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Conserved domains on  [gi|489519099|ref|WP_003423903|]
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3-deoxy-7-phosphoheptulonate synthase [Clostridioides difficile]

Protein Classification

3-deoxy-7-phosphoheptulonate synthase( domain architecture ID 11483421)

3-deoxy-7-phosphoheptulonate synthase catalyzes the condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) to produce 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP), the first step of the shikimate pathway for aromatic amino acid biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08673 PRK08673
3-deoxy-7-phosphoheptulonate synthase; Reviewed
2-336 0e+00

3-deoxy-7-phosphoheptulonate synthase; Reviewed


:

Pssm-ID: 181535 [Multi-domain]  Cd Length: 335  Bit Score: 591.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099   2 IVVLKIGADKNEVKKLIEAIGREGVEVNPIDGTELTVLGLVGDTSKIDAKRIEANKIVEKVMHVVEPFKKANRKFHPEPS 81
Cdd:PRK08673   1 IIVMKPGATEEEIDEVIEEVESAGLKTHVSPGVERTVIGLIGDKGKVDAAKFEALPGVEEVVPVLKPYKLASREFKPEPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  82 IINVNGMEIGSKKIAMIAGPCSVETEEQIVSIAEDVKKSGAGFLRGGAFKPRTSPYAFQGLRYDGLDLLKKAKEKTGLPI 161
Cdd:PRK08673  81 VVKVGDVEIGGGKPVVIAGPCSVESEEQILEIARAVKEAGAQILRGGAFKPRTSPYSFQGLGEEGLKLLAEAREETGLPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 162 VTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIMAGGNENVVLCERGIRT 241
Cdd:PRK08673 161 VTEVMDPRDVELVAEYVDILQIGARNMQNFDLLKEVGKTNKPVLLKRGMSATIEEWLMAAEYILAEGNPNVILCERGIRT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 242 FETYTRNTLDLSAILAVKKLSHLPVIVDPSHAAGKSWMVDSLSKAAIAVGADGLIIEVHNDPAHALCDGKQSIKPNEYDE 321
Cdd:PRK08673 241 FETATRNTLDLSAVPVIKKLTHLPVIVDPSHATGKRDLVEPLALAAVAAGADGLIVEVHPDPEKALSDGPQSLTPEEFEE 320
                        330
                 ....*....|....*
gi 489519099 322 LISELKTIASAVGRE 336
Cdd:PRK08673 321 LMKKLRAIAEALGRE 335
 
Name Accession Description Interval E-value
PRK08673 PRK08673
3-deoxy-7-phosphoheptulonate synthase; Reviewed
2-336 0e+00

3-deoxy-7-phosphoheptulonate synthase; Reviewed


Pssm-ID: 181535 [Multi-domain]  Cd Length: 335  Bit Score: 591.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099   2 IVVLKIGADKNEVKKLIEAIGREGVEVNPIDGTELTVLGLVGDTSKIDAKRIEANKIVEKVMHVVEPFKKANRKFHPEPS 81
Cdd:PRK08673   1 IIVMKPGATEEEIDEVIEEVESAGLKTHVSPGVERTVIGLIGDKGKVDAAKFEALPGVEEVVPVLKPYKLASREFKPEPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  82 IINVNGMEIGSKKIAMIAGPCSVETEEQIVSIAEDVKKSGAGFLRGGAFKPRTSPYAFQGLRYDGLDLLKKAKEKTGLPI 161
Cdd:PRK08673  81 VVKVGDVEIGGGKPVVIAGPCSVESEEQILEIARAVKEAGAQILRGGAFKPRTSPYSFQGLGEEGLKLLAEAREETGLPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 162 VTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIMAGGNENVVLCERGIRT 241
Cdd:PRK08673 161 VTEVMDPRDVELVAEYVDILQIGARNMQNFDLLKEVGKTNKPVLLKRGMSATIEEWLMAAEYILAEGNPNVILCERGIRT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 242 FETYTRNTLDLSAILAVKKLSHLPVIVDPSHAAGKSWMVDSLSKAAIAVGADGLIIEVHNDPAHALCDGKQSIKPNEYDE 321
Cdd:PRK08673 241 FETATRNTLDLSAVPVIKKLTHLPVIVDPSHATGKRDLVEPLALAAVAAGADGLIVEVHPDPEKALSDGPQSLTPEEFEE 320
                        330
                 ....*....|....*
gi 489519099 322 LISELKTIASAVGRE 336
Cdd:PRK08673 321 LMKKLRAIAEALGRE 335
AroGA COG2876
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and ...
59-337 0e+00

3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and metabolism]; 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 442123  Cd Length: 283  Bit Score: 558.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  59 VEKVMHVVEPFKKANRKFHPEPSIINVNGMEIGSKKIAMIAGPCSVETEEQIVSIAEDVKKSGAGFLRGGAFKPRTSPYA 138
Cdd:COG2876    5 VEKVVRVSKPYKLASREFKPEDTVVDVGGVKIGGGELVVIAGPCAVESEEQILETAKAVKAAGAKILRGGAFKPRTSPYS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 139 FQGLRYDGLDLLKKAKEKTGLPIVTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWL 218
Cdd:COG2876   85 FQGLGEEGLKLLAEAREETGLPVVTEVMDPRDVELVAEYADILQIGARNMQNFELLKEVGRTGKPVLLKRGLSATIEEWL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 219 MSAEYIMAGGNENVVLCERGIRTFETYTRNTLDLSAILAVKKLSHLPVIVDPSHAAGKSWMVDSLSKAAIAVGADGLIIE 298
Cdd:COG2876  165 MAAEYILSEGNPNVILCERGIRTFETATRNTLDLSAVPVLKELTHLPVIVDPSHATGRRDLVPPMAKAAVAAGADGLMIE 244
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 489519099 299 VHNDPAHALCDGKQSIKPNEYDELISELKTIASAVGREI 337
Cdd:COG2876  245 VHPDPEKALSDGPQSLTPEEFAELMEELRKLAEAVGRRL 283
DAHP_synth_Bsub TIGR01361
3-deoxy-7-phosphoheptulonate synthase; This model describes one of at least three types of ...
70-329 5.45e-154

3-deoxy-7-phosphoheptulonate synthase; This model describes one of at least three types of phospho-2-dehydro-3-deoxyheptonate aldolase (DAHP synthase). This enzyme catalyzes the first of 7 steps in the biosynthesis of chorismate, that last common precursor of all three aromatic amino acids and of PABA, ubiquinone and menaquinone. Some members of this family, including an experimentally characterized member from Bacillus subtilis, are bifunctional, with a chorismate mutase domain N-terminal to this region. The member of this family from Synechocystis PCC 6803, CcmA, was shown to be essential for carboxysome formation. However, no other candidate for this enzyme is present in that species, chorismate biosynthesis does occur, other species having this protein lack carboxysomes but appear to make chorismate, and a requirement of CcmA for carboxysome formation does not prohibit a role in chorismate biosynthesis. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273577  Cd Length: 260  Bit Score: 432.15  E-value: 5.45e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099   70 KKANRKFHPEPSIINVNGMEIGSKKIAMIAGPCSVETEEQIVSIAEDVKKSGAGFLRGGAFKPRTSPYAFQGLRYDGLDL 149
Cdd:TIGR01361   1 KLVSRKFHPEKTVVDVGGVKIGEGSPIVIAGPCSVESEEQIMETARFVKEAGAKILRGGAFKPRTSPYSFQGLGEEGLKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  150 LKKAKEKTGLPIVTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIMAGGN 229
Cdd:TIGR01361  81 LRRAADEHGLPVVTEVMDPRDVEIVAEYADILQIGARNMQNFELLKEVGKQGKPVLLKRGMGNTIEEWLYAAEYILSSGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  230 ENVVLCERGIRTFETYTRNTLDLSAILAVKKLSHLPVIVDPSHAAGKSWMVDSLSKAAIAVGADGLIIEVHNDPAHALCD 309
Cdd:TIGR01361 161 GNVILCERGIRTFEKATRNTLDLSAVPVLKKETHLPIIVDPSHAAGRRDLVIPLAKAAIAAGADGLMIEVHPDPEKALSD 240
                         250       260
                  ....*....|....*....|
gi 489519099  310 GKQSIKPNEYDELISELKTI 329
Cdd:TIGR01361 241 SKQQLTPEEFKRLVKELRAL 260
DAHP_synth_1 pfam00793
DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino ...
94-333 1.84e-86

DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino acid biosynthesis from chorismate. E-coli has three related synthetases, which are inhibited by different aromatic amino acids. This family also includes KDSA which has very similar catalytic activity but is involved in the first step of liposaccharide biosynthesis. The enzyme is also part of the shikimate pathway, EC:2.5.1.54.


Pssm-ID: 395641  Cd Length: 271  Bit Score: 261.48  E-value: 1.84e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099   94 KIAMIAGPCSVETEEQIVSIAEDVKKSGA---GFLRGGAF--KPRTSPYAFQGLRYD-GLDLLKKAKEKTGLPIVTEIMS 167
Cdd:pfam00793  17 RLLVIAGPCSIEDPEAAMEYARRLKKLGAklkLIIIMRAYfeKPRTSPVGFKGLGNDpDLNILFRIKDGLGLPIATEVLD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  168 TQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIM-AGGNENVVLCERGIRTFETYT 246
Cdd:pfam00793  97 PIDPQYLADVVDIGQIGARTTESQDLLELAGGLSKPVGFKNGTDAAIDEMLAAAEYHLfLGVTKGNILCERGIRGGEGPN 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  247 RNTLDLSAILAVKKLS-HLPVIVDPSHAAG-----KSWMVDSLSKAAIAVGADGLIIEVHNDPAHALCDGKQSIKPNEYD 320
Cdd:pfam00793 177 RNTLDVSAVAILKEETgHLPVMVDVSHANGrkdggRQPLVLPLAKAAIAVGIDGLMIEVHPNPGNALSDGPQQLKYGKSE 256
                         250
                  ....*....|...
gi 489519099  321 ELISELKTIASAV 333
Cdd:pfam00793 257 TDACILWELTELL 269
 
Name Accession Description Interval E-value
PRK08673 PRK08673
3-deoxy-7-phosphoheptulonate synthase; Reviewed
2-336 0e+00

3-deoxy-7-phosphoheptulonate synthase; Reviewed


Pssm-ID: 181535 [Multi-domain]  Cd Length: 335  Bit Score: 591.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099   2 IVVLKIGADKNEVKKLIEAIGREGVEVNPIDGTELTVLGLVGDTSKIDAKRIEANKIVEKVMHVVEPFKKANRKFHPEPS 81
Cdd:PRK08673   1 IIVMKPGATEEEIDEVIEEVESAGLKTHVSPGVERTVIGLIGDKGKVDAAKFEALPGVEEVVPVLKPYKLASREFKPEPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  82 IINVNGMEIGSKKIAMIAGPCSVETEEQIVSIAEDVKKSGAGFLRGGAFKPRTSPYAFQGLRYDGLDLLKKAKEKTGLPI 161
Cdd:PRK08673  81 VVKVGDVEIGGGKPVVIAGPCSVESEEQILEIARAVKEAGAQILRGGAFKPRTSPYSFQGLGEEGLKLLAEAREETGLPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 162 VTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIMAGGNENVVLCERGIRT 241
Cdd:PRK08673 161 VTEVMDPRDVELVAEYVDILQIGARNMQNFDLLKEVGKTNKPVLLKRGMSATIEEWLMAAEYILAEGNPNVILCERGIRT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 242 FETYTRNTLDLSAILAVKKLSHLPVIVDPSHAAGKSWMVDSLSKAAIAVGADGLIIEVHNDPAHALCDGKQSIKPNEYDE 321
Cdd:PRK08673 241 FETATRNTLDLSAVPVIKKLTHLPVIVDPSHATGKRDLVEPLALAAVAAGADGLIVEVHPDPEKALSDGPQSLTPEEFEE 320
                        330
                 ....*....|....*
gi 489519099 322 LISELKTIASAVGRE 336
Cdd:PRK08673 321 LMKKLRAIAEALGRE 335
AroGA COG2876
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and ...
59-337 0e+00

3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and metabolism]; 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 442123  Cd Length: 283  Bit Score: 558.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  59 VEKVMHVVEPFKKANRKFHPEPSIINVNGMEIGSKKIAMIAGPCSVETEEQIVSIAEDVKKSGAGFLRGGAFKPRTSPYA 138
Cdd:COG2876    5 VEKVVRVSKPYKLASREFKPEDTVVDVGGVKIGGGELVVIAGPCAVESEEQILETAKAVKAAGAKILRGGAFKPRTSPYS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 139 FQGLRYDGLDLLKKAKEKTGLPIVTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWL 218
Cdd:COG2876   85 FQGLGEEGLKLLAEAREETGLPVVTEVMDPRDVELVAEYADILQIGARNMQNFELLKEVGRTGKPVLLKRGLSATIEEWL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 219 MSAEYIMAGGNENVVLCERGIRTFETYTRNTLDLSAILAVKKLSHLPVIVDPSHAAGKSWMVDSLSKAAIAVGADGLIIE 298
Cdd:COG2876  165 MAAEYILSEGNPNVILCERGIRTFETATRNTLDLSAVPVLKELTHLPVIVDPSHATGRRDLVPPMAKAAVAAGADGLMIE 244
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 489519099 299 VHNDPAHALCDGKQSIKPNEYDELISELKTIASAVGREI 337
Cdd:COG2876  245 VHPDPEKALSDGPQSLTPEEFAELMEELRKLAEAVGRRL 283
DAHP_synth_Bsub TIGR01361
3-deoxy-7-phosphoheptulonate synthase; This model describes one of at least three types of ...
70-329 5.45e-154

3-deoxy-7-phosphoheptulonate synthase; This model describes one of at least three types of phospho-2-dehydro-3-deoxyheptonate aldolase (DAHP synthase). This enzyme catalyzes the first of 7 steps in the biosynthesis of chorismate, that last common precursor of all three aromatic amino acids and of PABA, ubiquinone and menaquinone. Some members of this family, including an experimentally characterized member from Bacillus subtilis, are bifunctional, with a chorismate mutase domain N-terminal to this region. The member of this family from Synechocystis PCC 6803, CcmA, was shown to be essential for carboxysome formation. However, no other candidate for this enzyme is present in that species, chorismate biosynthesis does occur, other species having this protein lack carboxysomes but appear to make chorismate, and a requirement of CcmA for carboxysome formation does not prohibit a role in chorismate biosynthesis. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 273577  Cd Length: 260  Bit Score: 432.15  E-value: 5.45e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099   70 KKANRKFHPEPSIINVNGMEIGSKKIAMIAGPCSVETEEQIVSIAEDVKKSGAGFLRGGAFKPRTSPYAFQGLRYDGLDL 149
Cdd:TIGR01361   1 KLVSRKFHPEKTVVDVGGVKIGEGSPIVIAGPCSVESEEQIMETARFVKEAGAKILRGGAFKPRTSPYSFQGLGEEGLKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  150 LKKAKEKTGLPIVTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIMAGGN 229
Cdd:TIGR01361  81 LRRAADEHGLPVVTEVMDPRDVEIVAEYADILQIGARNMQNFELLKEVGKQGKPVLLKRGMGNTIEEWLYAAEYILSSGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  230 ENVVLCERGIRTFETYTRNTLDLSAILAVKKLSHLPVIVDPSHAAGKSWMVDSLSKAAIAVGADGLIIEVHNDPAHALCD 309
Cdd:TIGR01361 161 GNVILCERGIRTFEKATRNTLDLSAVPVLKKETHLPIIVDPSHAAGRRDLVIPLAKAAIAAGADGLMIEVHPDPEKALSD 240
                         250       260
                  ....*....|....*....|
gi 489519099  310 GKQSIKPNEYDELISELKTI 329
Cdd:TIGR01361 241 SKQQLTPEEFKRLVKELRAL 260
PRK13396 PRK13396
3-deoxy-7-phosphoheptulonate synthase; Provisional
1-335 1.51e-143

3-deoxy-7-phosphoheptulonate synthase; Provisional


Pssm-ID: 237376 [Multi-domain]  Cd Length: 352  Bit Score: 409.53  E-value: 1.51e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099   1 MIVVLKIGADKNEVKKLIEAIGREGVEVNPIDGTELTVLGLVGDTSKIDAKRI-EANKIVEKVMHVVEPFKKANRKF-HP 78
Cdd:PRK13396   1 MIIVMKVGTPEAEIERISQELTSWGLTPEKIVGKHKVVIGLVGDTAELDPLQIqELSPWIEQVLRVEKPFKRASREYrHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  79 EPSIINVNG----MEIG-SKKIAMIAGPCSVETEEQIVSIAEDVKKSGAGFLRGGAFKPRTSPYAFQGLRYDGLDLLKKA 153
Cdd:PRK13396  81 EASEVVVPTpngpVPFGeNHPVVVVAGPCSVENEEMIVETAKRVKAAGAKFLRGGAYKPRTSPYAFQGHGESALELLAAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 154 KEKTGLPIVTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIMAGGNENVV 233
Cdd:PRK13396 161 REATGLGIITEVMDAADLEKIAEVADVIQVGARNMQNFSLLKKVGAQDKPVLLKRGMAATIDEWLMAAEYILAAGNPNVI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 234 LCERGIRTFET-YTRNTLDLSAILAVKKLSHLPVIVDPSHAAGKSWMVDSLSKAAIAVGADGLIIEVHNDPAHALCDGKQ 312
Cdd:PRK13396 241 LCERGIRTFDRqYTRNTLDLSVIPVLRSLTHLPIMIDPSHGTGKSEYVPSMAMAAIAAGTDSLMIEVHPNPAKALSDGPQ 320
                        330       340
                 ....*....|....*....|...
gi 489519099 313 SIKPNEYDELISELKTIASAVGR 335
Cdd:PRK13396 321 SLTPDRFDRLMQELAVIGKTVGR 343
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
74-332 9.32e-131

bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 377.39  E-value: 9.32e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  74 RKFHPEPSIINVNGMEIGSKKIAMIAGPCSVETEEQIVSIAEDVKKSGAGFLRGGAFKPRTSPYAFQGLRYDGLDLLKKA 153
Cdd:PRK12595  98 RKKKPEDTIVDVKGEVIGDGNQSFIFGPCSVESYEQVEAVAKALKAKGLKLLRGGAFKPRTSPYDFQGLGVEGLKILKQV 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 154 KEKTGLPIVTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIMAGGNENVV 233
Cdd:PRK12595 178 ADEYGLAVISEIVNPADVEVALDYVDVIQIGARNMQNFELLKAAGRVNKPVLLKRGLSATIEEFIYAAEYIMSQGNGQII 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 234 LCERGIRTFETYTRNTLDLSAILAVKKLSHLPVIVDPSHAAGKSWMVDSLSKAAIAVGADGLIIEVHNDPAHALCDGKQS 313
Cdd:PRK12595 258 LCERGIRTYEKATRNTLDISAVPILKQETHLPVMVDVTHSTGRRDLLLPTAKAALAIGADGVMAEVHPDPAVALSDSAQQ 337
                        250
                 ....*....|....*....
gi 489519099 314 IKPNEYDELISELKTIASA 332
Cdd:PRK12595 338 MDIPEFDRFLDELKPLANK 356
DAHP_synth_1 pfam00793
DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino ...
94-333 1.84e-86

DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino acid biosynthesis from chorismate. E-coli has three related synthetases, which are inhibited by different aromatic amino acids. This family also includes KDSA which has very similar catalytic activity but is involved in the first step of liposaccharide biosynthesis. The enzyme is also part of the shikimate pathway, EC:2.5.1.54.


Pssm-ID: 395641  Cd Length: 271  Bit Score: 261.48  E-value: 1.84e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099   94 KIAMIAGPCSVETEEQIVSIAEDVKKSGA---GFLRGGAF--KPRTSPYAFQGLRYD-GLDLLKKAKEKTGLPIVTEIMS 167
Cdd:pfam00793  17 RLLVIAGPCSIEDPEAAMEYARRLKKLGAklkLIIIMRAYfeKPRTSPVGFKGLGNDpDLNILFRIKDGLGLPIATEVLD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  168 TQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIM-AGGNENVVLCERGIRTFETYT 246
Cdd:pfam00793  97 PIDPQYLADVVDIGQIGARTTESQDLLELAGGLSKPVGFKNGTDAAIDEMLAAAEYHLfLGVTKGNILCERGIRGGEGPN 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  247 RNTLDLSAILAVKKLS-HLPVIVDPSHAAG-----KSWMVDSLSKAAIAVGADGLIIEVHNDPAHALCDGKQSIKPNEYD 320
Cdd:pfam00793 177 RNTLDVSAVAILKEETgHLPVMVDVSHANGrkdggRQPLVLPLAKAAIAVGIDGLMIEVHPNPGNALSDGPQQLKYGKSE 256
                         250
                  ....*....|...
gi 489519099  321 ELISELKTIASAV 333
Cdd:pfam00793 257 TDACILWELTELL 269
PRK05198 PRK05198
2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
86-333 7.53e-41

2-dehydro-3-deoxyphosphooctonate aldolase; Provisional


Pssm-ID: 235363  Cd Length: 264  Bit Score: 143.69  E-value: 7.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  86 NGMEIG-SKKIAMIAGPCSVETEEQIVSIAEDVK----KSGAGFLRGGAFKP--RTSPYAFQGLRYD-GLDLLKKAKEKT 157
Cdd:PRK05198   1 GDIEVGnDLPFFLIAGPCVIESRDLALRIAEHLKeitdKLGIPYVFKASFDKanRSSIHSFRGPGLEeGLKILQEVKETF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 158 GLPIVTEIMSTQDIDIFEENVDVIQVGArnmqnF-----DLLKELGKTNKTILLKRG--LSAtieeWLM--SAEYIMAGG 228
Cdd:PRK05198  81 GVPVLTDVHEPEQAAPVAEVVDVLQIPA-----FlcrqtDLLVAAAKTGKVVNIKKGqfLAP----WDMknVVDKVREAG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 229 NENVVLCERGIrTFeTYtrNTL--DLSAILAVKKLSHlPVIVDPSHAA-----------GKSWMVDSLSKAAIAVGADGL 295
Cdd:PRK05198 152 NDKIILCERGT-SF-GY--NNLvvDMRGLPIMRETGA-PVIFDATHSVqlpggqggssgGQREFVPVLARAAVAVGVAGL 226
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489519099 296 IIEVHNDPAHALCDGKQSIKPNEYDELISELKTIASAV 333
Cdd:PRK05198 227 FIETHPDPDNALSDGPNMLPLDKLEPLLEQLKAIDDLV 264
PLN03033 PLN03033
2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
97-332 2.40e-29

2-dehydro-3-deoxyphosphooctonate aldolase; Provisional


Pssm-ID: 178601  Cd Length: 290  Bit Score: 113.80  E-value: 2.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099  97 MIAGPCSVETEEQIVSIAEDVK----KSGAGFLRGGAFKP--RTSPYAFQGLRY-DGLDLLKKAKEKTGLPIVTEIMSTQ 169
Cdd:PLN03033  19 LLAGPNVIESEEHILRMAKHIKdistKLGLPLVFKSSFDKanRTSSKSFRGPGMaEGLKILEKVKVAYDLPIVTDVHESS 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 170 DIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLSATIEEWLMSAEYIMAGGNENVVLCERGirTFETYTRNT 249
Cdd:PLN03033  99 QCEAVGKVADIIQIPAFLCRQTDLLVAAAKTGKIINIKKGQFCAPSVMRNSAEKVRLAGNPNVMVCERG--TMFGYNDLI 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 250 LDLSAILAVKKlSHLPVIVDPSHA----AGKSW------------MVDSLSKAAIAVGADGLIIEVHNDPAHALCDGKQS 313
Cdd:PLN03033 177 VDPRNLEWMRE-ANCPVVADITHSlqqpAGKKLdgggvasgglreLIPCIARTAVAVGVDGIFMEVHDDPLSAPVDGPTQ 255
                        250
                 ....*....|....*....
gi 489519099 314 IKPNEYDELISELKTIASA 332
Cdd:PLN03033 256 WPLRHLEELLEELIAIARV 274
PRK12457 PRK12457
3-deoxy-8-phosphooctulonate synthase;
133-335 2.56e-21

3-deoxy-8-phosphooctulonate synthase;


Pssm-ID: 237105  Cd Length: 281  Bit Score: 91.73  E-value: 2.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 133 RTSPYAFQGLRYD-GLDLLKKAKEKTGLPIVTEIMSTQDIDIFEENVDVIQVGARNMQNFDLLKELGKTNKTILLKRGLS 211
Cdd:PRK12457  61 RSSIHSYRGVGLDeGLRIFEEVKARFGVPVITDVHEVEQAAPVAEVADVLQVPAFLARQTDLVVAIAKTGKPVNIKKPQF 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489519099 212 ATIEEWLMSAEYIMAGGNENVVLCERGirTFETYTRNTLDLSAILAVKKLS-HLPVIVDPSHA-----------AGKSWM 279
Cdd:PRK12457 141 MSPTQMKHVVSKCREAGNDRVILCERG--SSFGYDNLVVDMLGFRQMKRTTgDLPVIFDVTHSlqcrdplgaasGGRRRQ 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489519099 280 VDSLSKAAIAVGADGLIIEVHNDPAHALCDGKQSIKPNEYDELISELKTIASAVGR 335
Cdd:PRK12457 219 VLDLARAGMAVGLAGLFLEAHPDPDRARCDGPSALPLDQLEPFLSQVKALDDLVKS 274
DAHP_snth_FXD pfam18152
DAHP synthase ferredoxin-like domain; This domain is found in ...
1-67 1.50e-20

DAHP synthase ferredoxin-like domain; This domain is found in 3-Deoxy-d-arabino-heptulosonate-7-phosphate synthase (DAHPS) present in Thermotoga maritime. DAHPS catalyzes the first reaction of the aromatic biosynthetic pathway in bacteria, fungi, and plants, the condensation of PEP and E4P with the formation of DAHP. The domain is ferredoxin-like and is thought to play a critical role in feedback regulation of the enzyme.


Pssm-ID: 436312 [Multi-domain]  Cd Length: 67  Bit Score: 83.68  E-value: 1.50e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489519099    1 MIVVLKIGADKNEVKKLIEAIGREGVEVNPIDGTELTVLGLVGDTSKIDAKRIEANKIVEKVMHVVE 67
Cdd:pfam18152   1 MIIVMKPGATEEEIDEVIERIESLGLKVHVSRGTERTVIGLIGDTSKLDAEQLEALPGVERVVRVSK 67
 
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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