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Conserved domains on  [gi|15609022|ref|NP_216401|]
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chorismate mutase [Mycobacterium tuberculosis H37Rv]

Protein Classification

chorismate mutase( domain architecture ID 10793183)

chorismate mutase catalyzes the interconversion of chorismate to prephenate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09269 PRK09269
chorismate mutase; Provisional
 6-198 4.95e-73

chorismate mutase; Provisional


:

Pssm-ID: 236441  Cd Length: 193  Bit Score: 219.09  E-value: 4.95e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022    6 REIYLATAVSIGILLSLIAPLGPPLARADGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDAR 85
Cdd:PRK09269   1 MKQLLRASLAAAALLALLLLLGPPAAAAGDDSALTPLVDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022   86 SQHIDPDYVTRVFDDQIRATEAIEYSRFSDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLD 165
Cdd:PRK09269  81 AHGVDPDYVRRFFRDQIEANKLVQYALLARWRLAGAAPPGPRPDLASIRPRLDRLQQELLDALADVAPLRSAPDCPARLA 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15609022  166 RAKRDIVRSRHLDSLYQRALTTATQSYCQALPP 198
Cdd:PRK09269 161 RAVANVARLRRLDSLHRQALDRATGDYCHAGGA 193
 
Name Accession Description Interval E-value
PRK09269 PRK09269
chorismate mutase; Provisional
 6-198 4.95e-73

chorismate mutase; Provisional


Pssm-ID: 236441  Cd Length: 193  Bit Score: 219.09  E-value: 4.95e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022    6 REIYLATAVSIGILLSLIAPLGPPLARADGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDAR 85
Cdd:PRK09269   1 MKQLLRASLAAAALLALLLLLGPPAAAAGDDSALTPLVDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022   86 SQHIDPDYVTRVFDDQIRATEAIEYSRFSDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLD 165
Cdd:PRK09269  81 AHGVDPDYVRRFFRDQIEANKLVQYALLARWRLAGAAPPGPRPDLASIRPRLDRLQQELLDALADVAPLRSAPDCPARLA 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15609022  166 RAKRDIVRSRHLDSLYQRALTTATQSYCQALPP 198
Cdd:PRK09269 161 RAVANVARLRRLDSLHRQALDRATGDYCHAGGA 193
CM_mono2 TIGR01806
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ...
 34-148 4.39e-48

chorismate mutase, putative; This model represents a clade of probable chorismate mutases from alpha, beta and gamma proteobacteria as well as Mycobacterium tuberculosis and a clade of nematodes. Although the most likely function for the enzymes represented by this model is as a chorismate mutase, in no species are these enzymes the sole chorismate mutase in the genome. Also, in no case are these enzymes located in a region of the genome proximal to any other enzymes involved in chorismate pathways. Although the Pantoea enzyme has been shown to complement a CM-free mutant of E. coli, this was also shown to be the case with isochorismate-pyruvate lyase which only has a secondary (non-physiologically relevant) chorismate mutase activity. This enzyme is believed to be a homodimer and be localized to the periplasm. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130865  Cd Length: 114  Bit Score: 152.97  E-value: 4.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022    34 DGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSRF 113
Cdd:TIGR01806   1 DQSPQLGQLVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQINANKAIQYRLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15609022   114 SDWkLNPASAPPEPPDLSASRSAIDSLNNRMLSQI 148
Cdd:TIGR01806  81 SDW-LNPPSPPPQVPDLTDTRSAIDQLNTEMLSAI 114
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 40-110 1.51e-15

Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine..


Pssm-ID: 214841 [Multi-domain]  Cd Length: 79  Bit Score: 68.37  E-value: 1.51e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15609022     40 AELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEY 110
Cdd:smart00830   9 DQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 40-110 7.24e-14

Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine.


Pssm-ID: 460345 [Multi-domain]  Cd Length: 79  Bit Score: 64.05  E-value: 7.24e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15609022    40 AELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEY 110
Cdd:pfam01817   9 REILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 40-110 4.04e-13

Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 441213 [Multi-domain]  Cd Length: 166  Bit Score: 64.40  E-value: 4.04e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15609022  40 AELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEY 110
Cdd:COG1605  19 RQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISESIALQE 89
 
Name Accession Description Interval E-value
PRK09269 PRK09269
chorismate mutase; Provisional
 6-198 4.95e-73

chorismate mutase; Provisional


Pssm-ID: 236441  Cd Length: 193  Bit Score: 219.09  E-value: 4.95e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022    6 REIYLATAVSIGILLSLIAPLGPPLARADGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDAR 85
Cdd:PRK09269   1 MKQLLRASLAAAALLALLLLLGPPAAAAGDDSALTPLVDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022   86 SQHIDPDYVTRVFDDQIRATEAIEYSRFSDWKLNPASAPPEPPDLSASRSAIDSLNNRMLSQIWSHWSLLSAPSCAAQLD 165
Cdd:PRK09269  81 AHGVDPDYVRRFFRDQIEANKLVQYALLARWRLAGAAPPGPRPDLASIRPRLDRLQQELLDALADVAPLRSAPDCPARLA 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 15609022  166 RAKRDIVRSRHLDSLYQRALTTATQSYCQALPP 198
Cdd:PRK09269 161 RAVANVARLRRLDSLHRQALDRATGDYCHAGGA 193
CM_mono2 TIGR01806
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ...
 34-148 4.39e-48

chorismate mutase, putative; This model represents a clade of probable chorismate mutases from alpha, beta and gamma proteobacteria as well as Mycobacterium tuberculosis and a clade of nematodes. Although the most likely function for the enzymes represented by this model is as a chorismate mutase, in no species are these enzymes the sole chorismate mutase in the genome. Also, in no case are these enzymes located in a region of the genome proximal to any other enzymes involved in chorismate pathways. Although the Pantoea enzyme has been shown to complement a CM-free mutant of E. coli, this was also shown to be the case with isochorismate-pyruvate lyase which only has a secondary (non-physiologically relevant) chorismate mutase activity. This enzyme is believed to be a homodimer and be localized to the periplasm. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130865  Cd Length: 114  Bit Score: 152.97  E-value: 4.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022    34 DGTSQLAELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSRF 113
Cdd:TIGR01806   1 DQSPQLGQLVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQINANKAIQYRLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15609022   114 SDWkLNPASAPPEPPDLSASRSAIDSLNNRMLSQI 148
Cdd:TIGR01806  81 SDW-LNPPSPPPQVPDLTDTRSAIDQLNTEMLSAI 114
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 40-110 1.51e-15

Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine..


Pssm-ID: 214841 [Multi-domain]  Cd Length: 79  Bit Score: 68.37  E-value: 1.51e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15609022     40 AELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEY 110
Cdd:smart00830   9 DQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
PRK08055 PRK08055
chorismate mutase; Provisional
 33-148 3.70e-15

chorismate mutase; Provisional


Pssm-ID: 236143  Cd Length: 181  Bit Score: 70.11  E-value: 3.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022   33 ADGTSQLAELVDaaaERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEYSR 112
Cdd:PRK08055  24 AVSLGALATLIN---ERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLDPESIKPFIVAQMDAAKAIQYRY 100

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15609022  113 FSDWKLNPASAPPePPDLSASRSAIDSLNNRMLSQI 148
Cdd:PRK08055 101 RADWLSQPEPSWP-PQDLSDVRQRIRQLDTQILIQI 135
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 40-110 7.24e-14

Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine.


Pssm-ID: 460345 [Multi-domain]  Cd Length: 79  Bit Score: 64.05  E-value: 7.24e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15609022    40 AELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEY 110
Cdd:pfam01817   9 REILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 40-110 4.04e-13

Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 441213 [Multi-domain]  Cd Length: 166  Bit Score: 64.40  E-value: 4.04e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15609022  40 AELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIRATEAIEY 110
Cdd:COG1605  19 RQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISESIALQE 89
PRK09239 PRK09239
chorismate mutase; Provisional
 33-108 1.31e-04

chorismate mutase; Provisional


Pssm-ID: 181719 [Multi-domain]  Cd Length: 104  Bit Score: 39.62  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15609022   33 ADGTSQLAEL------VDAA-----AERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTR----V 97
Cdd:PRK09239   6 ARAPAELAALrqsidnIDAAlihmlAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQLAKDANLDPDFAEKflnfI 85

                         90
                 ....*....|.
gi 15609022   98 FDDQIRATEAI 108
Cdd:PRK09239  86 IKEVIRHHERI 96
pheA PRK10622
bifunctional chorismate mutase/prephenate dehydratase; Provisional
 28-98 7.74e-04

bifunctional chorismate mutase/prephenate dehydratase; Provisional


Pssm-ID: 182594 [Multi-domain]  Cd Length: 386  Bit Score: 39.33  E-value: 7.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15609022   28 PPLARADGTSQL-AELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVF 98
Cdd:PRK10622   6 PLLALREKISALdEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLF 77
CM_archaeal TIGR01791
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ...
 41-103 5.06e-03

chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. Chorismate mutase catalyzes the conversion of chorismate into prephenate which is subsequently converted into either phenylalanine or tyrosine. In Sulfolobus this gene is found as a fusion with prephenate dehydrogenase (although the non-TIGR annotation contains a typographical error indicating it as a dehydratase OMNI|NTL02SS0274) which is the next enzyme in the tyrosine biosynthesis pathway. The Archaeoglobus gene contains an N-terminal prephenate dehydrogenase domain and a C-terminal prephenate dehydratase domain followed by a regulatory amino acid-binding ACT domain. The Thermoplasma volcanium gene is adjacent to prephenate dehydratase. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130851 [Multi-domain]  Cd Length: 83  Bit Score: 34.71  E-value: 5.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15609022    41 ELVDAAAERLEVADPVAAFKWRAQLPIEDSGRVEQQLAKLGEDARSQHIDPDYVTRVFDDQIR 103
Cdd:TIGR01791  14 SILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEIFEILMS 76
 
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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