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Conserved domains on  [gi|491111895|ref|WP_004970358|]
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MULTISPECIES: chorismate mutase [Acinetobacter]

Protein Classification

chorismate mutase( domain architecture ID 10004036)

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
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 4-94 2.59e-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: 66.71  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111895   4 EKVNSLQQARDKIDQIDVALIELIASRQFYVDQAMRHKQ----TVEDvqsPQRVKEVIEKVRTLAVQHAVDPDMVERLYH 79
Cdd:COG1605    2 SESESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKehglPIYD---PEREAEVLERLRELAEELGLDPEFVEAIFR 78

                         90
                 ....*....|....*
gi 491111895  80 DMIQHFIQRELKEFR 94
Cdd:COG1605   79 EIISESIALQEKLLA 93
 
Name Accession Description Interval E-value
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 4-94 2.59e-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: 66.71  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111895   4 EKVNSLQQARDKIDQIDVALIELIASRQFYVDQAMRHKQ----TVEDvqsPQRVKEVIEKVRTLAVQHAVDPDMVERLYH 79
Cdd:COG1605    2 SESESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKehglPIYD---PEREAEVLERLRELAEELGLDPEFVEAIFR 78

                         90
                 ....*....|....*
gi 491111895  80 DMIQHFIQRELKEFR 94
Cdd:COG1605   79 EIISESIALQEKLLA 93
PRK07075 PRK07075
isochorismate lyase;
4-94 1.22e-14

isochorismate lyase;


Pssm-ID: 136191 [Multi-domain]  Cd Length: 101  Bit Score: 63.21  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111895   4 EKVNSLQQARDKIDQIDVALIELIASRQFYVDQAMRHKQTVEDVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYHDMIQ 83
Cdd:PRK07075   5 EACTGLDDIREAIDRLDRDIIAALGRRMQYVKAASRFKPSEASIPAPERVAAMLPERRRWAEQAGLDADFVEKLFAQLIH 84

                         90
                 ....*....|.
gi 491111895  84 HFIQRELKEFR 94
Cdd:PRK07075  85 WYIAQQIKHWR 95
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 13-89 2.13e-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: 62.13  E-value: 2.13e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491111895  13 RDKIDQIDVALIELIASRQFYVDQAMRHKQTVE-DVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYHDMIQHFIQRE 89
Cdd:pfam01817  1 RAEIDEIDREILELLAERMELAREIGEYKKENGlPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQ 78
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 13-89 4.68e-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: 56.05  E-value: 4.68e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491111895   13 RDKIDQIDVALIELIASRQFYVDQAMRHKQ-TVEDVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYHDMIQHFIQRE 89
Cdd:smart00830  1 RAEIDAIDDQILALLAERAALAREVARLKAkNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQ 78
CM-like TIGR01803
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on ...
 13-89 3.23e-10

chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on the mechanism of chorismate mutase and are likely to have evolved from an ancestral chorismate mutase enzyme. 4-amino-4-deoxy-chorismate mutase produces amino-deoxy-prephenate which is subsequently converted to para-dimethylamino-phenylalanine, a component of the natural product pristinamycin. Isochorismate-pyruvate lyase presumably catalyzes the same type of 2+2+2 cyclo-rearrangement as chorismate mutase, but acting on isochorismate, this results in two broken bonds instead of one broken and one made. The product of this reaction is salicylate (2-hydroxy-benzoate) which is also incorporated into various natural products.


Pssm-ID: 130862 [Multi-domain]  Cd Length: 82  Bit Score: 51.44  E-value: 3.23e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491111895  13 RDKIDQIDVALIELIASRQFYVDQAMRHKQTVE-DVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYHDMIQHFIQRE 89
Cdd:TIGR01803  5 REAIDRIDLALVQALGRRMDYVKRASEFKRSHEaAIPAPERVAAVLPNAARWAEENGLDPPFVEGLFAQIIHWYIAEE 82
 
Name Accession Description Interval E-value
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 4-94 2.59e-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: 66.71  E-value: 2.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111895   4 EKVNSLQQARDKIDQIDVALIELIASRQFYVDQAMRHKQ----TVEDvqsPQRVKEVIEKVRTLAVQHAVDPDMVERLYH 79
Cdd:COG1605    2 SESESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKehglPIYD---PEREAEVLERLRELAEELGLDPEFVEAIFR 78

                         90
                 ....*....|....*
gi 491111895  80 DMIQHFIQRELKEFR 94
Cdd:COG1605   79 EIISESIALQEKLLA 93
PRK07075 PRK07075
isochorismate lyase;
4-94 1.22e-14

isochorismate lyase;


Pssm-ID: 136191 [Multi-domain]  Cd Length: 101  Bit Score: 63.21  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111895   4 EKVNSLQQARDKIDQIDVALIELIASRQFYVDQAMRHKQTVEDVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYHDMIQ 83
Cdd:PRK07075   5 EACTGLDDIREAIDRLDRDIIAALGRRMQYVKAASRFKPSEASIPAPERVAAMLPERRRWAEQAGLDADFVEKLFAQLIH 84

                         90
                 ....*....|.
gi 491111895  84 HFIQRELKEFR 94
Cdd:PRK07075  85 WYIAQQIKHWR 95
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 13-89 2.13e-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: 62.13  E-value: 2.13e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491111895  13 RDKIDQIDVALIELIASRQFYVDQAMRHKQTVE-DVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYHDMIQHFIQRE 89
Cdd:pfam01817  1 RAEIDEIDREILELLAERMELAREIGEYKKENGlPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQ 78
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 13-89 4.68e-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: 56.05  E-value: 4.68e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491111895   13 RDKIDQIDVALIELIASRQFYVDQAMRHKQ-TVEDVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYHDMIQHFIQRE 89
Cdd:smart00830  1 RAEIDAIDDQILALLAERAALAREVARLKAkNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQ 78
CM-like TIGR01803
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on ...
 13-89 3.23e-10

chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on the mechanism of chorismate mutase and are likely to have evolved from an ancestral chorismate mutase enzyme. 4-amino-4-deoxy-chorismate mutase produces amino-deoxy-prephenate which is subsequently converted to para-dimethylamino-phenylalanine, a component of the natural product pristinamycin. Isochorismate-pyruvate lyase presumably catalyzes the same type of 2+2+2 cyclo-rearrangement as chorismate mutase, but acting on isochorismate, this results in two broken bonds instead of one broken and one made. The product of this reaction is salicylate (2-hydroxy-benzoate) which is also incorporated into various natural products.


Pssm-ID: 130862 [Multi-domain]  Cd Length: 82  Bit Score: 51.44  E-value: 3.23e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491111895  13 RDKIDQIDVALIELIASRQFYVDQAMRHKQTVE-DVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYHDMIQHFIQRE 89
Cdd:TIGR01803  5 REAIDRIDLALVQALGRRMDYVKRASEFKRSHEaAIPAPERVAAVLPNAARWAEENGLDPPFVEGLFAQIIHWYIAEE 82
PRK06285 PRK06285
chorismate mutase; Provisional
 1-84 1.08e-07

chorismate mutase; Provisional


Pssm-ID: 180509 [Multi-domain]  Cd Length: 96  Bit Score: 45.41  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111895  1 MNNEKVNSLQQARDKIDQIDVALIELIASR-QFYVDQAMRHKQTVEDVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYH 79
Cdd:PRK06285  1 DSESAEKRLNEIRKRIDEIDEQIIDLIAERtSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNIDENIGLKIMK 80


                ....*
gi 491111895 80 DMIQH 84
Cdd:PRK06285 81 ILMEH 85
PRK09239 PRK09239
chorismate mutase; Provisional
 1-88 2.18e-05

chorismate mutase; Provisional


Pssm-ID: 181719 [Multi-domain]  Cd Length: 104  Bit Score: 39.62  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491111895   1 MNNEKVNSLQQARDKIDQIDVALIELIASRqFYVDQAM-----RHKQTVEDvqsPQRVKEVIEKVRTLAVQHAVDPDMVE 75
Cdd:PRK09239   4 EQARAPAELAALRQSIDNIDAALIHMLAER-FKCTQAVgvlkaEHGLPPAD---PAREAYQIERLRQLAKDANLDPDFAE 79

                         90
                 ....*....|...
gi 491111895  76 RLYHDMIQHFIQR 88
Cdd:PRK09239  80 KFLNFIIKEVIRH 92
PRK09269 PRK09269
chorismate mutase; Provisional
 21-82 2.42e-05

chorismate mutase; Provisional


Pssm-ID: 236441  Cd Length: 193  Bit Score: 40.74  E-value: 2.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491111895  21 VALIELIASRQFYVDQAMRHK-QTVEDVQSPQRVKEVIEKVRTLAVQHAVDPDMVERLYHDMI 82
Cdd:PRK09269  35 TPLVDLAAQRLALADPVALSKwDSGKPIEDPPREAQVLANVEAQAPAHGVDPDYVRRFFRDQI 97
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 6-75 7.97e-05

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 39.48  E-value: 7.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491111895   6 VNSLQQARDKIDQIDVALIELIASRQFYVDQ--AMRHKQTVEdVQSPQRVKEVIEKVRTLAVQHAVDPDMVE 75
Cdd:PRK11199   2 VAELTALRDQIDEVDKQLLELLAKRLELVAQvgEVKSRHGLP-IYVPEREAAMLASRRAEAEALGVPPDLIE 72
 
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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