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Conserved domains on  [gi|2556527334|ref|WP_304271150|]
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1-deoxy-D-xylulose-5-phosphate reductoisomerase [Pseudoglutamicibacter cumminsii]

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]; ...
3-377 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: 520.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   3 RSVVIVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLAGAEgmSADDVRggfmlhlagaket 82
Cdd:COG0743     2 KRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEA--AAEELR------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  83 aarngglelagagfvdvdaAGLDTYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLV 162
Cdd:COG0743    67 -------------------EALAGSGIEVLAGEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLV 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 163 AGGRLVMEAAA--PGQIVPVDSEHSAIAQALRSGARSEVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVVT 240
Cdd:COG0743   128 VAGELVMAAAKehGAQLLPVDSEHSAIFQCLPGEDREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKIT 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 241 TNSATLVNKALEVIEAHLLFDVALDRIVPVVHPQSVVHSMVEFVDGSTIAQASPPDMGLPIALGLNWPDRLPGACAPVDW 320
Cdd:COG0743   208 IDSATMMNKGLEVIEAHWLFDVPPDQIEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDL 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2556527334 321 TQAHTWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVIGFRKI 377
Cdd:COG0743   288 AKLGTLTFEPPDEERFPCLRLAYEALRAGGTAPAVLNAANEVAVAAFLAGRIGFLDI 344
 
Name Accession Description Interval E-value
Dxr COG0743
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
3-377 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: 520.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   3 RSVVIVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLAGAEgmSADDVRggfmlhlagaket 82
Cdd:COG0743     2 KRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEA--AAEELR------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  83 aarngglelagagfvdvdaAGLDTYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLV 162
Cdd:COG0743    67 -------------------EALAGSGIEVLAGEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLV 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 163 AGGRLVMEAAA--PGQIVPVDSEHSAIAQALRSGARSEVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVVT 240
Cdd:COG0743   128 VAGELVMAAAKehGAQLLPVDSEHSAIFQCLPGEDREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKIT 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 241 TNSATLVNKALEVIEAHLLFDVALDRIVPVVHPQSVVHSMVEFVDGSTIAQASPPDMGLPIALGLNWPDRLPGACAPVDW 320
Cdd:COG0743   208 IDSATMMNKGLEVIEAHWLFDVPPDQIEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDL 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2556527334 321 TQAHTWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVIGFRKI 377
Cdd:COG0743   288 AKLGTLTFEPPDEERFPCLRLAYEALRAGGTAPAVLNAANEVAVAAFLAGRIGFLDI 344
PRK05447 PRK05447
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
3-377 2.35e-180

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


Pssm-ID: 235472  Cd Length: 385  Bit Score: 507.31  E-value: 2.35e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   3 RSVVIVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLAGAEgmSADDVRggfmlhlagaket 82
Cdd:PRK05447    2 KRITILGSTGSIGTQTLDVIRRNPDRFRVVALSAGKNVELLAEQAREFRPKYVVVADEE--AAKELK------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  83 aarngglelagagfvdvdaAGLDTYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLV 162
Cdd:PRK05447   67 -------------------EALAAAGIEVLAGEEGLCELAALPEADVVVAAIVGAAGLLPTLAAIRAGKRIALANKESLV 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 163 AGGRLVMEAAA--PGQIVPVDSEHSAIAQALRSGARSEVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVVT 240
Cdd:PRK05447  128 CAGELVMDAAKksGAQILPVDSEHSAIFQCLPGEKQEGVEKIILTASGGPFRDWPLEELANVTPEQALKHPNWSMGRKIT 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 241 TNSATLVNKALEVIEAHLLFDVALDRIVPVVHPQSVVHSMVEFVDGSTIAQASPPDMGLPIALGLNWPDRLPGACAPVDW 320
Cdd:PRK05447  208 IDSATMMNKGLEVIEAHWLFGLPYEQIEVVIHPQSIIHSMVEYVDGSVLAQLGPPDMRLPIAYALAYPERVPSGVKPLDL 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2556527334 321 TQAHTWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVIGFRKI 377
Cdd:PRK05447  288 TKLGTLTFEPPDFERFPCLKLAYEALKAGGTAPAVLNAANEVAVAAFLAGKIGFLDI 344
Dxr TIGR00243
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
3-377 4.37e-112

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: 334.10  E-value: 4.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   3 RSVVIVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLAGAEgmSADDvrggfmlhlagaket 82
Cdd:TIGR00243   2 KQIVILGSTGSIGKSTLDVVRHNPDHFQVVALSAGKNVALMVEQILEFRPKFVAIDDEA--SLKD--------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  83 aarnggLELAGAGFvdvdaagldTYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLV 162
Cdd:TIGR00243  65 ------LKTMLQQQ---------GSRTEVLVGEEGICEMAALEDVDQVMNAIVGAAGLLPTLAAIRAGKTIALANKESLV 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 163 AGGRLVMEAAAP--GQIVPVDSEHSAIAQALRSGARS-EVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVV 239
Cdd:TIGR00243 130 TAGHLFLDAVKKygVQLLPVDSEHNAIFQSLQHGLEElGVVSIILTASGGAFRDTPLEDLPTVTPQQALKHPNWSMGRKI 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 240 TTNSATLVNKALEVIEAHLLFDVALDRIVPVVHPQSVVHSMVEFVDGSTIAQASPPDMGLPIALGLNWPDRLPGACAPVD 319
Cdd:TIGR00243 210 TIDSATMMNKGLEYIEARWLFGASAEQIDVLIHPQSIIHSMVEFQDGSVIAQLGEPDMRLPIAYAMAWPNRVNSGVKPLD 289
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2556527334 320 WTQAHTWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVIGFRKI 377
Cdd:TIGR00243 290 LCKLSALTFEEPDFDRYPCLKLAMEAFKAGQAATTVLNAANEVAVAAFLAQQIRFLDI 347
DXP_redisom_C pfam08436
1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the ...
177-260 1.11e-55

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: 178.36  E-value: 1.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 177 IVPVDSEHSAIAQALRSGARSEVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVVTTNSATLVNKALEVIEA 256
Cdd:pfam08436   1 ILPVDSEHSAIFQCLPGGSQGEVEKIILTASGGPFRGKPREELANVTPEQALKHPNWSMGAKITIDSATMMNKGLEVIEA 80

                  ....
gi 2556527334 257 HLLF 260
Cdd:pfam08436  81 HWLF 84
 
Name Accession Description Interval E-value
Dxr COG0743
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
3-377 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: 520.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   3 RSVVIVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLAGAEgmSADDVRggfmlhlagaket 82
Cdd:COG0743     2 KRIAILGSTGSIGTQTLDVIRRHPDRFRVVALAAGSNVELLAEQAREFRPEYVVVADEA--AAEELR------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  83 aarngglelagagfvdvdaAGLDTYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLV 162
Cdd:COG0743    67 -------------------EALAGSGIEVLAGEEALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLV 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 163 AGGRLVMEAAA--PGQIVPVDSEHSAIAQALRSGARSEVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVVT 240
Cdd:COG0743   128 VAGELVMAAAKehGAQLLPVDSEHSAIFQCLPGEDREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKIT 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 241 TNSATLVNKALEVIEAHLLFDVALDRIVPVVHPQSVVHSMVEFVDGSTIAQASPPDMGLPIALGLNWPDRLPGACAPVDW 320
Cdd:COG0743   208 IDSATMMNKGLEVIEAHWLFDVPPDQIEVVVHPQSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDL 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2556527334 321 TQAHTWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVIGFRKI 377
Cdd:COG0743   288 AKLGTLTFEPPDEERFPCLRLAYEALRAGGTAPAVLNAANEVAVAAFLAGRIGFLDI 344
PRK05447 PRK05447
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
3-377 2.35e-180

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


Pssm-ID: 235472  Cd Length: 385  Bit Score: 507.31  E-value: 2.35e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   3 RSVVIVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLAGAEgmSADDVRggfmlhlagaket 82
Cdd:PRK05447    2 KRITILGSTGSIGTQTLDVIRRNPDRFRVVALSAGKNVELLAEQAREFRPKYVVVADEE--AAKELK------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  83 aarngglelagagfvdvdaAGLDTYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLV 162
Cdd:PRK05447   67 -------------------EALAAAGIEVLAGEEGLCELAALPEADVVVAAIVGAAGLLPTLAAIRAGKRIALANKESLV 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 163 AGGRLVMEAAA--PGQIVPVDSEHSAIAQALRSGARSEVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVVT 240
Cdd:PRK05447  128 CAGELVMDAAKksGAQILPVDSEHSAIFQCLPGEKQEGVEKIILTASGGPFRDWPLEELANVTPEQALKHPNWSMGRKIT 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 241 TNSATLVNKALEVIEAHLLFDVALDRIVPVVHPQSVVHSMVEFVDGSTIAQASPPDMGLPIALGLNWPDRLPGACAPVDW 320
Cdd:PRK05447  208 IDSATMMNKGLEVIEAHWLFGLPYEQIEVVIHPQSIIHSMVEYVDGSVLAQLGPPDMRLPIAYALAYPERVPSGVKPLDL 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2556527334 321 TQAHTWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVIGFRKI 377
Cdd:PRK05447  288 TKLGTLTFEPPDFERFPCLKLAYEALKAGGTAPAVLNAANEVAVAAFLAGKIGFLDI 344
Dxr TIGR00243
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
3-377 4.37e-112

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: 334.10  E-value: 4.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   3 RSVVIVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLAGAEgmSADDvrggfmlhlagaket 82
Cdd:TIGR00243   2 KQIVILGSTGSIGKSTLDVVRHNPDHFQVVALSAGKNVALMVEQILEFRPKFVAIDDEA--SLKD--------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  83 aarnggLELAGAGFvdvdaagldTYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLV 162
Cdd:TIGR00243  65 ------LKTMLQQQ---------GSRTEVLVGEEGICEMAALEDVDQVMNAIVGAAGLLPTLAAIRAGKTIALANKESLV 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 163 AGGRLVMEAAAP--GQIVPVDSEHSAIAQALRSGARS-EVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVV 239
Cdd:TIGR00243 130 TAGHLFLDAVKKygVQLLPVDSEHNAIFQSLQHGLEElGVVSIILTASGGAFRDTPLEDLPTVTPQQALKHPNWSMGRKI 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 240 TTNSATLVNKALEVIEAHLLFDVALDRIVPVVHPQSVVHSMVEFVDGSTIAQASPPDMGLPIALGLNWPDRLPGACAPVD 319
Cdd:TIGR00243 210 TIDSATMMNKGLEYIEARWLFGASAEQIDVLIHPQSIIHSMVEFQDGSVIAQLGEPDMRLPIAYAMAWPNRVNSGVKPLD 289
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2556527334 320 WTQAHTWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVIGFRKI 377
Cdd:TIGR00243 290 LCKLSALTFEEPDFDRYPCLKLAMEAFKAGQAATTVLNAANEVAVAAFLAQQIRFLDI 347
PRK12464 PRK12464
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
7-377 1.03e-99

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


Pssm-ID: 237107  Cd Length: 383  Bit Score: 302.09  E-value: 1.03e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   7 IVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLagaegmsaddvrggfmlhlaGAKETAARn 86
Cdd:PRK12464    1 ILGSTGSIGTSALDVVSAHPEHFKVVGLTANYNIELLEQQIKRFQPRIVSV--------------------ADKELADT- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  87 ggLElagagfvdvdaAGLDTYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLVAGGR 166
Cdd:PRK12464   60 --LR-----------TRLSANTSKITYGTDGLIAVATHPGSDLVLSSVVGAAGLLPTIEALKAKKDIALANKETLVAAGH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 167 LVMEAAAP--GQIVPVDSEHSAIAQALRSGARSEVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVVTTNSA 244
Cdd:PRK12464  127 IVTDLAKQngCRLIPVDSEHSAIFQCLNGENNKEIDKLIVTASGGAFRDKTREEMATLTAKDALKHPNWLMGAKLTIDSA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 245 TLVNKALEVIEAHLLFDVALDRIVPVVHPQSVVHSMVEFVDGSTIAQASPPDMGLPIALGLNWPDRLPGACAPVDWTQAH 324
Cdd:PRK12464  207 TLMNKGFEVIEAHWLFDIPYEKIDVLIHKESIIHSLVEFIDGSVLAQLGAPDMRMPIQYAFHYPTRLPSSYEKLNLLEIG 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2556527334 325 TWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVIGFRKI 377
Cdd:PRK12464  287 SLHFEKPDLEKFPCLQYAYEAGKIGGTTPAVLNAANEIANALFLKNRIAFFDI 339
PLN02696 PLN02696
1-deoxy-D-xylulose-5-phosphate reductoisomerase
7-377 9.48e-96

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


Pssm-ID: 215374  Cd Length: 454  Bit Score: 294.39  E-value: 9.48e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   7 IVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLAGAEgmSADDVrggfmlhlagaKETAArn 86
Cdd:PLN02696   62 LLGSTGSIGTQTLDIVAENPDKFKVVALAAGSNVTLLADQVRKFKPKLVAVRNES--LVDEL-----------KEALA-- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  87 gglelagagfvDVDaagldtYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLVAGGR 166
Cdd:PLN02696  127 -----------DLD------DKPEIIPGEEGIVEVARHPEAVTVVTGIVGCAGLKPTVAAIEAGKDIALANKETLIAGGP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 167 LVMEAAAPG--QIVPVDSEHSAIAQALRSGARSEVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVVTTNSA 244
Cdd:PLN02696  190 FVLPLAKKHgvKILPADSEHSAIFQCIQGLPEGGLRRIILTASGGAFRDWPVEKLKEVKVADALKHPNWSMGKKITVDSA 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 245 TLVNKALEVIEAHLLFDVALDRIVPVVHPQSVVHSMVEFVDGSTIAQASPPDMGLPIALGLNWPDRLPgaCAPVDW---- 320
Cdd:PLN02696  270 TLMNKGLEVIEAHYLFGADYDDIDIVIHPQSIIHSMVETQDSSVLAQLGWPDMRLPILYTMSWPDRVP--CSEITWprld 347
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2556527334 321 -TQAHTWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVIGFRKI 377
Cdd:PLN02696  348 lCKLGSLTFKAPDNVKYPSMDLAYAAGRAGGTMTGVLSAANEKAVEMFIDEKIGYLDI 405
DXP_redisom_C pfam08436
1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the ...
177-260 1.11e-55

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: 178.36  E-value: 1.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 177 IVPVDSEHSAIAQALRSGARSEVERLIITASGGPFRGWGAEQLEDVTPEQALAHPTWDMGRVVTTNSATLVNKALEVIEA 256
Cdd:pfam08436   1 ILPVDSEHSAIFQCLPGGSQGEVEKIILTASGGPFRGKPREELANVTPEQALKHPNWSMGAKITIDSATMMNKGLEVIEA 80

                  ....
gi 2556527334 257 HLLF 260
Cdd:pfam08436  81 HWLF 84
DXP_reductoisom pfam02670
1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose ...
5-165 1.09e-33

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: 122.20  E-value: 1.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334   5 VVIVGSTGSIGTQALAQIGRAAGRFVVRALSAGQQARELAAQAVVFRPDVVGLAGAEgmSADDVRggfmlhlagaketaa 84
Cdd:pfam02670   1 ITILGSTGSIGTQTLDVIRRHPDRFEVVALAAGRNVELLAEQIKEFKPKYVAVADEE--AAEELK--------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  85 rngglelagagfvdvdaAGLDTYTPELVVGEDAARACAALPDVDVVLNGVTGSRGLRPTLAAIEAGSVVALANKESLVAG 164
Cdd:pfam02670  64 -----------------AALAGTGTEVLAGEEGLCEVAALPEADIVMAAIVGAAGLLPTLAAIKAGKRIALANKESLVAA 126

                  .
gi 2556527334 165 G 165
Cdd:pfam02670 127 G 127
DXPR_C pfam13288
DXP reductoisomerase C-terminal domain; This is the C-terminal domain of the ...
293-377 7.34e-33

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: 119.83  E-value: 7.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334 293 SPPDMGLPIALGLNWPDRLPGAcAPVDWTQAHTWEFFPLDHDAFPAVELAKKAQETSPTHMAVYNAANEEAVDAFHDGVI 372
Cdd:pfam13288   1 GPPDMRLPIAYALSYPERLSGV-EPLDLAKLGSLTFEEPDLERFPCLKLAYEALRAGGTAPAVLNAANEVAVAAFLAGKI 79

                  ....*
gi 2556527334 373 GFRKI 377
Cdd:pfam13288  80 GFLDI 84
COG4091 COG4091
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ...
40-159 2.96e-03

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


Pssm-ID: 443267 [Multi-domain]  Cd Length: 429  Bit Score: 39.75  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556527334  40 ARELAAQAVVFRPDVVGLAGAEGMSAD-----------DVRGGFMLHLAGAKEtAARNGGLELAGAGFVDvDAAGLDTYT 108
Cdd:COG4091     3 DRLLAARAAEGRPIRVGLIGAGQMGRGllaqirrmpgmEVVAIADRNPERARA-ALREAGIPEEDIRVVD-TAAEADAAI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2556527334 109 PE--LVVGEDAARACAALPdVDVVLNgVTGS--RGLRPTLAAIEAGSVVALANKE 159
Cdd:COG4091    81 AAgkTVVTDDAELLIAADG-IDVVVE-ATGVpeAGARHALAAIEAGKHVVMVNVE 133
 
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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