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Conserved domains on  [gi|1550397553|gb|RVQ60689|]
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chorismate mutase family protein [Sinorhizobium meliloti]

Protein Classification

chorismate mutase; bifunctional chorismate mutase/prephenate dehydratase( domain architecture ID 10020004)

chorismate mutase catalyzes the interconversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis| bifunctional chorismate mutase/prephenate dehydratase catalyzes the formation of prephenate from chorismate and the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CM-like TIGR01803
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on ...
 11-92 1.49e-36

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: 118.46  E-value: 1.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553  11 MADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIA 90
Cdd:TIGR01803   1 LADIREAIDRIDLALVQALGRRMDYVKRASEFKRSHEAAIPAPERVAAVLPNAARWAEENGLDPPFVEGLFAQIIHWYIA 80


                  ..
gi 1550397553  91 HE 92
Cdd:TIGR01803  81 EE 82
 
Name Accession Description Interval E-value
CM-like TIGR01803
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on ...
 11-92 1.49e-36

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: 118.46  E-value: 1.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553  11 MADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIA 90
Cdd:TIGR01803   1 LADIREAIDRIDLALVQALGRRMDYVKRASEFKRSHEAAIPAPERVAAVLPNAARWAEENGLDPPFVEGLFAQIIHWYIA 80


                  ..
gi 1550397553  91 HE 92
Cdd:TIGR01803  81 EE 82
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 6-98 2.24e-21

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: 82.51  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553   6 AECTTMADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLV 85
Cdd:COG1605     2 SESESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREII 81

                          90
                  ....*....|...
gi 1550397553  86 ERAIAHERKLLGE 98
Cdd:COG1605    82 SESIALQEKLLAE 94
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 15-93 2.42e-17

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: 69.83  E-value: 2.42e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550397553  15 RVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIAHER 93
Cdd:pfam01817   1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 15-93 6.10e-17

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: 68.76  E-value: 6.10e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550397553   15 RVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIAHER 93
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
PRK07075 PRK07075
isochorismate lyase;
2-94 4.92e-16

isochorismate lyase;


Pssm-ID: 136191 [Multi-domain]  Cd Length: 101  Bit Score: 67.07  E-value: 4.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553   2 QKTPAECTTMADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPlnlKADIPA--RVAEVKENARRNAVELGLDPDFYER 79
Cdd:PRK07075    1 MKTPEACTGLDDIREAIDRLDRDIIAALGRRMQYVKAASRFKPS---EASIPApeRVAAMLPERRRWAEQAGLDADFVEK 77

                          90
                  ....*....|....*
gi 1550397553  80 FWGQLVERAIAHERK 94
Cdd:PRK07075   78 LFAQLIHWYIAQQIK 92
 
Name Accession Description Interval E-value
CM-like TIGR01803
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on ...
 11-92 1.49e-36

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: 118.46  E-value: 1.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553  11 MADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIA 90
Cdd:TIGR01803   1 LADIREAIDRIDLALVQALGRRMDYVKRASEFKRSHEAAIPAPERVAAVLPNAARWAEENGLDPPFVEGLFAQIIHWYIA 80


                  ..
gi 1550397553  91 HE 92
Cdd:TIGR01803  81 EE 82
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 6-98 2.24e-21

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: 82.51  E-value: 2.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553   6 AECTTMADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLV 85
Cdd:COG1605     2 SESESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREII 81

                          90
                  ....*....|...
gi 1550397553  86 ERAIAHERKLLGE 98
Cdd:COG1605    82 SESIALQEKLLAE 94
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 15-93 2.42e-17

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: 69.83  E-value: 2.42e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550397553  15 RVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIAHER 93
Cdd:pfam01817   1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 15-93 6.10e-17

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: 68.76  E-value: 6.10e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1550397553   15 RVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIAHER 93
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
PRK07075 PRK07075
isochorismate lyase;
2-94 4.92e-16

isochorismate lyase;


Pssm-ID: 136191 [Multi-domain]  Cd Length: 101  Bit Score: 67.07  E-value: 4.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553   2 QKTPAECTTMADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPlnlKADIPA--RVAEVKENARRNAVELGLDPDFYER 79
Cdd:PRK07075    1 MKTPEACTGLDDIREAIDRLDRDIIAALGRRMQYVKAASRFKPS---EASIPApeRVAAMLPERRRWAEQAGLDADFVEK 77

                          90
                  ....*....|....*
gi 1550397553  80 FWGQLVERAIAHERK 94
Cdd:PRK07075   78 LFAQLIHWYIAQQIK 92
PRK09239 PRK09239
chorismate mutase; Provisional
 11-94 1.30e-08

chorismate mutase; Provisional


Pssm-ID: 181719 [Multi-domain]  Cd Length: 104  Bit Score: 48.10  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553  11 MADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIA 90
Cdd:PRK09239   12 LAALRQSIDNIDAALIHMLAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQLAKDANLDPDFAEKFLNFIIKEVIR 91


                  ....
gi 1550397553  91 HERK 94
Cdd:PRK09239   92 HHER 95
CM_mono_cladeE TIGR01795
monofunctional chorismate mutase, alpha proteobacterial type; This model represents a small ...
 11-95 1.11e-06

monofunctional chorismate mutase, alpha proteobacterial type; This model represents a small clade of monofunctional (non-fused) chorismate mutases spanning alpha proteobacteria and two actinobacter gram positive species. The alpha proteobacterial members are trusted because the pathways of CM are evident and there is only one plausible CM in the genome. In S. coelicolor, however, there is another aparrent monofunctional CM. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130854  Cd Length: 94  Bit Score: 43.02  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553  11 MADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIA 90
Cdd:TIGR01795   5 LKALRQSIDNIDAAVIHMLAERFKCTSQVGVLKANAGLAPADPAREDYQIARLRRLAIDAGLDPEFAEKFLNFIVTEVIK 84


                  ....*
gi 1550397553  91 HERKL 95
Cdd:TIGR01795  85 HHERI 89
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 14-78 1.19e-05

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 42.17  E-value: 1.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1550397553  14 IRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYE 78
Cdd:PRK11199    8 LRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIE 72
PRK06285 PRK06285
chorismate mutase; Provisional
 9-76 2.31e-05

chorismate mutase; Provisional


Pssm-ID: 180509 [Multi-domain]  Cd Length: 96  Bit Score: 39.63  E-value: 2.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1550397553   9 TTMADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDF 76
Cdd:PRK06285    7 KRLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNIDENI 74
PRK06034 PRK06034
hypothetical protein; Provisional
 1-44 1.37e-04

hypothetical protein; Provisional


Pssm-ID: 235680 [Multi-domain]  Cd Length: 279  Bit Score: 38.92  E-value: 1.37e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1550397553   1 MQKTPAECTTMADIRVEIDRLDRALMTLFAERWGYIERAAEIKR 44
Cdd:PRK06034    1 GSTAPPAPPSLAELRWEIDAIDEELHQLLMERGDIIDRLIAVKR 44
CM_archaeal TIGR01791
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ...
 13-93 1.23e-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: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550397553  13 DIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVKENARRNAVELGLDPDFYERFWGQLVERAIAHE 92
Cdd:TIGR01791   3 ELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEIFEILMSLSKEEQ 82


                  .
gi 1550397553  93 R 93
Cdd:TIGR01791  83 R 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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