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Conserved domains on  [gi|15608088|ref|NP_215463|]
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chorismate mutase [Mycobacterium tuberculosis H37Rv]

Protein Classification

chorismate mutase( domain architecture ID 10012972)

chorismate mutase catalyzes the interconversion of chorismate to prephenate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK07857 PRK07857
chorismate mutase;
1-93 3.08e-39

chorismate mutase;


:

Pssm-ID: 236117  Cd Length: 106  Bit Score: 126.34  E-value: 3.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608088    1 MRPEPPHHENAELAA-MNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIE 79
Cdd:PRK07857   1 MRPEPPHHENAELEArMPTGTDDPLSDAEIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIE 80

                         90
                 ....*....|....*
gi 15608088   80 RYSE-LGPDGKDLAI 93
Cdd:PRK07857  81 RYREeLGPEGKDLAM 95
 
Name Accession Description Interval E-value
PRK07857 PRK07857
chorismate mutase;
1-93 3.08e-39

chorismate mutase;


Pssm-ID: 236117  Cd Length: 106  Bit Score: 126.34  E-value: 3.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608088    1 MRPEPPHHENAELAA-MNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIE 79
Cdd:PRK07857   1 MRPEPPHHENAELEArMPTGTDDPLSDAEIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIE 80

                         90
                 ....*....|....*
gi 15608088   80 RYSE-LGPDGKDLAI 93
Cdd:PRK07857  81 RYREeLGPEGKDLAM 95
CM_M_hiGC-arch TIGR01808
monofunctional chorismate mutase, high GC gram positive type; This model represents the ...
 28-93 1.16e-29

monofunctional chorismate mutase, high GC gram positive type; This model represents the monofunctional chorismate mutase from high GC gram-positive bacteria and archaea. Trusted annotations from Corynebacterium and Pyrococcus are aparrently the sole chorismate mutase enzymes in their respective genomes. This is coupled with the presence in those genomes of the enzymes of the chorismate pathways both up- and downstream of chorismate mutase. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130867 [Multi-domain]  Cd Length: 74  Bit Score: 101.14  E-value: 1.16e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608088    28 EIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAI 93
Cdd:TIGR01808   1 EIDTLREEIDRLDAEILALVKRRAEISQAIGKARMASGGTRLVHSREMKVIERYSELGPEGKDLAI 66
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 27-87 8.24e-11

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: 55.16  E-value: 8.24e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608088  27 PEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPD 87
Cdd:COG1605   5 ESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEE 65
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 33-85 1.30e-09

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: 50.18  E-value: 1.30e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15608088    33 REEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELG 85
Cdd:pfam01817   1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGA 53
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 33-87 2.27e-09

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: 49.50  E-value: 2.27e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 15608088     33 REEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPD 87
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEG 55
 
Name Accession Description Interval E-value
PRK07857 PRK07857
chorismate mutase;
1-93 3.08e-39

chorismate mutase;


Pssm-ID: 236117  Cd Length: 106  Bit Score: 126.34  E-value: 3.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608088    1 MRPEPPHHENAELAA-MNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIE 79
Cdd:PRK07857   1 MRPEPPHHENAELEArMPTGTDDPLSDAEIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIE 80

                         90
                 ....*....|....*
gi 15608088   80 RYSE-LGPDGKDLAI 93
Cdd:PRK07857  81 RYREeLGPEGKDLAM 95
CM_M_hiGC-arch TIGR01808
monofunctional chorismate mutase, high GC gram positive type; This model represents the ...
 28-93 1.16e-29

monofunctional chorismate mutase, high GC gram positive type; This model represents the monofunctional chorismate mutase from high GC gram-positive bacteria and archaea. Trusted annotations from Corynebacterium and Pyrococcus are aparrently the sole chorismate mutase enzymes in their respective genomes. This is coupled with the presence in those genomes of the enzymes of the chorismate pathways both up- and downstream of chorismate mutase. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130867 [Multi-domain]  Cd Length: 74  Bit Score: 101.14  E-value: 1.16e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15608088    28 EIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAI 93
Cdd:TIGR01808   1 EIDTLREEIDRLDAEILALVKRRAEISQAIGKARMASGGTRLVHSREMKVIERYSELGPEGKDLAI 66
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 27-87 8.24e-11

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: 55.16  E-value: 8.24e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608088  27 PEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPD 87
Cdd:COG1605   5 ESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEE 65
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 33-85 1.30e-09

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: 50.18  E-value: 1.30e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15608088    33 REEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELG 85
Cdd:pfam01817   1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGA 53
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 33-87 2.27e-09

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: 49.50  E-value: 2.27e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 15608088     33 REEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPD 87
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEG 55
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
 28-86 1.37e-06

bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 44.97  E-value: 1.37e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15608088   28 EIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGP 86
Cdd:PRK12595   5 ELEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLDMIAENNE 63
CM_archaeal TIGR01791
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ...
 29-80 1.55e-05

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: 39.72  E-value: 1.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15608088    29 IDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIER 80
Cdd:TIGR01791   1 IEELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIER 52
PRK06034 PRK06034
hypothetical protein; Provisional
 19-66 1.01e-03

hypothetical protein; Provisional


Pssm-ID: 235680 [Multi-domain]  Cd Length: 279  Bit Score: 36.61  E-value: 1.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 15608088   19 EMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGG 66
Cdd:PRK06034   1 GSTAPPAPPSLAELRWEIDAIDEELHQLLMERGDIIDRLIAVKRTQEV 48
pheA PRK10622
bifunctional chorismate mutase/prephenate dehydratase; Provisional
 31-85 7.47e-03

bifunctional chorismate mutase/prephenate dehydratase; Provisional


Pssm-ID: 182594 [Multi-domain]  Cd Length: 386  Bit Score: 34.32  E-value: 7.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15608088   31 TLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELG 85
Cdd:PRK10622   9 ALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLG 63
 
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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