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Conserved domains on  [gi|545668057|ref|WP_021774397|]
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1-deoxy-D-xylulose-5-phosphate reductoisomerase [Oribacterium sp. oral taxon 078]

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]; ...
1-384 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: 599.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057   1 MRNIVILGSSGSIGRQAVDVIARDPE-LRISGLAVRSSISLLREQTERFRPEAVCVFEREAAERFSS--FGLPVRVLSGM 77
Cdd:COG0743    1 MKRIAILGSTGSIGTQTLDVIRRHPDrFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREalAGSGIEVLAGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  78 EGLIELSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAGHLIMPLLKECRTELRPIDSEHSAIWQSLMG 157
Cdd:COG0743   81 EALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEHGAQLLPVDSEHSAIFQCLPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 158 EDPESLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEAKWLFSVPPEKITVLIQP 237
Cdd:COG0743  161 EDREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDSATMMNKGLEVIEAHWLFDVPPDQIEVVVHP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 238 ESIIHSAVQFKDGSVKAQLGAADMRIPIEYALYAPSRRFLPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGGSLP 317
Cdd:COG0743  241 QSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDLAKLGTLTFEPPDEERFPCLRLAYEALRAGGTAP 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668057 318 TIYNAANEEAVASFLRGEIGFLRIAELVEEAMRAHEegYLPNPDLSEILEAERWAREFVRKRKEGRA 384
Cdd:COG0743  321 AVLNAANEVAVAAFLAGRIGFLDIADVVEKVLERHP--PIAPPSLEDVLEADAWARRRARELIARLA 385
 
Name Accession Description Interval E-value
Dxr COG0743
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
1-384 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: 599.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057   1 MRNIVILGSSGSIGRQAVDVIARDPE-LRISGLAVRSSISLLREQTERFRPEAVCVFEREAAERFSS--FGLPVRVLSGM 77
Cdd:COG0743    1 MKRIAILGSTGSIGTQTLDVIRRHPDrFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREalAGSGIEVLAGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  78 EGLIELSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAGHLIMPLLKECRTELRPIDSEHSAIWQSLMG 157
Cdd:COG0743   81 EALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEHGAQLLPVDSEHSAIFQCLPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 158 EDPESLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEAKWLFSVPPEKITVLIQP 237
Cdd:COG0743  161 EDREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDSATMMNKGLEVIEAHWLFDVPPDQIEVVVHP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 238 ESIIHSAVQFKDGSVKAQLGAADMRIPIEYALYAPSRRFLPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGGSLP 317
Cdd:COG0743  241 QSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDLAKLGTLTFEPPDEERFPCLRLAYEALRAGGTAP 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668057 318 TIYNAANEEAVASFLRGEIGFLRIAELVEEAMRAHEegYLPNPDLSEILEAERWAREFVRKRKEGRA 384
Cdd:COG0743  321 AVLNAANEVAVAAFLAGRIGFLDIADVVEKVLERHP--PIAPPSLEDVLEADAWARRRARELIARLA 385
PRK05447 PRK05447
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
1-384 0e+00

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


Pssm-ID: 235472  Cd Length: 385  Bit Score: 582.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057   1 MRNIVILGSSGSIGRQAVDVIARDPE-LRISGLAVRSSISLLREQTERFRPEAVCVFEREAAERFSS--FGLPVRVLSGM 77
Cdd:PRK05447   1 MKRITILGSTGSIGTQTLDVIRRNPDrFRVVALSAGKNVELLAEQAREFRPKYVVVADEEAAKELKEalAAAGIEVLAGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  78 EGLIELSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAGHLIMPLLKECRTELRPIDSEHSAIWQSLMG 157
Cdd:PRK05447  81 EGLCELAALPEADVVVAAIVGAAGLLPTLAAIRAGKRIALANKESLVCAGELVMDAAKKSGAQILPVDSEHSAIFQCLPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 158 EDPESLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEAKWLFSVPPEKITVLIQP 237
Cdd:PRK05447 161 EKQEGVEKIILTASGGPFRDWPLEELANVTPEQALKHPNWSMGRKITIDSATMMNKGLEVIEAHWLFGLPYEQIEVVIHP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 238 ESIIHSAVQFKDGSVKAQLGAADMRIPIEYALYAPSRRFLPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGGSLP 317
Cdd:PRK05447 241 QSIIHSMVEYVDGSVLAQLGPPDMRLPIAYALAYPERVPSGVKPLDLTKLGTLTFEPPDFERFPCLKLAYEALKAGGTAP 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668057 318 TIYNAANEEAVASFLRGEIGFLRIAELVEEAMRAHEEgylPNPDLSEILEAERWAREFVRKRKEGRA 384
Cdd:PRK05447 321 AVLNAANEVAVAAFLAGKIGFLDIADLIEKVLERHNP---EPPSLEDVLEADAEARERARELIARLA 384
Dxr TIGR00243
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
1-378 3.25e-149

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: 427.31  E-value: 3.25e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057    1 MRNIVILGSSGSIGRQAVDVIARDPE-LRISGLAVRSSISLLREQTERFRPEAVCVFEREAAERF----SSFGLPVRVLS 75
Cdd:TIGR00243   1 MKQIVILGSTGSIGKSTLDVVRHNPDhFQVVALSAGKNVALMVEQILEFRPKFVAIDDEASLKDLktmlQQQGSRTEVLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057   76 GMEGLIELSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAGHLIMPLLKECRTELRPIDSEHSAIWQSL 155
Cdd:TIGR00243  81 GEEGICEMAALEDVDQVMNAIVGAAGLLPTLAAIRAGKTIALANKESLVTAGHLFLDAVKKYGVQLLPVDSEHNAIFQSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  156 MGEDPE-SLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEAKWLFSVPPEKITVL 234
Cdd:TIGR00243 161 QHGLEElGVVSIILTASGGAFRDTPLEDLPTVTPQQALKHPNWSMGRKITIDSATMMNKGLEYIEARWLFGASAEQIDVL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  235 IQPESIIHSAVQFKDGSVKAQLGAADMRIPIEYALYAPSRRFLPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGG 314
Cdd:TIGR00243 241 IHPQSIIHSMVEFQDGSVIAQLGEPDMRLPIAYAMAWPNRVNSGVKPLDLCKLSALTFEEPDFDRYPCLKLAMEAFKAGQ 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668057  315 SLPTIYNAANEEAVASFLRGEIGFLRIAELVEEAMRAHEEgyLPNPDLSEILEAERWAREFVRK 378
Cdd:TIGR00243 321 AATTVLNAANEVAVAAFLAQQIRFLDIAALISKVLYRMQP--RKPQSLEDVLEVDKNARETARK 382
DXP_redisom_C pfam08436
1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the ...
141-224 2.40e-57

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: 181.82  E-value: 2.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  141 LRPIDSEHSAIWQSLMGEDPESLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEA 220
Cdd:pfam08436   1 ILPVDSEHSAIFQCLPGGSQGEVEKIILTASGGPFRGKPREELANVTPEQALKHPNWSMGAKITIDSATMMNKGLEVIEA 80

                  ....
gi 545668057  221 KWLF 224
Cdd:pfam08436  81 HWLF 84
 
Name Accession Description Interval E-value
Dxr COG0743
1-deoxy-D-xylulose 5-phosphate reductoisomerase [Lipid transport and metabolism]; ...
1-384 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: 599.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057   1 MRNIVILGSSGSIGRQAVDVIARDPE-LRISGLAVRSSISLLREQTERFRPEAVCVFEREAAERFSS--FGLPVRVLSGM 77
Cdd:COG0743    1 MKRIAILGSTGSIGTQTLDVIRRHPDrFRVVALAAGSNVELLAEQAREFRPEYVVVADEAAAEELREalAGSGIEVLAGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  78 EGLIELSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAGHLIMPLLKECRTELRPIDSEHSAIWQSLMG 157
Cdd:COG0743   81 EALIEVAALPEVDVVMAAIVGAAGLLPTLAAIRAGKRIALANKESLVVAGELVMAAAKEHGAQLLPVDSEHSAIFQCLPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 158 EDPESLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEAKWLFSVPPEKITVLIQP 237
Cdd:COG0743  161 EDREGVERIILTASGGPFRGRPREELANVTPEQALAHPNWSMGRKITIDSATMMNKGLEVIEAHWLFDVPPDQIEVVVHP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 238 ESIIHSAVQFKDGSVKAQLGAADMRIPIEYALYAPSRRFLPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGGSLP 317
Cdd:COG0743  241 QSIIHSMVEFVDGSVLAQLGPPDMRLPIAYALAYPERIPSGVPPLDLAKLGTLTFEPPDEERFPCLRLAYEALRAGGTAP 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668057 318 TIYNAANEEAVASFLRGEIGFLRIAELVEEAMRAHEegYLPNPDLSEILEAERWAREFVRKRKEGRA 384
Cdd:COG0743  321 AVLNAANEVAVAAFLAGRIGFLDIADVVEKVLERHP--PIAPPSLEDVLEADAWARRRARELIARLA 385
PRK05447 PRK05447
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
1-384 0e+00

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


Pssm-ID: 235472  Cd Length: 385  Bit Score: 582.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057   1 MRNIVILGSSGSIGRQAVDVIARDPE-LRISGLAVRSSISLLREQTERFRPEAVCVFEREAAERFSS--FGLPVRVLSGM 77
Cdd:PRK05447   1 MKRITILGSTGSIGTQTLDVIRRNPDrFRVVALSAGKNVELLAEQAREFRPKYVVVADEEAAKELKEalAAAGIEVLAGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  78 EGLIELSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAGHLIMPLLKECRTELRPIDSEHSAIWQSLMG 157
Cdd:PRK05447  81 EGLCELAALPEADVVVAAIVGAAGLLPTLAAIRAGKRIALANKESLVCAGELVMDAAKKSGAQILPVDSEHSAIFQCLPG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 158 EDPESLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEAKWLFSVPPEKITVLIQP 237
Cdd:PRK05447 161 EKQEGVEKIILTASGGPFRDWPLEELANVTPEQALKHPNWSMGRKITIDSATMMNKGLEVIEAHWLFGLPYEQIEVVIHP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 238 ESIIHSAVQFKDGSVKAQLGAADMRIPIEYALYAPSRRFLPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGGSLP 317
Cdd:PRK05447 241 QSIIHSMVEYVDGSVLAQLGPPDMRLPIAYALAYPERVPSGVKPLDLTKLGTLTFEPPDFERFPCLKLAYEALKAGGTAP 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668057 318 TIYNAANEEAVASFLRGEIGFLRIAELVEEAMRAHEEgylPNPDLSEILEAERWAREFVRKRKEGRA 384
Cdd:PRK05447 321 AVLNAANEVAVAAFLAGKIGFLDIADLIEKVLERHNP---EPPSLEDVLEADAEARERARELIARLA 384
PRK12464 PRK12464
1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional
6-376 3.28e-154

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


Pssm-ID: 237107  Cd Length: 383  Bit Score: 439.60  E-value: 3.28e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057   6 ILGSSGSIGRQAVDVIARDPE-LRISGLAVRSSISLLREQTERFRPEAVCVFEREAAERFSS--FGLPVRVLSGMEGLIE 82
Cdd:PRK12464   1 ILGSTGSIGTSALDVVSAHPEhFKVVGLTANYNIELLEQQIKRFQPRIVSVADKELADTLRTrlSANTSKITYGTDGLIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  83 LSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAGHLIMPLLKECRTELRPIDSEHSAIWQSLMGEDPES 162
Cdd:PRK12464  81 VATHPGSDLVLSSVVGAAGLLPTIEALKAKKDIALANKETLVAAGHIVTDLAKQNGCRLIPVDSEHSAIFQCLNGENNKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 163 LERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEAKWLFSVPPEKITVLIQPESIIH 242
Cdd:PRK12464 161 IDKLIVTASGGAFRDKTREEMATLTAKDALKHPNWLMGAKLTIDSATLMNKGFEVIEAHWLFDIPYEKIDVLIHKESIIH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 243 SAVQFKDGSVKAQLGAADMRIPIEYALYAPSRRFLPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGGSLPTIYNA 322
Cdd:PRK12464 241 SLVEFIDGSVLAQLGAPDMRMPIQYAFHYPTRLPSSYEKLNLLEIGSLHFEKPDLEKFPCLQYAYEAGKIGGTTPAVLNA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 545668057 323 ANEEAVASFLRGEIGFLRIAELVEEAMRAHEEgyLPNPDLSEILEAERWAREFV 376
Cdd:PRK12464 321 ANEIANALFLKNRIAFFDIEKTIYATLEAHHN--VKDPSLDDILEADAWARRYA 372
Dxr TIGR00243
1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1-deoxy-D-xylulose 5-phosphate is converted ...
1-378 3.25e-149

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: 427.31  E-value: 3.25e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057    1 MRNIVILGSSGSIGRQAVDVIARDPE-LRISGLAVRSSISLLREQTERFRPEAVCVFEREAAERF----SSFGLPVRVLS 75
Cdd:TIGR00243   1 MKQIVILGSTGSIGKSTLDVVRHNPDhFQVVALSAGKNVALMVEQILEFRPKFVAIDDEASLKDLktmlQQQGSRTEVLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057   76 GMEGLIELSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAGHLIMPLLKECRTELRPIDSEHSAIWQSL 155
Cdd:TIGR00243  81 GEEGICEMAALEDVDQVMNAIVGAAGLLPTLAAIRAGKTIALANKESLVTAGHLFLDAVKKYGVQLLPVDSEHNAIFQSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  156 MGEDPE-SLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEAKWLFSVPPEKITVL 234
Cdd:TIGR00243 161 QHGLEElGVVSIILTASGGAFRDTPLEDLPTVTPQQALKHPNWSMGRKITIDSATMMNKGLEYIEARWLFGASAEQIDVL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  235 IQPESIIHSAVQFKDGSVKAQLGAADMRIPIEYALYAPSRRFLPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGG 314
Cdd:TIGR00243 241 IHPQSIIHSMVEFQDGSVIAQLGEPDMRLPIAYAMAWPNRVNSGVKPLDLCKLSALTFEEPDFDRYPCLKLAMEAFKAGQ 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545668057  315 SLPTIYNAANEEAVASFLRGEIGFLRIAELVEEAMRAHEEgyLPNPDLSEILEAERWAREFVRK 378
Cdd:TIGR00243 321 AATTVLNAANEVAVAAFLAQQIRFLDIAALISKVLYRMQP--RKPQSLEDVLEVDKNARETARK 382
PLN02696 PLN02696
1-deoxy-D-xylulose-5-phosphate reductoisomerase
4-377 8.76e-124

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


Pssm-ID: 215374  Cd Length: 454  Bit Score: 364.88  E-value: 8.76e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057   4 IVILGSSGSIGRQAVDVIARDPE-LRISGLAVRSSISLLREQTERFRPEAVCVFEREAA----ERFSSFGLPVRVLSGME 78
Cdd:PLN02696  60 ISLLGSTGSIGTQTLDIVAENPDkFKVVALAAGSNVTLLADQVRKFKPKLVAVRNESLVdelkEALADLDDKPEIIPGEE 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  79 GLIELSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAGHLIMPLLKECRTELRPIDSEHSAIWQSLMGE 158
Cdd:PLN02696 140 GIVEVARHPEAVTVVTGIVGCAGLKPTVAAIEAGKDIALANKETLIAGGPFVLPLAKKHGVKILPADSEHSAIFQCIQGL 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 159 DPESLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEAKWLFSVPPEKITVLIQPE 238
Cdd:PLN02696 220 PEGGLRRIILTASGGAFRDWPVEKLKEVKVADALKHPNWSMGKKITVDSATLMNKGLEVIEAHYLFGADYDDIDIVIHPQ 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057 239 SIIHSAVQFKDGSVKAQLGAADMRIPIEYALYAPSRRF---LPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGGS 315
Cdd:PLN02696 300 SIIHSMVETQDSSVLAQLGWPDMRLPILYTMSWPDRVPcseITWPRLDLCKLGSLTFKAPDNVKYPSMDLAYAAGRAGGT 379
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545668057 316 LPTIYNAANEEAVASFLRGEIGFLRIAELVEEAMRAHEEGYLPNPDLSEILEAERWAREFVR 377
Cdd:PLN02696 380 MTGVLSAANEKAVEMFIDEKIGYLDIFKVIELTCEAHKEELVTSPSLEDILHYDLWAREYAA 441
DXP_redisom_C pfam08436
1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal domain; This domain is found to the ...
141-224 2.40e-57

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: 181.82  E-value: 2.40e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  141 LRPIDSEHSAIWQSLMGEDPESLERILLTASGGPFRGLKREELKNKTKEDALKHPNWSMGRKITVDSATLINKGLEFIEA 220
Cdd:pfam08436   1 ILPVDSEHSAIFQCLPGGSQGEVEKIILTASGGPFRGKPREELANVTPEQALKHPNWSMGAKITIDSATMMNKGLEVIEA 80

                  ....
gi 545668057  221 KWLF 224
Cdd:pfam08436  81 HWLF 84
DXPR_C pfam13288
DXP reductoisomerase C-terminal domain; This is the C-terminal domain of the ...
257-375 3.80e-52

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: 169.52  E-value: 3.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057  257 GAADMRIPIEYALYAPSRRfLPAARLDFAALSCLHFERPDTETFRGLFWGIEAGKRGGSLPTIYNAANEEAVASFLRGEI 336
Cdd:pfam13288   1 GPPDMRLPIAYALSYPERL-SGVEPLDLAKLGSLTFEEPDLERFPCLKLAYEALRAGGTAPAVLNAANEVAVAAFLAGKI 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 545668057  337 GFLRIAELVEEAMRAHEegYLPNPDLSEILEAERWAREF 375
Cdd:pfam13288  80 GFLDIPDIIEKVLEAHD--GIEPPSLEDILEADAEAREY 116
DXP_reductoisom pfam02670
1-deoxy-D-xylulose 5-phosphate reductoisomerase; This is a family of 1-deoxy-D-xylulose ...
4-127 2.28e-44

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: 149.55  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668057    4 IVILGSSGSIGRQAVDVIARDPEL-RISGLAVRSSISLLREQTERFRPEAVCVFEREAAERFSSF--GLPVRVLSGMEGL 80
Cdd:pfam02670   1 ITILGSTGSIGTQTLDVIRRHPDRfEVVALAAGRNVELLAEQIKEFKPKYVAVADEEAAEELKAAlaGTGTEVLAGEEGL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 545668057   81 IELSEMEDFDDLLVSLVGMIGIEPTIAAIRKRKRILLANKETLVCAG 127
Cdd:pfam02670  81 CEVAALPEADIVMAAIVGAAGLLPTLAAIKAGKRIALANKESLVAAG 127
 
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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