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Conserved domains on  [gi|489923110|ref|WP_003826456|]
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MULTISPECIES: bifunctional chorismate mutase/prephenate dehydrogenase [Citrobacter]

Protein Classification

bifunctional chorismate mutase/prephenate dehydrogenase( domain architecture ID 11485267)

bifunctional chorismate mutase/prephenate dehydrogenase (TyrA) catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 1-373 0e+00

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


:

Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 780.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110   1 MVAELTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMR 80
Cdd:PRK11199   1 MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRVMR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110  81 ESYSSENDKGFKTLCPSLRPVVIVGGGGQMGRLFEKMLTLSGYQVRILEQQDWDRAPEIVSDAGMVIVSVPIHVTEQVIA 160
Cdd:PRK11199  81 ESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDILADAGMVIVSVPIHLTEEVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 161 KLPRLPSDCILVDLASVKNGPLQAMLAAHDGPVVGLHPMFGPDSGSLAKQVVVWCDGRQPEAYQWFLEQIQVWGARLHRI 240
Cdd:PRK11199 161 RLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQVVVVCDGRQPEAYQWLLEQIQVWGARLHRI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSESNLALIKRY 320
Cdd:PRK11199 241 SAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRY 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489923110 321 YQRFGEAIGLLEQGDKQAFIDSFRKVEHWFGDYAKRFQSESRTLLRQANDSRP 373
Cdd:PRK11199 321 YQRFGEALELLEQGDKQAFIDSFRKVEHWFGDYAEQFLKESRSLLQQANDNRQ 373
 
Name Accession Description Interval E-value
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 1-373 0e+00

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 780.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110   1 MVAELTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMR 80
Cdd:PRK11199   1 MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRVMR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110  81 ESYSSENDKGFKTLCPSLRPVVIVGGGGQMGRLFEKMLTLSGYQVRILEQQDWDRAPEIVSDAGMVIVSVPIHVTEQVIA 160
Cdd:PRK11199  81 ESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDILADAGMVIVSVPIHLTEEVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 161 KLPRLPSDCILVDLASVKNGPLQAMLAAHDGPVVGLHPMFGPDSGSLAKQVVVWCDGRQPEAYQWFLEQIQVWGARLHRI 240
Cdd:PRK11199 161 RLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQVVVVCDGRQPEAYQWLLEQIQVWGARLHRI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSESNLALIKRY 320
Cdd:PRK11199 241 SAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRY 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489923110 321 YQRFGEAIGLLEQGDKQAFIDSFRKVEHWFGDYAKRFQSESRTLLRQANDSRP 373
Cdd:PRK11199 321 YQRFGEALELLEQGDKQAFIDSFRKVEHWFGDYAEQFLKESRSLLQQANDNRQ 373
CM_T TIGR01799
chorismate mutase domain of T-protein; This model represents the chorismate mutase domain of ...
 5-87 7.56e-37

chorismate mutase domain of T-protein; This model represents the chorismate mutase domain of the gamma proteobacterial "T-protein" which consists of an N-terminal chorismate mutase domain and a C-terminal prephenate dehydrogenase domain. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130858 [Multi-domain]  Cd Length: 83  Bit Score: 128.48  E-value: 7.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110    5 LTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYS 84
Cdd:TIGR01799   1 LEDLRGEIDGVDQELLHLLAKRLELVAQVGKVKHAAGLPIYAPEREAAMLAARREEAEKAGIAPDLIEDVLRRFMRESYA 80


                  ...
gi 489923110   85 SEN 87
Cdd:TIGR01799  81 NEN 83
FDXACB COG4937
Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis];
101-356 1.22e-26

Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443964 [Multi-domain]  Cd Length: 443  Bit Score: 110.11  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 101 VVIVGGGGQMGRLFEKMLTLSGYQVRILEQQDWDRAPE------------IVSDAGMVIVSVPIHVTEQVIAKL-PRLPS 167
Cdd:COG4937    7 IGIIGGTGEMGQWFAKFFKDFGFEVTIWGRGGKVEIAEklgvgfandndaAIADADIIIVSVPIVITETTIVEVaPKMPK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 168 DCILVDLASVKNGPLQAMLAAHDGPVVGL--HPMFGPDSGSLAKQVVVW------CDGRQPEAYQWFLEQiqvwGARLHR 239
Cdd:COG4937   87 GSLLMDLTSTKVKPVEAMEKYAPVDVEILgtHPMFGPTPPTLSGQIVILtpiegrCDKWFPKIRNLLEEE----GARIII 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 240 ISAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSESNLALIKR 319
Cdd:COG4937  163 ITPEEHDRMMSVVQGLTHFAYISIGATIKRLDFDVKESRKFASPVYELMLDIIGRIIGQNPYLYASIQMENPEVKKVHET 242

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489923110 320 YYQRFGEAIGLLEQGDKQAFIDSFRKVEHWFGDYAKR 356
Cdd:COG4937  243 FIEECNELSNIVRKDDEEGFVEIMKEAAKHFGDTESA 279
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 9-87 2.09e-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: 67.52  E-value: 2.09e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489923110    9 RDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYSSEN 87
Cdd:pfam01817   1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 9-87 3.40e-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: 67.22  E-value: 3.40e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489923110     9 RDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYSSEN 87
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
 
Name Accession Description Interval E-value
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 1-373 0e+00

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 780.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110   1 MVAELTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMR 80
Cdd:PRK11199   1 MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRVMR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110  81 ESYSSENDKGFKTLCPSLRPVVIVGGGGQMGRLFEKMLTLSGYQVRILEQQDWDRAPEIVSDAGMVIVSVPIHVTEQVIA 160
Cdd:PRK11199  81 ESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDILADAGMVIVSVPIHLTEEVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 161 KLPRLPSDCILVDLASVKNGPLQAMLAAHDGPVVGLHPMFGPDSGSLAKQVVVWCDGRQPEAYQWFLEQIQVWGARLHRI 240
Cdd:PRK11199 161 RLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQVVVVCDGRQPEAYQWLLEQIQVWGARLHRI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSESNLALIKRY 320
Cdd:PRK11199 241 SAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRY 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489923110 321 YQRFGEAIGLLEQGDKQAFIDSFRKVEHWFGDYAKRFQSESRTLLRQANDSRP 373
Cdd:PRK11199 321 YQRFGEALELLEQGDKQAFIDSFRKVEHWFGDYAEQFLKESRSLLQQANDNRQ 373
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 101-352 1.08e-47

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 167.47  E-value: 1.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 101 VVIVGGGGQMGRLFEKMLTLSGYQVRIleqqdWDRAP-------------------EIVSDAGMVIVSVPIHVTEQVIAK 161
Cdd:PRK08655   3 ISIIGGTGGLGKWFARFLKEKGFEVIV-----TGRDPkkgkevakelgveyandniDAAKDADIVIISVPINVTEDVIKE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 162 L-PRLPSDCILVDLASVKNGPLQAML--AAHDGPVVGLHPMFGPDSGSLAKQVVVWC--DGRQ----PEAYQWFLEQiqv 232
Cdd:PRK08655  78 VaPHVKEGSLLMDVTSVKERPVEAMEeyAPEGVEILPTHPMFGPRTPSLKGQVVILTptEKRSnpwfDKVKNFLEKE--- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 233 wGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMS--- 309
Cdd:PRK08655 155 -GARVIVTSPEEHDRIMSVVQGLTHFAYISIASTLKRLGVDIKESRKFASPIYELMIDIIGRILGQNPYLYASIQMNnpq 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 489923110 310 -SESNLALIKRyYQRFGEaigLLEQGDKQAFIDSFRKVEHWFGD 352
Cdd:PRK08655 234 iPEIHETFIKE-CEELSE---LVKNGDREEFVERMKEAAKHFGD 273
CM_T TIGR01799
chorismate mutase domain of T-protein; This model represents the chorismate mutase domain of ...
 5-87 7.56e-37

chorismate mutase domain of T-protein; This model represents the chorismate mutase domain of the gamma proteobacterial "T-protein" which consists of an N-terminal chorismate mutase domain and a C-terminal prephenate dehydrogenase domain. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130858 [Multi-domain]  Cd Length: 83  Bit Score: 128.48  E-value: 7.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110    5 LTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYS 84
Cdd:TIGR01799   1 LEDLRGEIDGVDQELLHLLAKRLELVAQVGKVKHAAGLPIYAPEREAAMLAARREEAEKAGIAPDLIEDVLRRFMRESYA 80


                  ...
gi 489923110   85 SEN 87
Cdd:TIGR01799  81 NEN 83
FDXACB COG4937
Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis];
101-356 1.22e-26

Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443964 [Multi-domain]  Cd Length: 443  Bit Score: 110.11  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 101 VVIVGGGGQMGRLFEKMLTLSGYQVRILEQQDWDRAPE------------IVSDAGMVIVSVPIHVTEQVIAKL-PRLPS 167
Cdd:COG4937    7 IGIIGGTGEMGQWFAKFFKDFGFEVTIWGRGGKVEIAEklgvgfandndaAIADADIIIVSVPIVITETTIVEVaPKMPK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 168 DCILVDLASVKNGPLQAMLAAHDGPVVGL--HPMFGPDSGSLAKQVVVW------CDGRQPEAYQWFLEQiqvwGARLHR 239
Cdd:COG4937   87 GSLLMDLTSTKVKPVEAMEKYAPVDVEILgtHPMFGPTPPTLSGQIVILtpiegrCDKWFPKIRNLLEEE----GARIII 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 240 ISAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSESNLALIKR 319
Cdd:COG4937  163 ITPEEHDRMMSVVQGLTHFAYISIGATIKRLDFDVKESRKFASPVYELMLDIIGRIIGQNPYLYASIQMENPEVKKVHET 242

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489923110 320 YYQRFGEAIGLLEQGDKQAFIDSFRKVEHWFGDYAKR 356
Cdd:COG4937  243 FIEECNELSNIVRKDDEEGFVEIMKEAAKHFGDTESA 279
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 3-166 1.49e-24

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: 98.30  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110   3 AELTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRES 82
Cdd:COG1605    5 ESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISES 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110  83 YSSENDKGFKTLCpslrPVVIVGGGGQMGRLFEKMLTLSGYQVRILEQQDWDRAPEIVSDAGMVIVSVPIHVTEQVIAKL 162
Cdd:COG1605   85 IALQEKLLAEVAY----LGPEGGFTGQAAGKHFGGSAASLPAAAIDEVFREVEAGGAAYGVVPVENSTEGGVVETLDLLL 160


                 ....
gi 489923110 163 PRLP 166
Cdd:COG1605  161 ASPL 164
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 136-345 2.52e-21

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 92.50  E-value: 2.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 136 APEIVSDAGMVIVSVPIHVTEQVIAKL-PRLPSDCILVDLASVKNGPLQAM--LAAHDGPVVGLHPMFGPD-SGSLA--- 208
Cdd:COG0287   55 LEEAVADADLVVLAVPVGATIEVLAELaPHLKPGAIVTDVGSVKGAVVEAAeaLLPDGVRFVGGHPMAGTEkSGPEAada 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 209 -----KQVVVwC--DGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVQlEQLLALS 281
Cdd:COG0287  135 dlfegAPYIL-TptEGTDPEALERVEELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDE-EEILRLA 212

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489923110 282 SPIYRlelAMVgRLFAQDPQLYADIIMS-SESNLALIKRYYQRFGEAIGLLEQGDKQAFIDSFRK 345
Cdd:COG0287  213 AGGFR---DTT-RIAASDPEMWRDIFLAnREALLEALDRFIEELDALRDALEAGDGEALEELLER 273
PRK08818 PRK08818
prephenate dehydrogenase; Provisional
 97-338 1.17e-18

prephenate dehydrogenase; Provisional


Pssm-ID: 181561 [Multi-domain]  Cd Length: 370  Bit Score: 86.46  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110  97 SLRPVV-IVGGGGQMGRLFEKML-TLSGYQVRILEQQDWDRAPE--IVSDAGMVIVSVPIHVTEQVIAKLPRLP----SD 168
Cdd:PRK08818   2 IAQPVVgIVGSAGAYGRWLARFLrTRMQLEVIGHDPADPGSLDPatLLQRADVLIFSAPIRHTAALIEEYVALAggraAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 169 CILVDLASVKNGPLQAMLAAHdGPVVGLHPMFGP-DSGSLAKQVVVWCDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQ 247
Cdd:PRK08818  82 QLWLDVTSIKQAPVAAMLASQ-AEVVGLHPMTAPpKSPTLKGRVMVVCEARLQHWSPWVQSLCSALQAECVYATPEHHDR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 248 NMAFIQALRHfATfayglHLAEENV---------QLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSESNLALIK 318
Cdd:PRK08818 161 VMALVQAMVH-AT-----HLAQAGVlrdyapllgELRALMPYRSASFELDTAVIARILSLNPSIYEDIQFGNPYVGEMLD 234

                        250       260
                 ....*....|....*....|
gi 489923110 319 RYYQRFGEAIGLLEQGDKQA 338
Cdd:PRK08818 235 RLLAQLQELRALVAQGDDAA 254
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 9-87 2.09e-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: 67.52  E-value: 2.09e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489923110    9 RDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYSSEN 87
Cdd:pfam01817   1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 9-87 3.40e-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: 67.22  E-value: 3.40e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489923110     9 RDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYSSEN 87
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
PRK08507 PRK08507
prephenate dehydrogenase; Validated
 138-314 6.77e-11

prephenate dehydrogenase; Validated


Pssm-ID: 181452 [Multi-domain]  Cd Length: 275  Bit Score: 62.22  E-value: 6.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 138 EIVS-----DAGMVIVSVPIHVTEQVIAKLPRLPSDCILVDLASVKNGPLQAMLAAHDGPVVGLHPM-----FGPDS--- 204
Cdd:PRK08507  49 EIVSfeelkKCDVIFLAIPVDAIIEILPKLLDIKENTTIIDLGSTKAKIIESVPKHIRKNFIAAHPMagtenSGPKAaik 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 205 GSLAKQVVVWCDGRQP-EAYQWFLEQI-QVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLH-LAEENVQleQLLALS 281
Cdd:PRK08507 129 GLYEGKVVVLCDVEKSgEKHQERAKEIfSGLGMRIVYMDAKEHDLHAAYISHLPHIISFALANTvLKEEDER--NIFDLA 206

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489923110 282 SPIYRlelAMVgRLFAQDPQLYADIIMSSESNL 314
Cdd:PRK08507 207 GGGFR---SMS-RLAKSSPAMWSDIFKQNKENV 235
PDH_C pfam20463
Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate ...
 241-344 5.95e-10

Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate dehydrogenases EC:1.3.1.12 (PDHs) involved in tyrosine biosynthesis. This is the C-terminal, helical dimerization domain of PDHs.


Pssm-ID: 466612 [Multi-domain]  Cd Length: 102  Bit Score: 55.85  E-value: 5.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110  241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLelamVGRLFAQDPQLYADIIMSSESNLA-LIKR 319
Cdd:pfam20463   1 SPETHDRVVAVVSHLPHFVAIALAATLAELGVDIKEARKLASGGFRD----MTRIAGSNPELWADIQTHNARAVLeALDD 76

                          90       100
                  ....*....|....*....|....*
gi 489923110  320 YYQRFGEAIGLLEQGDKQAFIDSFR 344
Cdd:pfam20463  77 FIAELKQLKELIRNGDWEELVEYMK 101
PLN02712 PLN02712
arogenate dehydrogenase
 106-324 6.68e-09

arogenate dehydrogenase


Pssm-ID: 215382 [Multi-domain]  Cd Length: 667  Bit Score: 57.68  E-value: 6.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 106 GGGQMGRLFEKMLTLSGYQVRILEQQDW-DRAPEI----VSDAG--------MVIVSVPIHVTEQVIAKLP--RLPSDCI 170
Cdd:PLN02712 376 GFGNFGQFLAKTMVKQGHTVLAYSRSDYsDEAQKLgvsyFSDADdlceehpeVILLCTSILSTEKVLKSLPfqRLKRSTL 455

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 171 LVDLASVKNGPLQAMLAA--HDGPVVGLHPMFGPDSGS--------LAKQVVVWCDGRQPEAYQWFLEQIQVWGARLHRI 240
Cdd:PLN02712 456 FVDVLSVKEFPRNLFLQHlpQDFDILCTHPMFGPESGKngwnnlafVFDKVRIGSDDRRVSRCDSFLDIFAREGCRMVEM 535

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 241 SAVEHDQNMAFIQalrhFATFAYGLHLaeENVQLEqllalSSPI----YRLELAMVGRLFAQDPQLYADIIMSSESNLAL 316
Cdd:PLN02712 536 SCAEHDWHAAGSQ----FITHTMGRLL--EKLGLE-----STPIntkgYETLLNLVENTAGDSFDLYYGLFMYNVNAMEQ 604


                 ....*...
gi 489923110 317 IKRYYQRF 324
Cdd:PLN02712 605 LERLDLAF 612
PRK06545 PRK06545
prephenate dehydrogenase; Validated
 138-338 7.87e-09

prephenate dehydrogenase; Validated


Pssm-ID: 235824 [Multi-domain]  Cd Length: 359  Bit Score: 56.45  E-value: 7.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 138 EIVSDAGMVIVSVPIHVTEQVIAKLPR--LPSDCILVDLASVKNGPLQAMLAAHDGPV--VGLHPMFGPD-SGSLAKQ-- 210
Cdd:PRK06545  56 RAAAEADLIVLAVPVDATAALLAELADleLKPGVIVTDVGSVKGAILAEAEALLGDLIrfVGGHPMAGSHkSGVAAARad 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 211 -------VVVWCDGRQPEAyqwfLEQIQVW----GARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENvqleqLLA 279
Cdd:PRK06545 136 lfenapwVLTPDDHTDPDA----VAELKDLlsgtGAKFVVLDAEEHDRAVALVSHLPHILASSLAARLAGEH-----PLA 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489923110 280 LSspiyrleLAMVG-----RLFAQDPQLYADIImssESN----LALIKRYYQRFGEAIGLLEQGDKQA 338
Cdd:PRK06545 207 LR-------LAAGGfrditRIASSDPGMWRDIL---ESNaealLDALDEWIEDLDRARDALESGDAEA 264
PDH_N pfam02153
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ...
 138-237 2.73e-08

Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face.


Pssm-ID: 460467 [Multi-domain]  Cd Length: 154  Bit Score: 52.39  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110  138 EIVSDAGMVIVSVPIHVTEQVIAKL-PRLPSDCILVDLASVKNGP---LQAMLAAHDgpVVGLHPMFGPDS--------G 205
Cdd:pfam02153  41 EAVREADIVFLAVPVEQTLPVLKELaPHLKEDALITDVGSVKVKIireLEQHLPDKS--FVPGHPMAGTEKsgpdaaraN 118

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 489923110  206 SLAKQVVVWCDGRQPEAyQWFLEQIQVW---GARL 237
Cdd:pfam02153 119 LFENAPVILTPTEKTDT-EALNCVKELLegvGARV 152
PLN02256 PLN02256
arogenate dehydrogenase
 146-257 3.82e-08

arogenate dehydrogenase


Pssm-ID: 215144 [Multi-domain]  Cd Length: 304  Bit Score: 54.28  E-value: 3.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 146 VIVSVPIHVTEQVIAKLP--RLPSDCILVDLASVKNGPLQAMLAA--HDGPVVGLHPMFGPDSG--SLAKQVVVW----- 214
Cdd:PLN02256  96 VLLCTSILSTEAVLRSLPlqRLKRSTLFVDVLSVKEFPKNLLLQVlpEEFDILCTHPMFGPESGkgGWAGLPFVYdkvri 175

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489923110 215 -CDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRH 257
Cdd:PLN02256 176 gDEGEREARCERFLDIFEEEGCRMVEMSCEEHDRYAAGSQFITH 219
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 138-343 1.58e-07

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 53.07  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 138 EIVSDAGMVIVSVPIHVTEQVIAKL-PRLPSDCILVDLASVKNGPLQAMLAAHDG-P--VVGLHPMFGPD-SGSLAKQVV 212
Cdd:PRK14806  59 EAVSGADVIVLAVPVLAMEKVLADLkPLLSEHAIVTDVGSTKGNVVDAARAVFGElPagFVPGHPIAGSEkSGVHAANAD 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 213 VWCDGR-----QPEAYQWFLEQI-QVW---GARLHRISAVEHDQNMAFIQALRHFatFAYGL--HLAEENVQLEqllals 281
Cdd:PRK14806 139 LFRNHKviltpLAETDPAALARVdRLWravGADVLHMDVAHHDEVLAATSHLPHL--LAFSLvdQLANREDNLD------ 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489923110 282 spIYRleLAMVG-----RLFAQDPQLYADIIMSS-ESNLALIKRYYQRFGEAIGLLEQGDKQAFIDSF 343
Cdd:PRK14806 211 --IFR--YAAGGfrdftRIAASDPVMWHDIFLANkEAVLRALDHFRDDLDALRAAIEAGDGHALLGVF 274
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
134-343 2.77e-07

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 51.51  E-value: 2.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 134 DRAPEIVSDAGMVIVSVPIHVTEQVIAKL-PRLPSDCILVDLASVKnGPLQAMLAAHDGPVVGL---HPMF-----GPDS 204
Cdd:PRK07502  58 TSAAEAVKGADLVILCVPVGASGAVAAEIaPHLKPGAIVTDVGSVK-ASVIAAMAPHLPEGVHFipgHPLAgtehsGPDA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 205 GSLAKQVVVWC-----DGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFatFAYGL-----HLaeENVQL 274
Cdd:PRK07502 137 GFAELFENRWCiltppEGTDPAAVARLTAFWRALGARVEEMDPEHHDLVLAITSHLPHL--IAYTIvgtadDL--ERVTE 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489923110 275 EQLLALSSPIYRlelaMVGRLFAQDPQLYADIIMSS-ESNLALIkryyQRFGEAIGLLEQ----GDKQAFIDSF 343
Cdd:PRK07502 213 SEVIKYSASGFR----DFTRIAASDPTMWRDVFLHNkDAVLEML----GRFTEDLAALQRairwGDGDALFDLF 278
PRK06444 PRK06444
prephenate dehydrogenase; Provisional
 101-255 6.87e-07

prephenate dehydrogenase; Provisional


Pssm-ID: 102381 [Multi-domain]  Cd Length: 197  Bit Score: 49.46  E-value: 6.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 101 VVIVGGGGQMGRLFEKMLTLSGYQVRIleqQDWDrapeivsdagMVIVSVPIHVTEQVIAKlprlpSDCILVDLASVKng 180
Cdd:PRK06444   3 EIIIGKNGRLGRVLCSILDDNGLGVYI---KKAD----------HAFLSVPIDAALNYIES-----YDNNFVEISSVK-- 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489923110 181 plqAMLAAHDGPVVGLHPMFGPDS--GSLAKQVVVWCDGRQPEaYQWFLEQIqVWGARLHRISAVEHDQNMAFIQAL 255
Cdd:PRK06444  63 ---WPFKKYSGKIVSIHPLFGPMSynDGVHRTVIFINDISRDN-YLNEINEM-FRGYHFVEMTADEHDLLMSEIMVK 134
CM_archaeal TIGR01791
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ...
 5-82 9.63e-06

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: 43.57  E-value: 9.63e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489923110    5 LTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRES 82
Cdd:TIGR01791   1 IEELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEIFEILMSLS 78
PLN02712 PLN02712
arogenate dehydrogenase
 145-355 1.69e-05

arogenate dehydrogenase


Pssm-ID: 215382 [Multi-domain]  Cd Length: 667  Bit Score: 46.90  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 145 MVIVSVPIHVTEQVIAKLP--RLPSDCILVDLASVKNGPLQAMLA--AHDGPVVGLHPMFGPDSGSLA--------KQVV 212
Cdd:PLN02712 111 VILLCTSIISTENVLKSLPlqRLKRNTLFVDVLSVKEFAKNLLLDylPEDFDIICSHPMFGPQSAKHGwdglrfvyEKVR 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 213 VWCDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQalrhFATFAYGLhlaeenvQLEQLLALSSPI----YRLE 288
Cdd:PLN02712 191 IGNEELRVSRCKSFLEVFEREGCKMVEMSCTEHDKYAAESQ----FITHTVGR-------VLEMLKLESTPIntkgYESL 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489923110 289 LAMVGRLFAQDPQLYADIIMSSESNLALIKRY--------YQRFGEAIGLLEqgdKQAFIDSFRKVeHWFGDYAK 355
Cdd:PLN02712 260 LDLVENTCGDSFDLYYGLFMYNKNSLEMLERLdlafealrKQLFGRLHGVVR---KQLFGNEEKKV-HVQPNHAE 330
PRK09239 PRK09239
chorismate mutase; Provisional
 1-81 5.71e-05

chorismate mutase; Provisional


Pssm-ID: 181719 [Multi-domain]  Cd Length: 104  Bit Score: 41.93  E-value: 5.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110   1 MVAELTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMR 80
Cdd:PRK09239   8 APAELAALRQSIDNIDAALIHMLAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQLAKDANLDPDFAEKFLNFIIK 87


                 .
gi 489923110  81 E 81
Cdd:PRK09239  88 E 88
PRK07417 PRK07417
prephenate/arogenate dehydrogenase;
137-338 8.52e-05

prephenate/arogenate dehydrogenase;


Pssm-ID: 180970 [Multi-domain]  Cd Length: 279  Bit Score: 43.73  E-value: 8.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 137 PEIVSDAGMVIVSVPIHVTEQVIAKL-PRLPSDCILVDLASVKNGPLQAMLAAHDGpVVGLHPMFG-PDSGSLAKQ---- 210
Cdd:PRK07417  52 LSLLKDCDLVILALPIGLLLPPSEQLiPALPPEAIVTDVGSVKAPIVEAWEKLHPR-FVGSHPMAGtAESGVEAGQrglf 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 211 -----VVVWCDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEEN----VQLEQLLALS 281
Cdd:PRK07417 131 knrpwVLTPTENTDLNALAIVEELAVSLGSKIYTADPEEHDRAVALISHLPVMVSAALIQTCGTEKdpsvLKLAQNLASS 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 282 SpiyrleLAMVGRLFAQDPQLYADiiMSSESNLAL---IKRYYQRFGEAIGLLEQGDKQA 338
Cdd:PRK07417 211 G------FADTSRVGGGNPELGVM--MAEYNRAALlrsLASYRQSLDQLEELIEQENWSA 262
CM-like TIGR01803
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on ...
 5-72 8.54e-05

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: 40.65  E-value: 8.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489923110    5 LTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIE 72
Cdd:TIGR01803   1 LADIREAIDRIDLALVQALGRRMDYVKRASEFKRSHEAAIPAPERVAAVLPNAARWAEENGLDPPFVE 68
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
 1-55 2.55e-04

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


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 42.66  E-value: 2.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489923110   1 MVAELTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLA 55
Cdd:PRK12595   2 MNEELEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLD 56
CM_P2 TIGR01807
chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of ...
 5-79 5.28e-04

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: 38.20  E-value: 5.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489923110    5 LTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRF--GLPIYVPEREASMLasRRAEAEALG-VPPDLIEDVLRRVM 79
Cdd:TIGR01807   1 LEELRNKIDAIDDRILDLLSERATYAQAVGELKGSGasGASFYRPEREAQVI--RRLQNLNKGpLDQEAIARIFREIM 76
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 146-314 1.12e-03

bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 40.84  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 146 VIVSVPIHVTEQVIAKL-PRLPSDCILVDLASVKN---GPLQAMLAAHDGPVVGLHPMFGPDSGSLAKQVVVWCDGRQ-- 219
Cdd:PRK11861   1 VLLAAPVAQTGPLLARIaPFLDASTIVTDAGSTKSdvvAAARAALGARIGQFVPGHPIAGRESSGVDAALADLYVGRNvv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489923110 220 ----PEAYQWFLEQIQ-VWGAR---LHRISAVEHDQNMAFIQALRHFATFAYglhlaeenvqLEQLLALSSPIYRLELAM 291
Cdd:PRK11861  81 lcalPENAPDALARVEaMWRAAradVRAMSAEQHDRVFAAVSHLPHVLSFAL----------VEQILGESDAELKFSYAA 150

                        170       180
                 ....*....|....*....|....*...
gi 489923110 292 VG-----RLFAQDPQLYADIIMSSESNL 314
Cdd:PRK11861 151 GGfrdftRIAASSPEMWRDVCLANRAAL 178
PRK06285 PRK06285
chorismate mutase; Provisional
 4-79 1.20e-03

chorismate mutase; Provisional


Pssm-ID: 180509 [Multi-domain]  Cd Length: 96  Bit Score: 37.71  E-value: 1.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489923110   4 ELTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVM 79
Cdd:PRK06285   8 RLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNIDENIGLKIMKILM 83
CM_mono_grmpos TIGR01805
monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade ...
 5-62 5.98e-03

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: 35.52  E-value: 5.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489923110    5 LTALRDQIDEVDKALLDLLARRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAE 62
Cdd:TIGR01805   1 LELIRKKIDEIDDKLVVLFEERMEVVKEIAAYKKKNGIPIFDSKREQEIIDKCTKNVE 58
PRK07075 PRK07075
isochorismate lyase;
5-73 8.47e-03

isochorismate lyase;


Pssm-ID: 136191 [Multi-domain]  Cd Length: 101  Bit Score: 35.48  E-value: 8.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489923110   5 LTALRDQIDEVDKALLDLLarrlelVAEVGEVK--SRFG---LPIYVPEREASMLASRRAEAEALGVPPDLIED 73
Cdd:PRK07075  10 LDDIREAIDRLDRDIIAAL------GRRMQYVKaaSRFKpseASIPAPERVAAMLPERRRWAEQAGLDADFVEK 77
 
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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