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Conserved domains on  [gi|15610086|ref|NP_217465|]
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chorismate pyruvate-lyase [Mycobacterium tuberculosis H37Rv]

Protein Classification

chorismate--pyruvate lyase family protein( domain architecture ID 10006995)

chorismate--pyruvate lyase family protein may catalyze the first step in ubiquinone synthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate

EC:  4.1.3.40
Gene Ontology:  GO:0008813|GO:0006744|GO:0005737
PubMed:  11583838|1644758|8012607

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiC COG3161
4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) [Coenzyme transport and metabolism]; ...
 8-176 5.75e-26

4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) [Coenzyme transport and metabolism]; 4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) is part of the Pathway/BioSystem: Ubiquinone biosynthesis


:

Pssm-ID: 442395  Cd Length: 177  Bit Score: 98.17  E-value: 5.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086   8 DQEIRKLNRDLRILIAANGTLTRVLNIVADDEVIVQIVKQRIhdVSPKLSEFEQLGQVGVGRVLQRYIILKGrnSEHLFV 87
Cdd:COG3161  16 PPLLSQLPPALRDWLLTDGSLTRRLEALTGGPFSVEVLRQGF--VPADADEAPLLGLPAGERVLVREVLLRG--DGQPWV 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086  88 AAESLIAIDRLPAAIITRLTQTNDPLGEVMAAsHIETFKEEAKVWVGDLPGWLALHGyQNSRKRAVARRYRVISGGQPIM 167
Cdd:COG3161  92 YARSVIPLSTLPGAWRELLRLGNRPLGELLFA-DPELRRDPLEVGRLEPAHPLARRG-LAAPGPLWARRSRFRLGGPPLL 169


                ....*....
gi 15610086 168 vVTEHFLRS 176
Cdd:COG3161 170 -VTEVFLPA 177
 
Name Accession Description Interval E-value
UbiC COG3161
4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) [Coenzyme transport and metabolism]; ...
 8-176 5.75e-26

4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) [Coenzyme transport and metabolism]; 4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 442395  Cd Length: 177  Bit Score: 98.17  E-value: 5.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086   8 DQEIRKLNRDLRILIAANGTLTRVLNIVADDEVIVQIVKQRIhdVSPKLSEFEQLGQVGVGRVLQRYIILKGrnSEHLFV 87
Cdd:COG3161  16 PPLLSQLPPALRDWLLTDGSLTRRLEALTGGPFSVEVLRQGF--VPADADEAPLLGLPAGERVLVREVLLRG--DGQPWV 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086  88 AAESLIAIDRLPAAIITRLTQTNDPLGEVMAAsHIETFKEEAKVWVGDLPGWLALHGyQNSRKRAVARRYRVISGGQPIM 167
Cdd:COG3161  92 YARSVIPLSTLPGAWRELLRLGNRPLGELLFA-DPELRRDPLEVGRLEPAHPLARRG-LAAPGPLWARRSRFRLGGPPLL 169


                ....*....
gi 15610086 168 vVTEHFLRS 176
Cdd:COG3161 170 -VTEVFLPA 177
Rv2949c-like pfam01947
Chorismate pyruvate-lyase Rv2949c-like; This domain is found in chorismate pyruvate-lyases (EC: ...
 26-173 1.56e-03

Chorismate pyruvate-lyase Rv2949c-like; This domain is found in chorismate pyruvate-lyases (EC:4.1.3.40, also known as 4-HB synthase and p-hydroxybenzoic acid synthase) such as those found in Mycobacterium tuberculosis where it removes the pyruvyl group from chorismate to provide 4-hydroxybenzoate (4HB). The chorismate pyruvate-lyase encoded by sll1797 in cyanobacteria Synechocystis sp., has been shown to catalyze the initial and essential step in plastoquinone biosynthesis. In E. coli, the chorismate lyase (UbiC) catalyzes the conversion of chorismate to p-hydroxybenzoate and pyruvate in the biosynthesis of ubiquinone as well.


Pssm-ID: 366866  Cd Length: 149  Bit Score: 37.64  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086    26 GTLTRVLNIVADDEVIVQIVKQRIHDVSPKL--SEFEQLGqvgvGRVLQRYIILkgRNSEHLFVAAESLIAIDRLPAAii 103
Cdd:pfam01947   5 GSPTRHLQLLTGEPTEVDLIAMSPIPSDDESapKEVQELG----GPLLRRQVWL--RCNGQPLAYAESWWNLERLEKY-- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086   104 trLTQTNDPLGEVMAASHIETFKEEAKVWVGDlPGWLAlHGYQnSRKRAVARRYRVISGGQPIMVVTEHF 173
Cdd:pfam01947  77 --LRDRDQPIWKSLTQHRLELFREIDGLYLGE-ADWLE-EAFG-EKGPFWSRHYRFFHKGKPLTVIYEVF 141
 
Name Accession Description Interval E-value
UbiC COG3161
4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) [Coenzyme transport and metabolism]; ...
 8-176 5.75e-26

4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) [Coenzyme transport and metabolism]; 4-hydroxybenzoate synthetase (chorismate-pyruvate lyase) is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 442395  Cd Length: 177  Bit Score: 98.17  E-value: 5.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086   8 DQEIRKLNRDLRILIAANGTLTRVLNIVADDEVIVQIVKQRIhdVSPKLSEFEQLGQVGVGRVLQRYIILKGrnSEHLFV 87
Cdd:COG3161  16 PPLLSQLPPALRDWLLTDGSLTRRLEALTGGPFSVEVLRQGF--VPADADEAPLLGLPAGERVLVREVLLRG--DGQPWV 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086  88 AAESLIAIDRLPAAIITRLTQTNDPLGEVMAAsHIETFKEEAKVWVGDLPGWLALHGyQNSRKRAVARRYRVISGGQPIM 167
Cdd:COG3161  92 YARSVIPLSTLPGAWRELLRLGNRPLGELLFA-DPELRRDPLEVGRLEPAHPLARRG-LAAPGPLWARRSRFRLGGPPLL 169


                ....*....
gi 15610086 168 vVTEHFLRS 176
Cdd:COG3161 170 -VTEVFLPA 177
Rv2949c-like pfam01947
Chorismate pyruvate-lyase Rv2949c-like; This domain is found in chorismate pyruvate-lyases (EC: ...
 26-173 1.56e-03

Chorismate pyruvate-lyase Rv2949c-like; This domain is found in chorismate pyruvate-lyases (EC:4.1.3.40, also known as 4-HB synthase and p-hydroxybenzoic acid synthase) such as those found in Mycobacterium tuberculosis where it removes the pyruvyl group from chorismate to provide 4-hydroxybenzoate (4HB). The chorismate pyruvate-lyase encoded by sll1797 in cyanobacteria Synechocystis sp., has been shown to catalyze the initial and essential step in plastoquinone biosynthesis. In E. coli, the chorismate lyase (UbiC) catalyzes the conversion of chorismate to p-hydroxybenzoate and pyruvate in the biosynthesis of ubiquinone as well.


Pssm-ID: 366866  Cd Length: 149  Bit Score: 37.64  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086    26 GTLTRVLNIVADDEVIVQIVKQRIHDVSPKL--SEFEQLGqvgvGRVLQRYIILkgRNSEHLFVAAESLIAIDRLPAAii 103
Cdd:pfam01947   5 GSPTRHLQLLTGEPTEVDLIAMSPIPSDDESapKEVQELG----GPLLRRQVWL--RCNGQPLAYAESWWNLERLEKY-- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610086   104 trLTQTNDPLGEVMAASHIETFKEEAKVWVGDlPGWLAlHGYQnSRKRAVARRYRVISGGQPIMVVTEHF 173
Cdd:pfam01947  77 --LRDRDQPIWKSLTQHRLELFREIDGLYLGE-ADWLE-EAFG-EKGPFWSRHYRFFHKGKPLTVIYEVF 141
 
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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