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Conserved domains on  [gi|506278990|ref|WP_015798765|]
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chorismate mutase [Acidimicrobium ferrooxidans]

Protein Classification

chorismate mutase( domain architecture ID 10790671)

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
AroH COG4401
Chorismate mutase AroH [Amino acid transport and metabolism]; Chorismate mutase AroH is part ...
 1-118 3.49e-61

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


:

Pssm-ID: 443526  Cd Length: 122  Bit Score: 183.05  E-value: 3.49e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506278990   1 MALRGLRGATTLDEDTPEAMRERVQELVSRMLAANGIGKEQLVSILFTATDDLHSLFPATAAREIGLGDVPLICARELDI 80
Cdd:COG4401    1 MMVRGIRGATTVEENTPEAILEATRELLEEILERNDLDPEDIVSVIFTVTPDLDAAFPAAAARELGWTDVPLLCAQEMDV 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 506278990  81 VGGTQRCVRVLMHLEDERPRSAFHHVYLHGAVGLRDDL 118
Cdd:COG4401   81 PGSLPRCIRVLIHVNTDKSQSEIKHVYLRGAKKLRPDL 118
 
Name Accession Description Interval E-value
AroH COG4401
Chorismate mutase AroH [Amino acid transport and metabolism]; Chorismate mutase AroH is part ...
 1-118 3.49e-61

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


Pssm-ID: 443526  Cd Length: 122  Bit Score: 183.05  E-value: 3.49e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506278990   1 MALRGLRGATTLDEDTPEAMRERVQELVSRMLAANGIGKEQLVSILFTATDDLHSLFPATAAREIGLGDVPLICARELDI 80
Cdd:COG4401    1 MMVRGIRGATTVEENTPEAILEATRELLEEILERNDLDPEDIVSVIFTVTPDLDAAFPAAAARELGWTDVPLLCAQEMDV 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 506278990  81 VGGTQRCVRVLMHLEDERPRSAFHHVYLHGAVGLRDDL 118
Cdd:COG4401   81 PGSLPRCIRVLIHVNTDKSQSEIKHVYLRGAKKLRPDL 118
CM_1 pfam07736
Chorismate mutase type I; Chorismate mutase (CM) EC:5.4.99.5 catalyzes the the conversion of ...
 4-118 3.71e-58

Chorismate mutase type I; Chorismate mutase (CM) EC:5.4.99.5 catalyzes the the conversion of chorismate to prephenate in the shikimate pathway of tyrosine and phenylalanine biosynthesis in bacteria, fungi and plants. The three types of CM are AroH class, AroQ class, prokaryotic type and AroQ class, eukaryotic type. Structurally CMs can be divided into two main groups: type I (AroH) class and type II (AroQ). Type I (AroH) CMs include CMs characterized by a trimeric pseudo alpha/beta barrel structure. The two types of the AroQ structural class (the Escherichia coli CM dimer and the yeast CM monomer) can be structurally superimposed, and the topology of the four-helix bundle forming the active site is conserved. CMs can be monofunctional or bifunctional (generally fused to another shikimate pathway member). Despite the structural differences, all CMs perform the same basic reaction. This entry represents chorismate mutases of the AroH class predominantly from Terrabacteria.


Pssm-ID: 429627  Cd Length: 115  Bit Score: 174.93  E-value: 3.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506278990    4 RGLRGATTLDEDTPEAMRERVQELVSRMLAANGIGKEQLVSILFTATDDLHSLFPATAAREIGLGDVPLICARELDIVGG 83
Cdd:pfam07736   1 RGIRGATTVEENTREAILEATRELLEEILERNGLDPEDIVSVIFTVTPDLDAAFPAAAARELGWDDVPLLCAQEMDVPGS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 506278990   84 TQRCVRVLMHLEDERPRSAFHHVYLHGAVGLRDDL 118
Cdd:pfam07736  81 LPRCIRVLIHVNTDKSQKEIKHVYLRGAKVLRPDL 115
AroH cd02185
Chorismate mutase (AroH) is one of at least five chorismate-utilizing enzymes present in ...
 3-118 2.99e-52

Chorismate mutase (AroH) is one of at least five chorismate-utilizing enzymes present in microorganisms that catalyze the rearrangement of chorismate to prephenic acid, the first committed step in the biosynthesis of aromatic amino acids. In prokaryotes, chorismate mutase may be fused to prephenate dehydratase, prephenate dehydrogenase, or 3-deoxy-D-arabino-heptulosonat-7-phosphate (DAHP) as part of a bifunctional enzyme. The AroH domain forms a homotrimer with three-fold symmetry.


Pssm-ID: 100026  Cd Length: 117  Bit Score: 160.40  E-value: 2.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506278990   3 LRGLRGATTLDEDTPEAMRERVQELVSRMLAANGIGKEQLVSILFTATDDLHSLFPATAAREIG-LGDVPLICARELDIV 81
Cdd:cd02185    1 VRGIRGATTVEENTAEEILEATRELLEEIIERNNIKPEDIISVIFTVTPDLDAAFPAKAARELGgWKYVPLMCAQEMDVP 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 506278990  82 GGTQRCVRVLMHLEDERPRSAFHHVYLHGAVGLRDDL 118
Cdd:cd02185   81 GSLPRCIRVLIHVNTDKAQQEIKHVYLGGAKKLRPDL 117
CM_mono_aroH TIGR01796
monofunctional chorismate mutase, gram positive type, clade 1; This model represents a family ...
 3-118 1.01e-39

monofunctional chorismate mutase, gram positive type, clade 1; This model represents a family of monofunctional (non-fused) chorismate mutases from gram positive bacteria (Firmicutes) and cyanobacteria. Trusted members of the family are found in operons with other enzymes of the chorismate pathways, both up- and downstream of CM (Listeria, Bacillus, Oceanobacillus) or are the sole CM in the genome where the other members of the chorismate pathways are found elsewhere in the genome (Nostoc, Thermosynechococcus). [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130855  Cd Length: 117  Bit Score: 128.77  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506278990    3 LRGLRGATTLDEDTPEAMRERVQELVSRMLAANGIGKEQLVSILFTATDDLHSLFPATAAREI-GLGDVPLICARELDIV 81
Cdd:TIGR01796   1 VRAVRGATTVERNEAEEIGEAVAELLTELMERNELTPEDLISVIFTVTEDLHADFPAAAARGLpGWTDVPVMCAQEIPVE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 506278990   82 GGTQRCVRVLMHLEDERPRSAFHHVYLHGAVGLRDDL 118
Cdd:TIGR01796  81 GSLPRCIRVLIHIESEKPRTGIHHVYLREAAKLRPDL 117
 
Name Accession Description Interval E-value
AroH COG4401
Chorismate mutase AroH [Amino acid transport and metabolism]; Chorismate mutase AroH is part ...
 1-118 3.49e-61

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


Pssm-ID: 443526  Cd Length: 122  Bit Score: 183.05  E-value: 3.49e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506278990   1 MALRGLRGATTLDEDTPEAMRERVQELVSRMLAANGIGKEQLVSILFTATDDLHSLFPATAAREIGLGDVPLICARELDI 80
Cdd:COG4401    1 MMVRGIRGATTVEENTPEAILEATRELLEEILERNDLDPEDIVSVIFTVTPDLDAAFPAAAARELGWTDVPLLCAQEMDV 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 506278990  81 VGGTQRCVRVLMHLEDERPRSAFHHVYLHGAVGLRDDL 118
Cdd:COG4401   81 PGSLPRCIRVLIHVNTDKSQSEIKHVYLRGAKKLRPDL 118
CM_1 pfam07736
Chorismate mutase type I; Chorismate mutase (CM) EC:5.4.99.5 catalyzes the the conversion of ...
 4-118 3.71e-58

Chorismate mutase type I; Chorismate mutase (CM) EC:5.4.99.5 catalyzes the the conversion of chorismate to prephenate in the shikimate pathway of tyrosine and phenylalanine biosynthesis in bacteria, fungi and plants. The three types of CM are AroH class, AroQ class, prokaryotic type and AroQ class, eukaryotic type. Structurally CMs can be divided into two main groups: type I (AroH) class and type II (AroQ). Type I (AroH) CMs include CMs characterized by a trimeric pseudo alpha/beta barrel structure. The two types of the AroQ structural class (the Escherichia coli CM dimer and the yeast CM monomer) can be structurally superimposed, and the topology of the four-helix bundle forming the active site is conserved. CMs can be monofunctional or bifunctional (generally fused to another shikimate pathway member). Despite the structural differences, all CMs perform the same basic reaction. This entry represents chorismate mutases of the AroH class predominantly from Terrabacteria.


Pssm-ID: 429627  Cd Length: 115  Bit Score: 174.93  E-value: 3.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506278990    4 RGLRGATTLDEDTPEAMRERVQELVSRMLAANGIGKEQLVSILFTATDDLHSLFPATAAREIGLGDVPLICARELDIVGG 83
Cdd:pfam07736   1 RGIRGATTVEENTREAILEATRELLEEILERNGLDPEDIVSVIFTVTPDLDAAFPAAAARELGWDDVPLLCAQEMDVPGS 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 506278990   84 TQRCVRVLMHLEDERPRSAFHHVYLHGAVGLRDDL 118
Cdd:pfam07736  81 LPRCIRVLIHVNTDKSQKEIKHVYLRGAKVLRPDL 115
AroH cd02185
Chorismate mutase (AroH) is one of at least five chorismate-utilizing enzymes present in ...
 3-118 2.99e-52

Chorismate mutase (AroH) is one of at least five chorismate-utilizing enzymes present in microorganisms that catalyze the rearrangement of chorismate to prephenic acid, the first committed step in the biosynthesis of aromatic amino acids. In prokaryotes, chorismate mutase may be fused to prephenate dehydratase, prephenate dehydrogenase, or 3-deoxy-D-arabino-heptulosonat-7-phosphate (DAHP) as part of a bifunctional enzyme. The AroH domain forms a homotrimer with three-fold symmetry.


Pssm-ID: 100026  Cd Length: 117  Bit Score: 160.40  E-value: 2.99e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506278990   3 LRGLRGATTLDEDTPEAMRERVQELVSRMLAANGIGKEQLVSILFTATDDLHSLFPATAAREIG-LGDVPLICARELDIV 81
Cdd:cd02185    1 VRGIRGATTVEENTAEEILEATRELLEEIIERNNIKPEDIISVIFTVTPDLDAAFPAKAARELGgWKYVPLMCAQEMDVP 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 506278990  82 GGTQRCVRVLMHLEDERPRSAFHHVYLHGAVGLRDDL 118
Cdd:cd02185   81 GSLPRCIRVLIHVNTDKAQQEIKHVYLGGAKKLRPDL 117
CM_mono_aroH TIGR01796
monofunctional chorismate mutase, gram positive type, clade 1; This model represents a family ...
 3-118 1.01e-39

monofunctional chorismate mutase, gram positive type, clade 1; This model represents a family of monofunctional (non-fused) chorismate mutases from gram positive bacteria (Firmicutes) and cyanobacteria. Trusted members of the family are found in operons with other enzymes of the chorismate pathways, both up- and downstream of CM (Listeria, Bacillus, Oceanobacillus) or are the sole CM in the genome where the other members of the chorismate pathways are found elsewhere in the genome (Nostoc, Thermosynechococcus). [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130855  Cd Length: 117  Bit Score: 128.77  E-value: 1.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506278990    3 LRGLRGATTLDEDTPEAMRERVQELVSRMLAANGIGKEQLVSILFTATDDLHSLFPATAAREI-GLGDVPLICARELDIV 81
Cdd:TIGR01796   1 VRAVRGATTVERNEAEEIGEAVAELLTELMERNELTPEDLISVIFTVTEDLHADFPAAAARGLpGWTDVPVMCAQEIPVE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 506278990   82 GGTQRCVRVLMHLEDERPRSAFHHVYLHGAVGLRDDL 118
Cdd:TIGR01796  81 GSLPRCIRVLIHIESEKPRTGIHHVYLREAAKLRPDL 117
 
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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