NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|496030694|ref|WP_008755201|]
View 

chorismate mutase [Lachnoanaerobaculum saburreum]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CM_2 super family cl00693
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 2-88 2.38e-22

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..


The actual alignment was detected with superfamily member PRK07248:

Pssm-ID: 469881 [Multi-domain]  Cd Length: 87  Bit Score: 82.42  E-value: 2.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694  2 NELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKEYTDSAIDFIKDIMKISK 81
Cdd:PRK07248  1 MDLEEIRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDKVSSLVENKAYQETIVATFKDIMKRSR 80


                ....*..
gi 496030694 82 KYQEKLI 88
Cdd:PRK07248 81 DYQTQNI 87
 
Name Accession Description Interval E-value
PRK07248 PRK07248
chorismate mutase;
2-88 2.38e-22

chorismate mutase;


Pssm-ID: 168880 [Multi-domain]  Cd Length: 87  Bit Score: 82.42  E-value: 2.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694  2 NELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKEYTDSAIDFIKDIMKISK 81
Cdd:PRK07248  1 MDLEEIRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDKVSSLVENKAYQETIVATFKDIMKRSR 80


                ....*..
gi 496030694 82 KYQEKLI 88
Cdd:PRK07248 81 DYQTQNI 87
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 3-88 5.19e-19

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: 75.96  E-value: 5.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694   3 ELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKE-YTDSAIDFIKDIMKISK 81
Cdd:COG1605    6 SLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGlDPEFVEAIFREIISESI 85


                 ....*..
gi 496030694  82 KYQEKLI 88
Cdd:COG1605   86 ALQEKLL 92
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 8-85 5.23e-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: 68.67  E-value: 5.23e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496030694   8 RCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKE-YTDSAIDFIKDIMKISKKYQE 85
Cdd:pfam01817  1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGlDPDFIEAIFREIISESRALQK 79
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 8-85 2.01e-14

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: 62.21  E-value: 2.01e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496030694    8 RCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKEYTDSAI-DFIKDIMKISKKYQE 85
Cdd:smart00830  1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVeRIFREIIEASIALQK 79
CM_mono_grmpos TIGR01805
monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade ...
 4-84 2.26e-13

monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade of chorismate mutase proteins/domains from gram positive species. The sequence from Enterococcus is fused to the C-terminus of an aparrent acetyltransferase, and the seuence from Clostridium acetobutylicum (but not perfringens) is fused to the N-terminus of shikimate-5-dehydrogenase, another enzyme of the chorismate pathway. All the other members of this clade are mono-functional. Members of this clade from Streptococcus and Lactococcus have been found which represent the sole chorismate mutase domain in their respective genomes which also exhibit evidence of the enzymes of both the upstream and downstream branches of the chorismate pathways. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130864 [Multi-domain]  Cd Length: 81  Bit Score: 59.40  E-value: 2.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694   4 LENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKEYTDSAIDFIKDIMKISKKY 83
Cdd:TIGR01805  1 LELIRKKIDEIDDKLVVLFEERMEVVKEIAAYKKKNGIPIFDSKREQEIIDKCTKNVENKEYRETIEEFFRNIMDISKEV 80


                 .
gi 496030694  84 Q 84
Cdd:TIGR01805 81 Q 81
 
Name Accession Description Interval E-value
PRK07248 PRK07248
chorismate mutase;
2-88 2.38e-22

chorismate mutase;


Pssm-ID: 168880 [Multi-domain]  Cd Length: 87  Bit Score: 82.42  E-value: 2.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694  2 NELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKEYTDSAIDFIKDIMKISK 81
Cdd:PRK07248  1 MDLEEIRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDKVSSLVENKAYQETIVATFKDIMKRSR 80


                ....*..
gi 496030694 82 KYQEKLI 88
Cdd:PRK07248 81 DYQTQNI 87
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 3-88 5.19e-19

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: 75.96  E-value: 5.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694   3 ELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKE-YTDSAIDFIKDIMKISK 81
Cdd:COG1605    6 SLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGlDPEFVEAIFREIISESI 85


                 ....*..
gi 496030694  82 KYQEKLI 88
Cdd:COG1605   86 ALQEKLL 92
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 8-85 5.23e-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: 68.67  E-value: 5.23e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496030694   8 RCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKE-YTDSAIDFIKDIMKISKKYQE 85
Cdd:pfam01817  1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGlDPDFIEAIFREIISESRALQK 79
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 8-85 2.01e-14

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: 62.21  E-value: 2.01e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496030694    8 RCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKEYTDSAI-DFIKDIMKISKKYQE 85
Cdd:smart00830  1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVeRIFREIIEASIALQK 79
CM_mono_grmpos TIGR01805
monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade ...
 4-84 2.26e-13

monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade of chorismate mutase proteins/domains from gram positive species. The sequence from Enterococcus is fused to the C-terminus of an aparrent acetyltransferase, and the seuence from Clostridium acetobutylicum (but not perfringens) is fused to the N-terminus of shikimate-5-dehydrogenase, another enzyme of the chorismate pathway. All the other members of this clade are mono-functional. Members of this clade from Streptococcus and Lactococcus have been found which represent the sole chorismate mutase domain in their respective genomes which also exhibit evidence of the enzymes of both the upstream and downstream branches of the chorismate pathways. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130864 [Multi-domain]  Cd Length: 81  Bit Score: 59.40  E-value: 2.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694   4 LENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKEYTDSAIDFIKDIMKISKKY 83
Cdd:TIGR01805  1 LELIRKKIDEIDDKLVVLFEERMEVVKEIAAYKKKNGIPIFDSKREQEIIDKCTKNVENKEYRETIEEFFRNIMDISKEV 80


                 .
gi 496030694  84 Q 84
Cdd:TIGR01805 81 Q 81
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 1-55 1.02e-10

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 56.04  E-value: 1.02e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496030694   1 MNELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISK 55
Cdd:PRK11199   2 VAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLAS 56
PRK07857 PRK07857
chorismate mutase;
3-60 4.54e-06

chorismate mutase;


Pssm-ID: 236117  Cd Length: 106  Bit Score: 41.22  E-value: 4.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496030694   3 ELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESI 60
Cdd:PRK07857  29 EIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIERYREEL 86
pheA PRK10622
bifunctional chorismate mutase/prephenate dehydratase; Provisional
 2-62 6.71e-06

bifunctional chorismate mutase/prephenate dehydratase; Provisional


Pssm-ID: 182594 [Multi-domain]  Cd Length: 386  Bit Score: 42.41  E-value: 6.71e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496030694   2 NELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKN 62
Cdd:PRK10622   5 NPLLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLGKA 65
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
 1-85 1.14e-05

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


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 41.89  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694   1 MNELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSEsiKNK-EYTDSAIDFI-KDIMK 78
Cdd:PRK12595   3 NEELEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLDMIAE--NNEgPFEDSTIQHLfKEIFK 80


                 ....*..
gi 496030694  79 ISKKYQE 85
Cdd:PRK12595  81 ASLELQE 87
PRK06285 PRK06285
chorismate mutase; Provisional
 2-88 1.17e-05

chorismate mutase; Provisional


Pssm-ID: 180509 [Multi-domain]  Cd Length: 96  Bit Score: 40.02  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694  2 NELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSE-SIKNKEYTDSAIDFIKDIMKIS 80
Cdd:PRK06285  7 KRLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKlCEEHNIDENIGLKIMKILMEHS 86


                ....*...
gi 496030694 81 KKYQEKLI 88
Cdd:PRK06285 87 KELQKEYL 94
CM_mono2 TIGR01806
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ...
 17-87 1.34e-05

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: 40.10  E-value: 1.34e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496030694   17 ELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKEYT-DSAIDFIKDIMKISKKYQEKL 87
Cdd:TIGR01806   8 QLVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDpDYVTRFFQAQINANKAIQYRL 79
CM_archaeal TIGR01791
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ...
 4-84 1.34e-04

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: 37.02  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496030694   4 LENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAIISKVSESIKNKEYTDSAIDFIKDI-MKISKK 82
Cdd:TIGR01791  1 IEELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEIFEIlMSLSKE 80


                 ..
gi 496030694  83 YQ 84
Cdd:TIGR01791 81 EQ 82
PRK08055 PRK08055
chorismate mutase; Provisional
 25-84 2.91e-04

chorismate mutase; Provisional


Pssm-ID: 236143  Cd Length: 181  Bit Score: 37.37  E-value: 2.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496030694  25 RMATVHDIAKYKIANNLPILNQGREEAIISKV-SESIKNKEYTDSAIDFIKDIMKISKKYQ 84
Cdd:PRK08055  37 RLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAeEEAASNGLDPESIKPFIVAQMDAAKAIQ 97
PRK06443 PRK06443
chorismate mutase; Validated
 3-52 6.19e-04

chorismate mutase; Validated


Pssm-ID: 235801  Cd Length: 177  Bit Score: 36.42  E-value: 6.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496030694   3 ELENLRCRIDAIDKELIAVFEKRMATVHDIAKYKIANNLPILNQGREEAI 52
Cdd:PRK06443   6 DMEDLRSEILENTMDIIELIEKRRELARMIGIIKMRNGLSIRDSERENYV 55
CM_P2 TIGR01807
chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of ...
 4-58 7.47e-03

chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of two separate clades of the chorismate mutase domain of the gamma and beta and epsilon proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. It is also found in Aquifex aolicus. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130866 [Multi-domain]  Cd Length: 76  Bit Score: 32.42  E-value: 7.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496030694   4 LENLRCRIDAIDKELIAVFEKRMATVHDIA--KYKIANNLPILNQGREEAIISKVSE 58
Cdd:TIGR01807  1 LEELRNKIDAIDDRILDLLSERATYAQAVGelKGSGASGASFYRPEREAQVIRRLQN 57
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH