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Conserved domains on  [gi|488617876|ref|WP_002554725|]
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MULTISPECIES: 1-deoxy-D-xylulose-5-phosphate reductoisomerase [Pseudomonas]

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]; ...
4-395 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: 659.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876   4 PQHITILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAvaGLDTRVLV 83
Cdd:COG0743    1 MKRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREALA--GSGIEVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  84 GEGGLCEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPIDSEHNAIFQCL 163
Cdd:COG0743   79 GEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEHGAQLLPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 164 PGDFARGlgavgVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGLELIEACWLFDARPDQ 243
Cdd:COG0743  159 PGEDREG-----VERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDSATMMNKGLEVIEAHWLFDVPPDQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 244 VEVVIHPQSVIHSLVDYVDGSVLAQLGNPDMRTPIANALAWPERVDSGVAPLDLFRIGQLDFQKPDEERFPCLRLARHAA 323
Cdd:COG0743  234 IEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDLAKLGTLTFEPPDEERFPCLRLAYEAL 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617876 324 EAGGSAPAMLNAANEVAVAAFLDGRIRYLEIAGIIEEVLNHEPVTAVEGLDAVFAADAKARLLAGQWLERNA 395
Cdd:COG0743  314 RAGGTAPAVLNAANEVAVAAFLAGRIGFLDIADVVEKVLERHPPIAPPSLEDVLEADAWARRRARELIARLA 385
 
Name Accession Description Interval E-value
Dxr COG0743
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
4-395 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: 659.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876   4 PQHITILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAvaGLDTRVLV 83
Cdd:COG0743    1 MKRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREALA--GSGIEVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  84 GEGGLCEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPIDSEHNAIFQCL 163
Cdd:COG0743   79 GEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEHGAQLLPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 164 PGDFARGlgavgVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGLELIEACWLFDARPDQ 243
Cdd:COG0743  159 PGEDREG-----VERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDSATMMNKGLEVIEAHWLFDVPPDQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 244 VEVVIHPQSVIHSLVDYVDGSVLAQLGNPDMRTPIANALAWPERVDSGVAPLDLFRIGQLDFQKPDEERFPCLRLARHAA 323
Cdd:COG0743  234 IEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDLAKLGTLTFEPPDEERFPCLRLAYEAL 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617876 324 EAGGSAPAMLNAANEVAVAAFLDGRIRYLEIAGIIEEVLNHEPVTAVEGLDAVFAADAKARLLAGQWLERNA 395
Cdd:COG0743  314 RAGGTAPAVLNAANEVAVAAFLAGRIGFLDIADVVEKVLERHPPIAPPSLEDVLEADAWARRRARELIARLA 385
PRK05447 PRK05447
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
4-396 0e+00

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


Pssm-ID: 235472  Cd Length: 385  Bit Score: 648.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876   4 PQHITILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAVAGLdtRVLV 83
Cdd:PRK05447   1 MKRITILGSTGSIGTQTLDVIRRNPDRFRVVALSAGKNVELLAEQAREFRPKYVVVADEEAAKELKEALAAAGI--EVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  84 GEGGLCEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPIDSEHNAIFQCL 163
Cdd:PRK05447  79 GEEGLCELAALPEADVVVAAIVGAAGLLPTLAAIRAGKRIALANKESLVCAGELVMDAAKKSGAQILPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 164 PGDFARGlgavgVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGLELIEACWLFDARPDQ 243
Cdd:PRK05447 159 PGEKQEG-----VEKIILTASGGPFRDWPLEELANVTPEQALKHPNWSMGRKITIDSATMMNKGLEVIEAHWLFGLPYEQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 244 VEVVIHPQSVIHSLVDYVDGSVLAQLGNPDMRTPIANALAWPERVDSGVAPLDLFRIGQLDFQKPDEERFPCLRLARHAA 323
Cdd:PRK05447 234 IEVVIHPQSIIHSMVEYVDGSVLAQLGPPDMRLPIAYALAYPERVPSGVKPLDLTKLGTLTFEPPDFERFPCLKLAYEAL 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488617876 324 EAGGSAPAMLNAANEVAVAAFLDGRIRYLEIAGIIEEVLNHEPVtAVEGLDAVFAADAKARLLAGQWLERNAR 396
Cdd:PRK05447 314 KAGGTAPAVLNAANEVAVAAFLAGKIGFLDIADLIEKVLERHNP-EPPSLEDVLEADAEARERARELIARLAA 385
Dxr TIGR00243
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
5-395 2.72e-170

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: 481.24  E-value: 2.72e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876    5 QHITILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAVAGLDTRVLVG 84
Cdd:TIGR00243   2 KQIVILGSTGSIGKSTLDVVRHNPDHFQVVALSAGKNVALMVEQILEFRPKFVAIDDEASLKDLKTMLQQQGSRTEVLVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876   85 EGGLCEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPIDSEHNAIFQCLp 164
Cdd:TIGR00243  82 EEGICEMAALEDVDQVMNAIVGAAGLLPTLAAIRAGKTIALANKESLVTAGHLFLDAVKKYGVQLLPVDSEHNAIFQSL- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  165 gdfARGLGAVGVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGLELIEACWLFDARPDQV 244
Cdd:TIGR00243 161 ---QHGLEELGVVSIILTASGGAFRDTPLEDLPTVTPQQALKHPNWSMGRKITIDSATMMNKGLEYIEARWLFGASAEQI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  245 EVVIHPQSVIHSLVDYVDGSVLAQLGNPDMRTPIANALAWPERVDSGVAPLDLFRIGQLDFQKPDEERFPCLRLARHAAE 324
Cdd:TIGR00243 238 DVLIHPQSIIHSMVEFQDGSVIAQLGEPDMRLPIAYAMAWPNRVNSGVKPLDLCKLSALTFEEPDFDRYPCLKLAMEAFK 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488617876  325 AGGSAPAMLNAANEVAVAAFLDGRIRYLEIAGIIEEVLNHEPVTAVEGLDAVFAADAKARLLAGQWLERNA 395
Cdd:TIGR00243 318 AGQAATTVLNAANEVAVAAFLAQQIRFLDIAALISKVLYRMQPRKPQSLEDVLEVDKNARETARKNVARVA 388
DXP_redisom_C pfam08436
1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the ...
149-237 2.86e-61

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: 192.22  E-value: 2.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  149 LLPIDSEHNAIFQCLPGDFARGlgavgVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGL 228
Cdd:pfam08436   1 ILPVDSEHSAIFQCLPGGSQGE-----VEKIILTASGGPFRGKPREELANVTPEQALKHPNWSMGAKITIDSATMMNKGL 75

                  ....*....
gi 488617876  229 ELIEACWLF 237
Cdd:pfam08436  76 EVIEAHWLF 84
 
Name Accession Description Interval E-value
Dxr COG0743
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
4-395 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: 659.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876   4 PQHITILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAvaGLDTRVLV 83
Cdd:COG0743    1 MKRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREALA--GSGIEVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  84 GEGGLCEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPIDSEHNAIFQCL 163
Cdd:COG0743   79 GEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEHGAQLLPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 164 PGDFARGlgavgVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGLELIEACWLFDARPDQ 243
Cdd:COG0743  159 PGEDREG-----VERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDSATMMNKGLEVIEAHWLFDVPPDQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 244 VEVVIHPQSVIHSLVDYVDGSVLAQLGNPDMRTPIANALAWPERVDSGVAPLDLFRIGQLDFQKPDEERFPCLRLARHAA 323
Cdd:COG0743  234 IEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDLAKLGTLTFEPPDEERFPCLRLAYEAL 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617876 324 EAGGSAPAMLNAANEVAVAAFLDGRIRYLEIAGIIEEVLNHEPVTAVEGLDAVFAADAKARLLAGQWLERNA 395
Cdd:COG0743  314 RAGGTAPAVLNAANEVAVAAFLAGRIGFLDIADVVEKVLERHPPIAPPSLEDVLEADAWARRRARELIARLA 385
PRK05447 PRK05447
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
4-396 0e+00

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


Pssm-ID: 235472  Cd Length: 385  Bit Score: 648.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876   4 PQHITILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAVAGLdtRVLV 83
Cdd:PRK05447   1 MKRITILGSTGSIGTQTLDVIRRNPDRFRVVALSAGKNVELLAEQAREFRPKYVVVADEEAAKELKEALAAAGI--EVLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  84 GEGGLCEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPIDSEHNAIFQCL 163
Cdd:PRK05447  79 GEEGLCELAALPEADVVVAAIVGAAGLLPTLAAIRAGKRIALANKESLVCAGELVMDAAKKSGAQILPVDSEHSAIFQCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 164 PGDFARGlgavgVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGLELIEACWLFDARPDQ 243
Cdd:PRK05447 159 PGEKQEG-----VEKIILTASGGPFRDWPLEELANVTPEQALKHPNWSMGRKITIDSATMMNKGLEVIEAHWLFGLPYEQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 244 VEVVIHPQSVIHSLVDYVDGSVLAQLGNPDMRTPIANALAWPERVDSGVAPLDLFRIGQLDFQKPDEERFPCLRLARHAA 323
Cdd:PRK05447 234 IEVVIHPQSIIHSMVEYVDGSVLAQLGPPDMRLPIAYALAYPERVPSGVKPLDLTKLGTLTFEPPDFERFPCLKLAYEAL 313
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488617876 324 EAGGSAPAMLNAANEVAVAAFLDGRIRYLEIAGIIEEVLNHEPVtAVEGLDAVFAADAKARLLAGQWLERNAR 396
Cdd:PRK05447 314 KAGGTAPAVLNAANEVAVAAFLAGKIGFLDIADLIEKVLERHNP-EPPSLEDVLEADAEARERARELIARLAA 385
Dxr TIGR00243
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
5-395 2.72e-170

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: 481.24  E-value: 2.72e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876    5 QHITILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAVAGLDTRVLVG 84
Cdd:TIGR00243   2 KQIVILGSTGSIGKSTLDVVRHNPDHFQVVALSAGKNVALMVEQILEFRPKFVAIDDEASLKDLKTMLQQQGSRTEVLVG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876   85 EGGLCEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPIDSEHNAIFQCLp 164
Cdd:TIGR00243  82 EEGICEMAALEDVDQVMNAIVGAAGLLPTLAAIRAGKTIALANKESLVTAGHLFLDAVKKYGVQLLPVDSEHNAIFQSL- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  165 gdfARGLGAVGVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGLELIEACWLFDARPDQV 244
Cdd:TIGR00243 161 ---QHGLEELGVVSIILTASGGAFRDTPLEDLPTVTPQQALKHPNWSMGRKITIDSATMMNKGLEYIEARWLFGASAEQI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  245 EVVIHPQSVIHSLVDYVDGSVLAQLGNPDMRTPIANALAWPERVDSGVAPLDLFRIGQLDFQKPDEERFPCLRLARHAAE 324
Cdd:TIGR00243 238 DVLIHPQSIIHSMVEFQDGSVIAQLGEPDMRLPIAYAMAWPNRVNSGVKPLDLCKLSALTFEEPDFDRYPCLKLAMEAFK 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488617876  325 AGGSAPAMLNAANEVAVAAFLDGRIRYLEIAGIIEEVLNHEPVTAVEGLDAVFAADAKARLLAGQWLERNA 395
Cdd:TIGR00243 318 AGQAATTVLNAANEVAVAAFLAQQIRFLDIAALISKVLYRMQPRKPQSLEDVLEVDKNARETARKNVARVA 388
PRK12464 PRK12464
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
9-393 2.72e-164

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


Pssm-ID: 237107  Cd Length: 383  Bit Score: 465.80  E-value: 2.72e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876   9 ILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAVAGldTRVLVGEGGL 88
Cdd:PRK12464   1 ILGSTGSIGTSALDVVSAHPEHFKVVGLTANYNIELLEQQIKRFQPRIVSVADKELADTLRTRLSANT--SKITYGTDGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  89 CEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPIDSEHNAIFQCLPGDfa 168
Cdd:PRK12464  79 IAVATHPGSDLVLSSVVGAAGLLPTIEALKAKKDIALANKETLVAAGHIVTDLAKQNGCRLIPVDSEHSAIFQCLNGE-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 169 rglGAVGVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGLELIEACWLFDARPDQVEVVI 248
Cdd:PRK12464 157 ---NNKEIDKLIVTASGGAFRDKTREEMATLTAKDALKHPNWLMGAKLTIDSATLMNKGFEVIEAHWLFDIPYEKIDVLI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 249 HPQSVIHSLVDYVDGSVLAQLGNPDMRTPIANALAWPERVDSGVAPLDLFRIGQLDFQKPDEERFPCLRLARHAAEAGGS 328
Cdd:PRK12464 234 HKESIIHSLVEFIDGSVLAQLGAPDMRMPIQYAFHYPTRLPSSYEKLNLLEIGSLHFEKPDLEKFPCLQYAYEAGKIGGT 313
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488617876 329 APAMLNAANEVAVAAFLDGRIRYLEIAGIIEEVLNHEPVTAVEGLDAVFAADAKARLLAGQWLER 393
Cdd:PRK12464 314 TPAVLNAANEIANALFLKNRIAFFDIEKTIYATLEAHHNVKDPSLDDILEADAWARRYANQLLIK 378
PLN02696 PLN02696
1-deoxy-D-xylulose-5-phosphate reductoisomerase
2-389 3.89e-126

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


Pssm-ID: 215374  Cd Length: 454  Bit Score: 371.43  E-value: 3.89e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876   2 SGPQHITILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAVAGLDTRV 81
Cdd:PLN02696  55 DGPKPISLLGSTGSIGTQTLDIVAENPDKFKVVALAAGSNVTLLADQVRKFKPKLVAVRNESLVDELKEALADLDDKPEI 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  82 LVGEGGLCEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPIDSEHNAIFQ 161
Cdd:PLN02696 135 IPGEEGIVEVARHPEAVTVVTGIVGCAGLKPTVAAIEAGKDIALANKETLIAGGPFVLPLAKKHGVKILPADSEHSAIFQ 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 162 CLpgdfaRGLGAVGVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGLELIEACWLFDARP 241
Cdd:PLN02696 215 CI-----QGLPEGGLRRIILTASGGAFRDWPVEKLKEVKVADALKHPNWSMGKKITVDSATLMNKGLEVIEAHYLFGADY 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876 242 DQVEVVIHPQSVIHSLVDYVDGSVLAQLGNPDMRTPIANALAWPERVDSGVAP---LDLFRIGQLDFQKPDEERFPCLRL 318
Cdd:PLN02696 290 DDIDIVIHPQSIIHSMVETQDSSVLAQLGWPDMRLPILYTMSWPDRVPCSEITwprLDLCKLGSLTFKAPDNVKYPSMDL 369
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488617876 319 ARHAAEAGGSAPAMLNAANEVAVAAFLDGRIRYLEIAGIIE---EVLNHEPVTAVEgLDAVFAADAKARLLAGQ 389
Cdd:PLN02696 370 AYAAGRAGGTMTGVLSAANEKAVEMFIDEKIGYLDIFKVIEltcEAHKEELVTSPS-LEDILHYDLWAREYAAE 442
DXP_redisom_C pfam08436
1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the ...
149-237 2.86e-61

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: 192.22  E-value: 2.86e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  149 LLPIDSEHNAIFQCLPGDFARGlgavgVRRIMLTASGGPFRETPLEQLQNVTPEQACAHPVWSMGRKISVDSATMMNKGL 228
Cdd:pfam08436   1 ILPVDSEHSAIFQCLPGGSQGE-----VEKIILTASGGPFRGKPREELANVTPEQALKHPNWSMGAKITIDSATMMNKGL 75

                  ....*....
gi 488617876  229 ELIEACWLF 237
Cdd:pfam08436  76 EVIEAHWLF 84
DXP_reductoisom pfam02670
1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose ...
7-135 2.53e-59

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: 188.45  E-value: 2.53e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876    7 ITILGATGSIGLSTLDVVARHPSLYQVFALTGFSRLDELLALCVRHTPQYAVVPDQFVARKLQDYLAvaGLDTRVLVGEG 86
Cdd:pfam02670   1 ITILGSTGSIGTQTLDVIRRHPDRFEVVALAAGRNVELLAEQIKEFKPKYVAVADEEAAEELKAALA--GTGTEVLAGEE 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 488617876   87 GLCEVAAHPRVDAVMAAIVGAAGLRPTLAAVEAGKKVLLANKEALVMSG 135
Cdd:pfam02670  79 GLCEVAALPEADIVMAAIVGAAGLLPTLAAIKAGKRIALANKESLVAAG 127
DXPR_C pfam13288
DXP reductoisomerase C-terminal domain; This is the C-terminal domain of the ...
270-384 6.53e-48

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: 158.74  E-value: 6.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  270 GNPDMRTPIANALAWPERVdSGVAPLDLFRIGQLDFQKPDEERFPCLRLARHAAEAGGSAPAMLNAANEVAVAAFLDGRI 349
Cdd:pfam13288   1 GPPDMRLPIAYALSYPERL-SGVEPLDLAKLGSLTFEEPDLERFPCLKLAYEALRAGGTAPAVLNAANEVAVAAFLAGKI 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 488617876  350 RYLEIAGIIEEVLNHEPVTAVEGLDAVFAADAKAR 384
Cdd:pfam13288  80 GFLDIPDIIEKVLEAHDGIEPPSLEDILEADAEAR 114
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
91-172 7.34e-03

Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 38.21  E-value: 7.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617876  91 VAAHPRVDAVMAAI-VGAAGLRPTLAAVEAGKKVLLANKEALVMSGDLFMQAVRQSGAVLLPID-SEHNAIFQCLpgDFA 168
Cdd:COG4091   94 LIAADGIDVVVEATgVPEAGARHALAAIEAGKHVVMVNVEADVTVGPLLKRRADEAGVVYTGADgDQPGLIMELY--DFA 171

                 ....
gi 488617876 169 RGLG 172
Cdd:COG4091  172 RALG 175
 
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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