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Conserved domains on  [gi|446854841|ref|WP_000932097|]
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MULTISPECIES: chorismate mutase [Acinetobacter]

Protein Classification

chorismate mutase( domain architecture ID 10012993)

chorismate mutase catalyzes the interconversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08055 PRK08055
chorismate mutase; Provisional
 7-185 7.68e-99

chorismate mutase; Provisional


:

Pssm-ID: 236143  Cd Length: 181  Bit Score: 283.12  E-value: 7.68e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446854841   7 IQQTVKVATTVaaLMCFSSLAQAYQYEQ---TARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLN 83
Cdd:PRK08055   1 IRHITIFLCSL--LMCSSAFALAVTAVSlgaLATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446854841  84 SETVKPFIVVQMDVAKAIQYRYRADWLSSPETNWKPQDLSEVRLKISALNTELLKNIAYELKK-NNNKAPHGCSYMWPVQ 162
Cdd:PRK08055  79 PESIKPFIVAQMDAAKAIQYRYRADWLSQPEPSWPPQDLSDVRQRIRQLDTQILIQIAQRLKVcGPFSHGDMAWFRSTIN 158

                        170       180
                 ....*....|....*....|...
gi 446854841 163 HPQLKEADKRALCVTLNKIKLKQ 185
Cdd:PRK08055 159 QPNLSEADKSAIFAALSQVRLKR 181
 
Name Accession Description Interval E-value
PRK08055 PRK08055
chorismate mutase; Provisional
 7-185 7.68e-99

chorismate mutase; Provisional


Pssm-ID: 236143  Cd Length: 181  Bit Score: 283.12  E-value: 7.68e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446854841   7 IQQTVKVATTVaaLMCFSSLAQAYQYEQ---TARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLN 83
Cdd:PRK08055   1 IRHITIFLCSL--LMCSSAFALAVTAVSlgaLATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446854841  84 SETVKPFIVVQMDVAKAIQYRYRADWLSSPETNWKPQDLSEVRLKISALNTELLKNIAYELKK-NNNKAPHGCSYMWPVQ 162
Cdd:PRK08055  79 PESIKPFIVAQMDAAKAIQYRYRADWLSQPEPSWPPQDLSDVRQRIRQLDTQILIQIAQRLKVcGPFSHGDMAWFRSTIN 158

                        170       180
                 ....*....|....*....|...
gi 446854841 163 HPQLKEADKRALCVTLNKIKLKQ 185
Cdd:PRK08055 159 QPNLSEADKSAIFAALSQVRLKR 181
CM_mono2 TIGR01806
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ...
 28-140 7.51e-40

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: 131.40  E-value: 7.51e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446854841   28 QAYQYEQTARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETVKPFIVVQMDVAKAIQYRYRA 107
Cdd:TIGR01806   2 QSPQLGQLVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQINANKAIQYRLVS 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446854841  108 DWLSSPETNWKPQDLSEVRLKISALNTELLKNI 140
Cdd:TIGR01806  82 DWLNPPSPPPQVPDLTDTRSAIDQLNTEMLSAI 114
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 37-108 1.20e-14

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: 67.87  E-value: 1.20e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446854841  37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETVKPFIVVQMDVAKAIQYRYRAD 108
Cdd:COG1605   23 ELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISESIALQEKLLAE 94
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 37-103 1.73e-12

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: 59.90  E-value: 1.73e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446854841    37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETVKPFIVVQMDVAKAIQY 103
Cdd:smart00830  13 ALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 37-103 2.41e-11

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: 57.12  E-value: 2.41e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446854841   37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETVKPFIVVQMDVAKAIQY 103
Cdd:pfam01817  13 ELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
 
Name Accession Description Interval E-value
PRK08055 PRK08055
chorismate mutase; Provisional
 7-185 7.68e-99

chorismate mutase; Provisional


Pssm-ID: 236143  Cd Length: 181  Bit Score: 283.12  E-value: 7.68e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446854841   7 IQQTVKVATTVaaLMCFSSLAQAYQYEQ---TARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLN 83
Cdd:PRK08055   1 IRHITIFLCSL--LMCSSAFALAVTAVSlgaLATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446854841  84 SETVKPFIVVQMDVAKAIQYRYRADWLSSPETNWKPQDLSEVRLKISALNTELLKNIAYELKK-NNNKAPHGCSYMWPVQ 162
Cdd:PRK08055  79 PESIKPFIVAQMDAAKAIQYRYRADWLSQPEPSWPPQDLSDVRQRIRQLDTQILIQIAQRLKVcGPFSHGDMAWFRSTIN 158

                        170       180
                 ....*....|....*....|...
gi 446854841 163 HPQLKEADKRALCVTLNKIKLKQ 185
Cdd:PRK08055 159 QPNLSEADKSAIFAALSQVRLKR 181
CM_mono2 TIGR01806
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ...
 28-140 7.51e-40

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: 131.40  E-value: 7.51e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446854841   28 QAYQYEQTARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETVKPFIVVQMDVAKAIQYRYRA 107
Cdd:TIGR01806   2 QSPQLGQLVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQINANKAIQYRLVS 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446854841  108 DWLSSPETNWKPQDLSEVRLKISALNTELLKNI 140
Cdd:TIGR01806  82 DWLNPPSPPPQVPDLTDTRSAIDQLNTEMLSAI 114
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 37-108 1.20e-14

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: 67.87  E-value: 1.20e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446854841  37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETVKPFIVVQMDVAKAIQYRYRAD 108
Cdd:COG1605   23 ELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISESIALQEKLLAE 94
PRK09269 PRK09269
chorismate mutase; Provisional
 13-141 2.51e-14

chorismate mutase; Provisional


Pssm-ID: 236441  Cd Length: 193  Bit Score: 67.70  E-value: 2.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446854841  13 VATTVAALMCFSSLAQAYQyEQTA-----RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETV 87
Cdd:PRK09269  11 AAALLALLLLLGPPAAAAG-DDSAltplvDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAPAHGVDPDYV 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446854841  88 KPFIVVQMDVAKAIQYRYRADWL---SSPETnwKPQDLSEVRLKISALNTELLKNIA 141
Cdd:PRK09269  90 RRFFRDQIEANKLVQYALLARWRlagAAPPG--PRPDLASIRPRLDRLQQELLDALA 144
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 37-103 1.73e-12

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: 59.90  E-value: 1.73e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446854841    37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETVKPFIVVQMDVAKAIQY 103
Cdd:smart00830  13 ALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 37-103 2.41e-11

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: 57.12  E-value: 2.41e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446854841   37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETVKPFIVVQMDVAKAIQY 103
Cdd:pfam01817  13 ELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
CM_archaeal TIGR01791
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ...
 33-103 1.46e-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: 36.25  E-value: 1.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446854841   33 EQTARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLNSETVKPFIVVQMDVAKAIQY 103
Cdd:TIGR01791  13 KSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEIFEILMSLSKEEQR 83
 
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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