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Conserved domains on  [gi|490929776|ref|WP_004791629|]
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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
 8-185 4.94e-96

chorismate mutase; Provisional


:

Pssm-ID: 236143  Cd Length: 181  Bit Score: 276.19  E-value: 4.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929776   8 QSAVKVVCTLatFMCVSSLAQAYQYDQ---TARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSS 84
Cdd:PRK08055   2 RHITIFLCSL--LMCSSAFALAVTAVSlgaLATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929776  85 ETVKPFIVTQMNVAKAIQYRYRADWLSSPETNWKPQDLAEVRLKISTLNTELLKNIAYELKK-NNNKAPHSCSYMWSVQH 163
Cdd:PRK08055  80 ESIKPFIVAQMDAAKAIQYRYRADWLSQPEPSWPPQDLSDVRQRIRQLDTQILIQIAQRLKVcGPFSHGDMAWFRSTINQ 159

                        170       180
                 ....*....|....*....|..
gi 490929776 164 PQLKEADKKVLCMTLNKIKLKQ 185
Cdd:PRK08055 160 PNLSEADKSAIFAALSQVRLKR 181
 
Name Accession Description Interval E-value
PRK08055 PRK08055
chorismate mutase; Provisional
 8-185 4.94e-96

chorismate mutase; Provisional


Pssm-ID: 236143  Cd Length: 181  Bit Score: 276.19  E-value: 4.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929776   8 QSAVKVVCTLatFMCVSSLAQAYQYDQ---TARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSS 84
Cdd:PRK08055   2 RHITIFLCSL--LMCSSAFALAVTAVSlgaLATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929776  85 ETVKPFIVTQMNVAKAIQYRYRADWLSSPETNWKPQDLAEVRLKISTLNTELLKNIAYELKK-NNNKAPHSCSYMWSVQH 163
Cdd:PRK08055  80 ESIKPFIVAQMDAAKAIQYRYRADWLSQPEPSWPPQDLSDVRQRIRQLDTQILIQIAQRLKVcGPFSHGDMAWFRSTINQ 159

                        170       180
                 ....*....|....*....|..
gi 490929776 164 PQLKEADKKVLCMTLNKIKLKQ 185
Cdd:PRK08055 160 PNLSEADKSAIFAALSQVRLKR 181
CM_mono2 TIGR01806
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ...
 28-140 8.14e-41

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: 133.71  E-value: 8.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929776   28 QAYQYDQTARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSSETVKPFIVTQMNVAKAIQYRYRA 107
Cdd:TIGR01806   2 QSPQLGQLVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQINANKAIQYRLVS 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 490929776  108 DWLSSPETNWKPQDLAEVRLKISTLNTELLKNI 140
Cdd:TIGR01806  82 DWLNPPSPPPQVPDLTDTRSAIDQLNTEMLSAI 114
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 37-108 2.80e-15

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: 69.79  E-value: 2.80e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490929776  37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSSETVKPFIVTQMNVAKAIQYRYRAD 108
Cdd:COG1605   23 ELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISESIALQEKLLAE 94
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 37-103 2.86e-13

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: 61.83  E-value: 2.86e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490929776    37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSSETVKPFIVTQMNVAKAIQY 103
Cdd:smart00830  13 ALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 33-103 1.07e-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: 57.89  E-value: 1.07e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490929776   33 DQTARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSSETVKPFIVTQMNVAKAIQY 103
Cdd:pfam01817   9 REILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
 
Name Accession Description Interval E-value
PRK08055 PRK08055
chorismate mutase; Provisional
 8-185 4.94e-96

chorismate mutase; Provisional


Pssm-ID: 236143  Cd Length: 181  Bit Score: 276.19  E-value: 4.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929776   8 QSAVKVVCTLatFMCVSSLAQAYQYDQ---TARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSS 84
Cdd:PRK08055   2 RHITIFLCSL--LMCSSAFALAVTAVSlgaLATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929776  85 ETVKPFIVTQMNVAKAIQYRYRADWLSSPETNWKPQDLAEVRLKISTLNTELLKNIAYELKK-NNNKAPHSCSYMWSVQH 163
Cdd:PRK08055  80 ESIKPFIVAQMDAAKAIQYRYRADWLSQPEPSWPPQDLSDVRQRIRQLDTQILIQIAQRLKVcGPFSHGDMAWFRSTINQ 159

                        170       180
                 ....*....|....*....|..
gi 490929776 164 PQLKEADKKVLCMTLNKIKLKQ 185
Cdd:PRK08055 160 PNLSEADKSAIFAALSQVRLKR 181
CM_mono2 TIGR01806
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ...
 28-140 8.14e-41

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: 133.71  E-value: 8.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929776   28 QAYQYDQTARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSSETVKPFIVTQMNVAKAIQYRYRA 107
Cdd:TIGR01806   2 QSPQLGQLVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQINANKAIQYRLVS 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 490929776  108 DWLSSPETNWKPQDLAEVRLKISTLNTELLKNI 140
Cdd:TIGR01806  82 DWLNPPSPPPQVPDLTDTRSAIDQLNTEMLSAI 114
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 37-108 2.80e-15

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: 69.79  E-value: 2.80e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490929776  37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSSETVKPFIVTQMNVAKAIQYRYRAD 108
Cdd:COG1605   23 ELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISESIALQEKLLAE 94
PRK09269 PRK09269
chorismate mutase; Provisional
 15-141 3.57e-14

chorismate mutase; Provisional


Pssm-ID: 236441  Cd Length: 193  Bit Score: 67.32  E-value: 3.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490929776  15 CTLATFMCVSSLAQAYQyDQTA-----RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSSETVKP 89
Cdd:PRK09269  13 ALLALLLLLGPPAAAAG-DDSAltplvDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAPAHGVDPDYVRR 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490929776  90 FIVTQMNVAKAIQYRYRADWL---SSPETnwKPQDLAEVRLKISTLNTELLKNIA 141
Cdd:PRK09269  92 FFRDQIEANKLVQYALLARWRlagAAPPG--PRPDLASIRPRLDRLQQELLDALA 144
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 37-103 2.86e-13

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: 61.83  E-value: 2.86e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490929776    37 RLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSSETVKPFIVTQMNVAKAIQY 103
Cdd:smart00830  13 ALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 33-103 1.07e-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: 57.89  E-value: 1.07e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490929776   33 DQTARLINERLSYMKDVAGYKAEQHLPIEDLTQEKKVLDQSLSEADSFGLSSETVKPFIVTQMNVAKAIQY 103
Cdd:pfam01817   9 REILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
 
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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