 454  Bit Score: 403.02  E-value: 1.73e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457   2 KQLTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGSRTEVLSG 81
Cdd:PLN02696  58 KPISLLGSTGSIGTQTLDIVAENPDKFKVVALAAGSNVTLLADQVRKFKPKLVAVRNESLVDELKEALADLDDKPEIIPG 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  82 QQAAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCGRLFMEAVQQSGARLLPVDSEHNAIFQsmp 161
Cdd:PLN02696 138 EEGIVEVARHPEAVTVVTGIVGCAGLKPTVAAIEAGKDIALANKETLIAGGPFVLPLAKKHGVKILPADSEHSAIFQ--- 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 162 eTIQqhlgyaDLARNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNA 241
Cdd:PLN02696 215 -CIQ------GLPEGGLRRIILTASGGAFRDWPVEKLKEVKVADALKHPNWSMGKKITVDSATLMNKGLEVIEAHYLFGA 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 242 SAQQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMGWPQRLNSG---VKPLDFCQLSNLSFSAPDYTRYPCL 318
Cdd:PLN02696 288 DYDDIDIVIHPQSIIHSMVETQDSSVLAQLGWPDMRLPILYTMSWPDRVPCSeitWPRLDLCKLGSLTFKAPDNVKYPSM 367
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457 319 KLAMDAFDVGQAATTTLNAANEESVAAFLHGDIRFTDIAAVNLAVLD--KMDLQEPQSIDDVLVIDAEARAIAHQQLQRL 396
Cdd:PLN02696 368 DLAYAAGRAGGTMTGVLSAANEKAVEMFIDEKIGYLDIFKVIELTCEahKEELVTSPSLEDILHYDLWAREYAAELVESG 447

                 ....
gi 488978457 397 VAQA 400
Cdd:PLN02696 448 GLSP 451
DXP_reductoisom pfam02670
1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose ...
4-132 1.88e-68

1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose 5-phosphate reductoisomerases. This enzyme catalyzes the formation of 2-C-methyl-D-erythritol 4-phosphate from 1-deoxy-D-xylulose-5-phosphate in the presence of NADPH. This reaction is part of the terpenoid biosynthesis pathway.


Pssm-ID: 460644 [Multi-domain]  Cd Length: 127  Bit Score: 212.34  E-value: 1.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457    4 LTVLGSTGSIGCSTLDVVRHNPGRFSVAALVAGKNVDRMVEQCLEFTPRYAVMDDAQSAERLRTRLHEHGsrTEVLSGQQ 83
Cdd:pfam02670   1 ITILGSTGSIGTQTLDVIRRHPDRFEVVALAAGRNVELLAEQIKEFKPKYVAVADEEAAEELKAALAGTG--TEVLAGEE 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 488978457   84 AAAEVAALDEVDQVMAAIVGAAGLVPTLAAIRAGKTVLLANKESLVTCG 132
Cdd:pfam02670  79 GLCEVAALPEADIVMAAIVGAAGLLPTLAAIKAGKRIALANKESLVAAG 127
DXPR_C pfam13288
DXP reductoisomerase C-terminal domain; This is the C-terminal domain of the ...
272-388 3.19e-56

DXP reductoisomerase C-terminal domain; This is the C-terminal domain of the 1-deoxy-D-xylulose-5-phosphate reductoisomerase enzyme. This domain forms a left handed super-helix.


Pssm-ID: 463830 [Multi-domain]  Cd Length: 116  Bit Score: 180.31  E-value: 3.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  272 GEPDMRTPIAHTMGWPQRLnSGVKPLDFCQLSNLSFSAPDYTRYPCLKLAMDAFDVGQAATTTLNAANEESVAAFLHGDI 351
Cdd:pfam13288   1 GPPDMRLPIAYALSYPERL-SGVEPLDLAKLGSLTFEEPDLERFPCLKLAYEALRAGGTAPAVLNAANEVAVAAFLAGKI 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 488978457  352 RFTDIAAVNLAVLDKMDLQEPQSIDDVLVIDAEARAI 388
Cdd:pfam13288  80 GFLDIPDIIEKVLEAHDGIEPPSLEDILEADAEAREY 116
DXP_redisom_C pfam08436
1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the ...
146-239 1.12e-54

1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the C-terminus of pfam02670 domains in bacterial and plant 1-deoxy-D-xylulose 5-phosphate reductoisomerases which catalyze the formation of 2-C-methyl-D-erythritol 4-phosphate from 1-deoxy-D-xylulose-5-phosphate in the presence of NADPH.


Pssm-ID: 462477 [Multi-domain]  Cd Length: 84  Bit Score: 175.28  E-value: 1.12e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488978457  146 LLPVDSEHNAIFQSMPetiqqhlgyaDLARNGVSSILLTGSGGPFRETAVAELAAMTPDQACRHPNWSMGRKISVDSATM 225
Cdd:pfam08436   1 ILPVDSEHSAIFQCLP----------GGSQGEVEKIILTASGGPFRGKPREELANVTPEQALKHPNWSMGAKITIDSATM 70
                          90
                  ....*....|....
gi 488978457  226 MNKGLEYIEARWLF 239
Cdd:pfam08436  71 MNKGLEVIEAHWLF 84
 
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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