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Conserved domains on  [gi|1533683560|gb|RSB08357|]
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3-deoxy-7-phosphoheptulonate synthase [Enterococcus faecium]

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
2-335 0e+00

3-deoxy-7-phosphoheptulonate synthase; Reviewed


:

Pssm-ID: 181535 [Multi-domain]  Cd Length: 335  Bit Score: 548.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560   2 IVIMKKEATEEQIKKVVDHIEKEGFKVSIDQGTERVVIGLKGDTRSLQEGAFTRYEGVENAVRILNTYKLTSREFHPGNT 81
Cdd:PRK08673    1 IIVMKPGATEEEIDEVIEEVESAGLKTHVSPGVERTVIGLIGDKGKVDAAKFEALPGVEEVVPVLKPYKLASREFKPEPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  82 VVDVDGVKIGDGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKPRTSPYAFQGLEEEGLKYIRQAADEFGMKV 161
Cdd:PRK08673   81 VVKVGDVEIGGGKPVVIAGPCSVESEEQILEIARAVKEAGAQILRGGAFKPRTSPYSFQGLGEEGLKLLAEAREETGLPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 162 ITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDKSPVIFIERGIRT 241
Cdd:PRK08673  161 VTEVMDPRDVELVAEYVDILQIGARNMQNFDLLKEVGKTNKPVLLKRGMSATIEEWLMAAEYILAEGNPNVILCERGIRT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 242 YETATRNTFDLSAVPLMKKLTHFPVIVDPSHGTGIWELVPPMARAGVASGADGMIVEIHPDPANAWSDGPQSLNEKTYSR 321
Cdd:PRK08673  241 FETATRNTLDLSAVPVIKKLTHLPVIVDPSHATGKRDLVEPLALAAVAAGADGLIVEVHPDPEKALSDGPQSLTPEEFEE 320
                         330
                  ....*....|....
gi 1533683560 322 MMKEVAIMKEAMEK 335
Cdd:PRK08673  321 LMKKLRAIAEALGR 334
 
Name Accession Description Interval E-value
PRK08673 PRK08673
3-deoxy-7-phosphoheptulonate synthase; Reviewed
2-335 0e+00

3-deoxy-7-phosphoheptulonate synthase; Reviewed


Pssm-ID: 181535 [Multi-domain]  Cd Length: 335  Bit Score: 548.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560   2 IVIMKKEATEEQIKKVVDHIEKEGFKVSIDQGTERVVIGLKGDTRSLQEGAFTRYEGVENAVRILNTYKLTSREFHPGNT 81
Cdd:PRK08673    1 IIVMKPGATEEEIDEVIEEVESAGLKTHVSPGVERTVIGLIGDKGKVDAAKFEALPGVEEVVPVLKPYKLASREFKPEPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  82 VVDVDGVKIGDGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKPRTSPYAFQGLEEEGLKYIRQAADEFGMKV 161
Cdd:PRK08673   81 VVKVGDVEIGGGKPVVIAGPCSVESEEQILEIARAVKEAGAQILRGGAFKPRTSPYSFQGLGEEGLKLLAEAREETGLPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 162 ITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDKSPVIFIERGIRT 241
Cdd:PRK08673  161 VTEVMDPRDVELVAEYVDILQIGARNMQNFDLLKEVGKTNKPVLLKRGMSATIEEWLMAAEYILAEGNPNVILCERGIRT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 242 YETATRNTFDLSAVPLMKKLTHFPVIVDPSHGTGIWELVPPMARAGVASGADGMIVEIHPDPANAWSDGPQSLNEKTYSR 321
Cdd:PRK08673  241 FETATRNTLDLSAVPVIKKLTHLPVIVDPSHATGKRDLVEPLALAAVAAGADGLIVEVHPDPEKALSDGPQSLTPEEFEE 320
                         330
                  ....*....|....
gi 1533683560 322 MMKEVAIMKEAMEK 335
Cdd:PRK08673  321 LMKKLRAIAEALGR 334
AroGA COG2876
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and ...
57-335 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: 529.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  57 EGVENAVRILNTYKLTSREFHPGNTVVDVDGVKIGDGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKPRTSP 136
Cdd:COG2876     3 PGVEKVVRVSKPYKLASREFKPEDTVVDVGGVKIGGGELVVIAGPCAVESEEQILETAKAVKAAGAKILRGGAFKPRTSP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 137 YAFQGLEEEGLKYIRQAADEFGMKVITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINE 216
Cdd:COG2876    83 YSFQGLGEEGLKLLAEAREETGLPVVTEVMDPRDVELVAEYADILQIGARNMQNFELLKEVGRTGKPVLLKRGLSATIEE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 217 WLNAAEYIAVEDKSPVIFIERGIRTYETATRNTFDLSAVPLMKKLTHFPVIVDPSHGTGIWELVPPMARAGVASGADGMI 296
Cdd:COG2876   163 WLMAAEYILSEGNPNVILCERGIRTFETATRNTLDLSAVPVLKELTHLPVIVDPSHATGRRDLVPPMAKAAVAAGADGLM 242
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1533683560 297 VEIHPDPANAWSDGPQSLNEKTYSRMMKEVAIMKEAMEK 335
Cdd:COG2876   243 IEVHPDPEKALSDGPQSLTPEEFAELMEELRKLAEAVGR 281
DAHP_synth_Bsub TIGR01361
3-deoxy-7-phosphoheptulonate synthase; This model describes one of at least three types of ...
70-329 1.56e-162

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: 454.11  E-value: 1.56e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  70 KLTSREFHPGNTVVDVDGVKIGDGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKPRTSPYAFQGLEEEGLKY 149
Cdd:TIGR01361   1 KLVSRKFHPEKTVVDVGGVKIGEGSPIVIAGPCSVESEEQIMETARFVKEAGAKILRGGAFKPRTSPYSFQGLGEEGLKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 150 IRQAADEFGMKVITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDK 229
Cdd:TIGR01361  81 LRRAADEHGLPVVTEVMDPRDVEIVAEYADILQIGARNMQNFELLKEVGKQGKPVLLKRGMGNTIEEWLYAAEYILSSGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 230 SPVIFIERGIRTYETATRNTFDLSAVPLMKKLTHFPVIVDPSHGTGIWELVPPMARAGVASGADGMIVEIHPDPANAWSD 309
Cdd:TIGR01361 161 GNVILCERGIRTFEKATRNTLDLSAVPVLKKETHLPIIVDPSHAAGRRDLVIPLAKAAIAAGADGLMIEVHPDPEKALSD 240
                         250       260
                  ....*....|....*....|
gi 1533683560 310 GPQSLNEKTYSRMMKEVAIM 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 ...
80-314 2.20e-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: 261.10  E-value: 2.20e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  80 NTVVDVD-GVKIGDGS-FVTMAGPCSIEGLDQIRECARMAKAGGAK---ILRGGAF--KPRTSPYAFQGL-EEEGLKYIR 151
Cdd:pfam00793   1 DIPISLKqDIIIGKDDrLLVIAGPCSIEDPEAAMEYARRLKKLGAKlklIIIMRAYfeKPRTSPVGFKGLgNDPDLNILF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 152 QAADEFGMKVITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDKSP 231
Cdd:pfam00793  81 RIKDGLGLPIATEVLDPIDPQYLADVVDIGQIGARTTESQDLLELAGGLSKPVGFKNGTDAAIDEMLAAAEYHLFLGVTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 232 -VIFIERGIRTYETATRNTFDLSAVPLMKKLT-HFPVIVDPSHGTG-----IWELVPPMARAGVASGADGMIVEIHPDPA 304
Cdd:pfam00793 161 gNILCERGIRGGEGPNRNTLDVSAVAILKEETgHLPVMVDVSHANGrkdggRQPLVLPLAKAAIAVGIDGLMIEVHPNPG 240
                         250
                  ....*....|
gi 1533683560 305 NAWSDGPQSL 314
Cdd:pfam00793 241 NALSDGPQQL 250
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
142-193 6.42e-03

Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.


Pssm-ID: 238203  Cd Length: 217  Bit Score: 37.44  E-value: 6.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1533683560 142 LEEEGLKYIRQAADEFGMKVITEVMDEGHIDMVAEYS-DILQIGARNMQNFKL 193
Cdd:cd00331   105 LDDEQLKELYELARELGMEVLVEVHDEEELERALALGaKIIGINNRDLKTFEV 157
 
Name Accession Description Interval E-value
PRK08673 PRK08673
3-deoxy-7-phosphoheptulonate synthase; Reviewed
2-335 0e+00

3-deoxy-7-phosphoheptulonate synthase; Reviewed


Pssm-ID: 181535 [Multi-domain]  Cd Length: 335  Bit Score: 548.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560   2 IVIMKKEATEEQIKKVVDHIEKEGFKVSIDQGTERVVIGLKGDTRSLQEGAFTRYEGVENAVRILNTYKLTSREFHPGNT 81
Cdd:PRK08673    1 IIVMKPGATEEEIDEVIEEVESAGLKTHVSPGVERTVIGLIGDKGKVDAAKFEALPGVEEVVPVLKPYKLASREFKPEPT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  82 VVDVDGVKIGDGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKPRTSPYAFQGLEEEGLKYIRQAADEFGMKV 161
Cdd:PRK08673   81 VVKVGDVEIGGGKPVVIAGPCSVESEEQILEIARAVKEAGAQILRGGAFKPRTSPYSFQGLGEEGLKLLAEAREETGLPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 162 ITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDKSPVIFIERGIRT 241
Cdd:PRK08673  161 VTEVMDPRDVELVAEYVDILQIGARNMQNFDLLKEVGKTNKPVLLKRGMSATIEEWLMAAEYILAEGNPNVILCERGIRT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 242 YETATRNTFDLSAVPLMKKLTHFPVIVDPSHGTGIWELVPPMARAGVASGADGMIVEIHPDPANAWSDGPQSLNEKTYSR 321
Cdd:PRK08673  241 FETATRNTLDLSAVPVIKKLTHLPVIVDPSHATGKRDLVEPLALAAVAAGADGLIVEVHPDPEKALSDGPQSLTPEEFEE 320
                         330
                  ....*....|....
gi 1533683560 322 MMKEVAIMKEAMEK 335
Cdd:PRK08673  321 LMKKLRAIAEALGR 334
AroGA COG2876
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and ...
57-335 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: 529.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  57 EGVENAVRILNTYKLTSREFHPGNTVVDVDGVKIGDGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKPRTSP 136
Cdd:COG2876     3 PGVEKVVRVSKPYKLASREFKPEDTVVDVGGVKIGGGELVVIAGPCAVESEEQILETAKAVKAAGAKILRGGAFKPRTSP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 137 YAFQGLEEEGLKYIRQAADEFGMKVITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINE 216
Cdd:COG2876    83 YSFQGLGEEGLKLLAEAREETGLPVVTEVMDPRDVELVAEYADILQIGARNMQNFELLKEVGRTGKPVLLKRGLSATIEE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 217 WLNAAEYIAVEDKSPVIFIERGIRTYETATRNTFDLSAVPLMKKLTHFPVIVDPSHGTGIWELVPPMARAGVASGADGMI 296
Cdd:COG2876   163 WLMAAEYILSEGNPNVILCERGIRTFETATRNTLDLSAVPVLKELTHLPVIVDPSHATGRRDLVPPMAKAAVAAGADGLM 242
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1533683560 297 VEIHPDPANAWSDGPQSLNEKTYSRMMKEVAIMKEAMEK 335
Cdd:COG2876   243 IEVHPDPEKALSDGPQSLTPEEFAELMEELRKLAEAVGR 281
DAHP_synth_Bsub TIGR01361
3-deoxy-7-phosphoheptulonate synthase; This model describes one of at least three types of ...
70-329 1.56e-162

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: 454.11  E-value: 1.56e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  70 KLTSREFHPGNTVVDVDGVKIGDGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKPRTSPYAFQGLEEEGLKY 149
Cdd:TIGR01361   1 KLVSRKFHPEKTVVDVGGVKIGEGSPIVIAGPCSVESEEQIMETARFVKEAGAKILRGGAFKPRTSPYSFQGLGEEGLKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 150 IRQAADEFGMKVITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDK 229
Cdd:TIGR01361  81 LRRAADEHGLPVVTEVMDPRDVEIVAEYADILQIGARNMQNFELLKEVGKQGKPVLLKRGMGNTIEEWLYAAEYILSSGN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 230 SPVIFIERGIRTYETATRNTFDLSAVPLMKKLTHFPVIVDPSHGTGIWELVPPMARAGVASGADGMIVEIHPDPANAWSD 309
Cdd:TIGR01361 161 GNVILCERGIRTFEKATRNTLDLSAVPVLKKETHLPIIVDPSHAAGRRDLVIPLAKAAIAAGADGLMIEVHPDPEKALSD 240
                         250       260
                  ....*....|....*....|
gi 1533683560 310 GPQSLNEKTYSRMMKEVAIM 329
Cdd:TIGR01361 241 SKQQLTPEEFKRLVKELRAL 260
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
71-335 1.23e-131

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


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 379.71  E-value: 1.23e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  71 LTSREFHPGNTVVDVDGVKIGDGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKPRTSPYAFQGLEEEGLKYI 150
Cdd:PRK12595   95 LVSRKKKPEDTIVDVKGEVIGDGNQSFIFGPCSVESYEQVEAVAKALKAKGLKLLRGGAFKPRTSPYDFQGLGVEGLKIL 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 151 RQAADEFGMKVITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDKS 230
Cdd:PRK12595  175 KQVADEYGLAVISEIVNPADVEVALDYVDVIQIGARNMQNFELLKAAGRVNKPVLLKRGLSATIEEFIYAAEYIMSQGNG 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 231 PVIFIERGIRTYETATRNTFDLSAVPLMKKLTHFPVIVDPSHGTGIWELVPPMARAGVASGADGMIVEIHPDPANAWSDG 310
Cdd:PRK12595  255 QIILCERGIRTYEKATRNTLDISAVPILKQETHLPVMVDVTHSTGRRDLLLPTAKAALAIGADGVMAEVHPDPAVALSDS 334
                         250       260
                  ....*....|....*....|....*
gi 1533683560 311 PQSLNEKTYSRMMKEVAIMKEAMEK 335
Cdd:PRK12595  335 AQQMDIPEFDRFLDELKPLANKLNA 359
PRK13396 PRK13396
3-deoxy-7-phosphoheptulonate synthase; Provisional
1-335 3.46e-120

3-deoxy-7-phosphoheptulonate synthase; Provisional


Pssm-ID: 237376 [Multi-domain]  Cd Length: 352  Bit Score: 350.21  E-value: 3.46e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560   1 MIVIMKKEATEEQIKKVVDHIEKEGFKVSIDQGTERVVIGLKGDTRSLQEGAFTRYEG-VENAVRILNTYKLTSREFHPG 79
Cdd:PRK13396    1 MIIVMKVGTPEAEIERISQELTSWGLTPEKIVGKHKVVIGLVGDTAELDPLQIQELSPwIEQVLRVEKPFKRASREYRHG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  80 N---TVVDV-DG-VKIGDG-SFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKPRTSPYAFQGLEEEGLKYIRQA 153
Cdd:PRK13396   81 EaseVVVPTpNGpVPFGENhPVVVVAGPCSVENEEMIVETAKRVKAAGAKFLRGGAYKPRTSPYAFQGHGESALELLAAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 154 ADEFGMKVITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDKSPVI 233
Cdd:PRK13396  161 REATGLGIITEVMDAADLEKIAEVADVIQVGARNMQNFSLLKKVGAQDKPVLLKRGMAATIDEWLMAAEYILAAGNPNVI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 234 FIERGIRTYETA-TRNTFDLSAVPLMKKLTHFPVIVDPSHGTGIWELVPPMARAGVASGADGMIVEIHPDPANAWSDGPQ 312
Cdd:PRK13396  241 LCERGIRTFDRQyTRNTLDLSVIPVLRSLTHLPIMIDPSHGTGKSEYVPSMAMAAIAAGTDSLMIEVHPNPAKALSDGPQ 320
                         330       340
                  ....*....|....*....|...
gi 1533683560 313 SLNEKTYSRMMKEVAIMKEAMEK 335
Cdd:PRK13396  321 SLTPDRFDRLMQELAVIGKTVGR 343
DAHP_synth_1 pfam00793
DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino ...
80-314 2.20e-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: 261.10  E-value: 2.20e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  80 NTVVDVD-GVKIGDGS-FVTMAGPCSIEGLDQIRECARMAKAGGAK---ILRGGAF--KPRTSPYAFQGL-EEEGLKYIR 151
Cdd:pfam00793   1 DIPISLKqDIIIGKDDrLLVIAGPCSIEDPEAAMEYARRLKKLGAKlklIIIMRAYfeKPRTSPVGFKGLgNDPDLNILF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 152 QAADEFGMKVITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDKSP 231
Cdd:pfam00793  81 RIKDGLGLPIATEVLDPIDPQYLADVVDIGQIGARTTESQDLLELAGGLSKPVGFKNGTDAAIDEMLAAAEYHLFLGVTK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 232 -VIFIERGIRTYETATRNTFDLSAVPLMKKLT-HFPVIVDPSHGTG-----IWELVPPMARAGVASGADGMIVEIHPDPA 304
Cdd:pfam00793 161 gNILCERGIRGGEGPNRNTLDVSAVAILKEETgHLPVMVDVSHANGrkdggRQPLVLPLAKAAIAVGIDGLMIEVHPNPG 240
                         250
                  ....*....|
gi 1533683560 305 NAWSDGPQSL 314
Cdd:pfam00793 241 NALSDGPQQL 250
KdsA COG2877
3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase [Cell wall/membrane/envelope ...
85-314 8.05e-39

3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase [Cell wall/membrane/envelope biogenesis]; 3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 442124  Cd Length: 265  Bit Score: 138.24  E-value: 8.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  85 VDGVKIGDGS-FVTMAGPCSIEGLDQIRECA----RMAKAGGAKILrggaFKP------RTSPYAFQGL-EEEGLKYIRQ 152
Cdd:COG2877     1 IGGIEVGNDKpLFLIAGPCVIESEDLALEIAeklkEITDKLGIPYI----FKAsfdkanRSSIDSFRGPgLEEGLKILAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 153 AADEFGMKVITEVMDEGHIDMVAEYSDILQIGArnmqnF-----KLLSAVGKTGKPVGLKRGisgtinEWL------NAA 221
Cdd:COG2877    77 VKEEFGVPVLTDVHEPEQAAPVAEVVDVLQIPA-----FlcrqtDLLVAAAKTGKVVNVKKG------QFLapwdmkNVV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 222 EYIAVEDKSPVIFIERGirtyetatrNTF-------DLSAVPLMKKlTHFPVIVDPSH--------GT---GIWELVPPM 283
Cdd:COG2877   146 EKVREAGNDNILLTERG---------TSFgynnlvvDMRSLPIMRE-TGYPVVFDATHsvqlpggqGGssgGQREFVPVL 215
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1533683560 284 ARAGVASGADGMIVEIHPDPANAWSDGPQSL 314
Cdd:COG2877   216 ARAAVAVGVDGLFMETHPDPDKALSDGPNML 246
PRK05198 PRK05198
2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
87-314 1.15e-38

2-dehydro-3-deoxyphosphooctonate aldolase; Provisional


Pssm-ID: 235363  Cd Length: 264  Bit Score: 137.91  E-value: 1.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  87 GVKIG-DGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKP------RTSPYAFQGL-EEEGLKYIRQAADEFG 158
Cdd:PRK05198    2 DIEVGnDLPFFLIAGPCVIESRDLALRIAEHLKEITDKLGIPYVFKAsfdkanRSSIHSFRGPgLEEGLKILQEVKETFG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 159 MKVITEVMDEGHIDMVAEYSDILQIGArnmqnF-----KLLSAVGKTGKPVGLKRGisgtinEWL------NAAEYIAVE 227
Cdd:PRK05198   82 VPVLTDVHEPEQAAPVAEVVDVLQIPA-----FlcrqtDLLVAAAKTGKVVNIKKG------QFLapwdmkNVVDKVREA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 228 DKSPVIFIERGirtyetatrNTF-------DLSAVPLMKKlTHFPVIVDPSH--------GT---GIWELVPPMARAGVA 289
Cdd:PRK05198  151 GNDKIILCERG---------TSFgynnlvvDMRGLPIMRE-TGAPVIFDATHsvqlpggqGGssgGQREFVPVLARAAVA 220
                         250       260
                  ....*....|....*....|....*
gi 1533683560 290 SGADGMIVEIHPDPANAWSDGPQSL 314
Cdd:PRK05198  221 VGVAGLFIETHPDPDNALSDGPNML 245
DAHP_snth_FXD pfam18152
DAHP synthase ferredoxin-like domain; This domain is found in ...
1-66 1.68e-24

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: 94.47  E-value: 1.68e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533683560   1 MIVIMKKEATEEQIKKVVDHIEKEGFKVSIDQGTERVVIGLKGDTRSLQEGAFTRYEGVENAVRIL 66
Cdd:pfam18152   1 MIIVMKPGATEEEIDEVIERIESLGLKVHVSRGTERTVIGLIGDTSKLDAEQLEALPGVERVVRVS 66
PLN03033 PLN03033
2-dehydro-3-deoxyphosphooctonate aldolase; Provisional
95-311 1.90e-22

2-dehydro-3-deoxyphosphooctonate aldolase; Provisional


Pssm-ID: 178601  Cd Length: 290  Bit Score: 95.31  E-value: 1.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  95 FVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKP------RTSPYAFQGLE-EEGLKYIRQAADEFGMKVITEVMD 167
Cdd:PLN03033   17 FFLLAGPNVIESEEHILRMAKHIKDISTKLGLPLVFKSsfdkanRTSSKSFRGPGmAEGLKILEKVKVAYDLPIVTDVHE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 168 EGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRGISGTINEWLNAAEYIAVEDKSPVIFIERGirTYETATR 247
Cdd:PLN03033   97 SSQCEAVGKVADIIQIPAFLCRQTDLLVAAAKTGKIINIKKGQFCAPSVMRNSAEKVRLAGNPNVMVCERG--TMFGYND 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 248 NTFDLSAVPLMKKlTHFPVIVDPSHGT----------------GIWELVPPMARAGVASGADGMIVEIHPDPANAWSDGP 311
Cdd:PLN03033  175 LIVDPRNLEWMRE-ANCPVVADITHSLqqpagkkldgggvasgGLRELIPCIARTAVAVGVDGIFMEVHDDPLSAPVDGP 253
PRK12457 PRK12457
3-deoxy-8-phosphooctulonate synthase;
86-314 4.41e-18

3-deoxy-8-phosphooctulonate synthase;


Pssm-ID: 237105  Cd Length: 281  Bit Score: 82.87  E-value: 4.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560  86 DGVKIG-DGSFVTMAGPCSIEGLDQIRECARMAKAGGAKILRGGAFKP------RTSPYAFQGLE-EEGLKYIRQAADEF 157
Cdd:PRK12457    7 PGITVGnDLPFVLFGGINVLESLDFTLDVCGEYVEVTRKLGIPFVFKAsfdkanRSSIHSYRGVGlDEGLRIFEEVKARF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 158 GMKVITEVMDEGHIDMVAEYSDILQIGARNMQNFKLLSAVGKTGKPVGLKRgisgtiNEWLNAAEYIAVEDK------SP 231
Cdd:PRK12457   87 GVPVITDVHEVEQAAPVAEVADVLQVPAFLARQTDLVVAIAKTGKPVNIKK------PQFMSPTQMKHVVSKcreagnDR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 232 VIFIERGIR-TYETAtrnTFDLSAVPLMKKLT-HFPVIVDPSHGT-----------GIWELVPPMARAGVASGADGMIVE 298
Cdd:PRK12457  161 VILCERGSSfGYDNL---VVDMLGFRQMKRTTgDLPVIFDVTHSLqcrdplgaasgGRRRQVLDLARAGMAVGLAGLFLE 237
                         250
                  ....*....|....*.
gi 1533683560 299 IHPDPANAWSDGPQSL 314
Cdd:PRK12457  238 AHPDPDRARCDGPSAL 253
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
142-193 6.42e-03

Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.


Pssm-ID: 238203  Cd Length: 217  Bit Score: 37.44  E-value: 6.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1533683560 142 LEEEGLKYIRQAADEFGMKVITEVMDEGHIDMVAEYS-DILQIGARNMQNFKL 193
Cdd:cd00331   105 LDDEQLKELYELARELGMEVLVEVHDEEELERALALGaKIIGINNRDLKTFEV 157
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
105-182 6.48e-03

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 37.68  E-value: 6.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533683560 105 EGLDQIRECARMAKAGGAKILRGGAFKPRTSPYAFQGLEE---EGLKYIRQAADEFGMKVITEVMDEGHIDMVAEYSDIL 181
Cdd:COG1082    75 AALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEEAWDrlaERLRELAELAEEAGVTLALENHEGTFVNTPEEALRLL 154

                  .
gi 1533683560 182 Q 182
Cdd:COG1082   155 E 155
 
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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