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Conserved domains on  [gi|515652205|ref|WP_017084805|]
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MULTISPECIES: bifunctional chorismate mutase/prephenate dehydrogenase [Vibrio]

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
 1-374 0e+00

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


:

Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 764.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205   1 MAVELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMR 80
Cdd:PRK11199   1 MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRVMR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  81 ESYASEKDSGFKCLNPELRSVVIVGGNGQLGGLFGRMFKLSGYEVKILGSQDWDRADEILDNAGLVVVTVPIHLTEGVIA 160
Cdd:PRK11199  81 ESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDILADAGMVIVSVPIHLTEEVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 161 KLGNLPSDCILCDLTSIKSKPLQAMMNMHQGPVVGLHPMFGPDVPSLAKQVIVYSDGRGSESYQWLLNQFGIWGASLCQM 240
Cdd:PRK11199 161 RLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQVVVVCDGRQPEAYQWLLEQIQVWGARLHRI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 241 DAAEHDHGMTLIQALRHFTSFAYGLHLSKENPNIDQLLKLSSPIYRLEIAMVGRLFAQDPNLYGDIILSSDENIEMIRRF 320
Cdd:PRK11199 241 SAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRY 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515652205 321 HSRFGEALEILDGKDKAKFVDSFNQVSDWFGDYSQQFLQESQNLLKQAHDSIHR 374
Cdd:PRK11199 321 YQRFGEALELLEQGDKQAFIDSFRKVEHWFGDYAEQFLKESRSLLQQANDNRQR 374
 
Name Accession Description Interval E-value
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 1-374 0e+00

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 764.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205   1 MAVELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMR 80
Cdd:PRK11199   1 MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRVMR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  81 ESYASEKDSGFKCLNPELRSVVIVGGNGQLGGLFGRMFKLSGYEVKILGSQDWDRADEILDNAGLVVVTVPIHLTEGVIA 160
Cdd:PRK11199  81 ESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDILADAGMVIVSVPIHLTEEVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 161 KLGNLPSDCILCDLTSIKSKPLQAMMNMHQGPVVGLHPMFGPDVPSLAKQVIVYSDGRGSESYQWLLNQFGIWGASLCQM 240
Cdd:PRK11199 161 RLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQVVVVCDGRQPEAYQWLLEQIQVWGARLHRI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 241 DAAEHDHGMTLIQALRHFTSFAYGLHLSKENPNIDQLLKLSSPIYRLEIAMVGRLFAQDPNLYGDIILSSDENIEMIRRF 320
Cdd:PRK11199 241 SAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRY 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515652205 321 HSRFGEALEILDGKDKAKFVDSFNQVSDWFGDYSQQFLQESQNLLKQAHDSIHR 374
Cdd:PRK11199 321 YQRFGEALELLEQGDKQAFIDSFRKVEHWFGDYAEQFLKESRSLLQQANDNRQR 374
CM_T TIGR01799
chorismate mutase domain of T-protein; This model represents the chorismate mutase domain of ...
 5-87 2.52e-41

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: 140.03  E-value: 2.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205    5 LNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESYA 84
Cdd:TIGR01799   1 LEDLRGEIDGVDQELLHLLAKRLELVAQVGKVKHAAGLPIYAPEREAAMLAARREEAEKAGIAPDLIEDVLRRFMRESYA 80


                  ...
gi 515652205   85 SEK 87
Cdd:TIGR01799  81 NEN 83
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 4-166 4.93e-38

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: 134.12  E-value: 4.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205   4 ELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESY 83
Cdd:COG1605    6 SLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISESI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  84 ASEKdsgfKCLNPELRSVVIVGGNGQLGGLFGRMFKLSGYEVKILGSQDWDRADEILDNAGLVVVTVPIHLTEGVIAKLG 163
Cdd:COG1605   86 ALQE----KLLAEVAYLGPEGGFTGQAAGKHFGGSAASLPAAAIDEVFREVEAGGAAYGVVPVENSTEGGVVETLDLLLA 161


                 ...
gi 515652205 164 NLP 166
Cdd:COG1605  162 SPL 164
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 9-87 1.12e-28

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: 106.42  E-value: 1.12e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515652205    9 RDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESYASEK 87
Cdd:pfam01817   1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 9-87 4.26e-26

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: 99.58  E-value: 4.26e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515652205     9 RDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESYASEK 87
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
 
Name Accession Description Interval E-value
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 1-374 0e+00

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 764.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205   1 MAVELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMR 80
Cdd:PRK11199   1 MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRVMR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  81 ESYASEKDSGFKCLNPELRSVVIVGGNGQLGGLFGRMFKLSGYEVKILGSQDWDRADEILDNAGLVVVTVPIHLTEGVIA 160
Cdd:PRK11199  81 ESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDILADAGMVIVSVPIHLTEEVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 161 KLGNLPSDCILCDLTSIKSKPLQAMMNMHQGPVVGLHPMFGPDVPSLAKQVIVYSDGRGSESYQWLLNQFGIWGASLCQM 240
Cdd:PRK11199 161 RLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQVVVVCDGRQPEAYQWLLEQIQVWGARLHRI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 241 DAAEHDHGMTLIQALRHFTSFAYGLHLSKENPNIDQLLKLSSPIYRLEIAMVGRLFAQDPNLYGDIILSSDENIEMIRRF 320
Cdd:PRK11199 241 SAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRY 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515652205 321 HSRFGEALEILDGKDKAKFVDSFNQVSDWFGDYSQQFLQESQNLLKQAHDSIHR 374
Cdd:PRK11199 321 YQRFGEALELLEQGDKQAFIDSFRKVEHWFGDYAEQFLKESRSLLQQANDNRQR 374
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 100-352 1.14e-44

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 159.38  E-value: 1.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 100 SVVIVGGNGQLGGLFGRMFKLSGYEVKI--------------LGSQDWDRADEILDNAGLVVVTVPIHLTEGVIAKLG-N 164
Cdd:PRK08655   2 KISIIGGTGGLGKWFARFLKEKGFEVIVtgrdpkkgkevakeLGVEYANDNIDAAKDADIVIISVPINVTEDVIKEVApH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 165 LPSDCILCDLTSIKSKPLQAMMNM--HQGPVVGLHPMFGPDVPSLAKQVIVYSDGRGSES------YQWLLNQfgiwGAS 236
Cdd:PRK08655  82 VKEGSLLMDVTSVKERPVEAMEEYapEGVEILPTHPMFGPRTPSLKGQVVILTPTEKRSNpwfdkvKNFLEKE----GAR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 237 LCQMDAAEHDHGMTLIQALRHFTSFAYGLHLSKENPNIDQLLKLSSPIYRLEIAMVGRLFAQDPNLYGDIILSSDENIEM 316
Cdd:PRK08655 158 VIVTSPEEHDRIMSVVQGLTHFAYISIASTLKRLGVDIKESRKFASPIYELMIDIIGRILGQNPYLYASIQMNNPQIPEI 237

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 515652205 317 IRRFHSRFGEALEILDGKDKAKFVDSFNQVSDWFGD 352
Cdd:PRK08655 238 HETFIKECEELSELVKNGDREEFVERMKEAAKHFGD 273
CM_T TIGR01799
chorismate mutase domain of T-protein; This model represents the chorismate mutase domain of ...
 5-87 2.52e-41

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: 140.03  E-value: 2.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205    5 LNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESYA 84
Cdd:TIGR01799   1 LEDLRGEIDGVDQELLHLLAKRLELVAQVGKVKHAAGLPIYAPEREAAMLAARREEAEKAGIAPDLIEDVLRRFMRESYA 80


                  ...
gi 515652205   85 SEK 87
Cdd:TIGR01799  81 NEN 83
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 4-166 4.93e-38

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: 134.12  E-value: 4.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205   4 ELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESY 83
Cdd:COG1605    6 SLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISESI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  84 ASEKdsgfKCLNPELRSVVIVGGNGQLGGLFGRMFKLSGYEVKILGSQDWDRADEILDNAGLVVVTVPIHLTEGVIAKLG 163
Cdd:COG1605   86 ALQE----KLLAEVAYLGPEGGFTGQAAGKHFGGSAASLPAAAIDEVFREVEAGGAAYGVVPVENSTEGGVVETLDLLLA 161


                 ...
gi 515652205 164 NLP 166
Cdd:COG1605  162 SPL 164
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 9-87 1.12e-28

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: 106.42  E-value: 1.12e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515652205    9 RDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESYASEK 87
Cdd:pfam01817   1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 9-87 4.26e-26

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: 99.58  E-value: 4.26e-26
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515652205     9 RDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESYASEK 87
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
PRK08818 PRK08818
prephenate dehydrogenase; Provisional
 99-375 1.19e-18

prephenate dehydrogenase; Provisional


Pssm-ID: 181561 [Multi-domain]  Cd Length: 370  Bit Score: 86.46  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  99 RSVVIVGGNGQLGGLFGRMFKlSGYEVKILGSQDWDRA----DEILDNAGLVVVTVPIHLTEGVIAKL----GNLPSDCI 170
Cdd:PRK08818   5 PVVGIVGSAGAYGRWLARFLR-TRMQLEVIGHDPADPGsldpATLLQRADVLIFSAPIRHTAALIEEYvalaGGRAAGQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 171 LCDLTSIKSKPLQAMMnMHQGPVVGLHPMFG-PDVPSLAKQVIVYSDGRgsesyqwlLNQFGIWGASLCQMDAAE----- 244
Cdd:PRK08818  84 WLDVTSIKQAPVAAML-ASQAEVVGLHPMTApPKSPTLKGRVMVVCEAR--------LQHWSPWVQSLCSALQAEcvyat 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 245 ---HDHGMTLIQALRHFTSFAYGLHLSKENPNIDQLLKL---SSPIYRLEIAMVGRLFAQDPNLYGDIILSSDENIEMIR 318
Cdd:PRK08818 155 pehHDRVMALVQAMVHATHLAQAGVLRDYAPLLGELRALmpyRSASFELDTAVIARILSLNPSIYEDIQFGNPYVGEMLD 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515652205 319 RFHSRFGE-ALEILDGKDKAKfvdsfnqvsdwfGDYSQQFLQESQNLLKqaHDSIHRG 375
Cdd:PRK08818 235 RLLAQLQElRALVAQGDDAAR------------ARFRAQFLHANAQALQ--EDALAAG 278
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 98-345 1.98e-18

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: 84.41  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  98 LRSVVIVGgNGQLGGLFGRMFKLSGYEVKILGsqdWDR--------------------ADEILDNAGLVVVTVPIHLTEG 157
Cdd:COG0287    1 FMRIAIIG-LGLIGGSLALALKRAGLAHEVVG---VDRspetleralelgvidraatdLEEAVADADLVVLAVPVGATIE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 158 VIAKL-GNLPSDCILCDLTSIKSKPLQAMMNMHQGPV--VGLHPMFGPDV-------PSL---AKQVIVYSDGRGSESYQ 224
Cdd:COG0287   77 VLAELaPHLKPGAIVTDVGSVKGAVVEAAEALLPDGVrfVGGHPMAGTEKsgpeaadADLfegAPYILTPTEGTDPEALE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 225 WLLNqfgIW---GASLCQMDAAEHDHGMTLIQALRHFTSFAYGLHLSKEnPNIDQLLKLSSPIYRleiAMVgRLFAQDPN 301
Cdd:COG0287  157 RVEE---LWealGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADL-EDEEEILRLAAGGFR---DTT-RIAASDPE 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 515652205 302 LYGDIILSSDENI-EMIRRFHSRFGEALEILDGKDKAKFVDSFNQ 345
Cdd:COG0287  229 MWRDIFLANREALlEALDRFIEELDALRDALEAGDGEALEELLER 273
CM_archaeal TIGR01791
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ...
 5-82 2.60e-13

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: 64.76  E-value: 2.60e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515652205    5 LNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRES 82
Cdd:TIGR01791   1 IEELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEIFEILMSLS 78
CM-like TIGR01803
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on ...
 5-81 7.10e-13

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: 63.77  E-value: 7.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205    5 LNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIE----DILRRTMR 80
Cdd:TIGR01803   1 LADIREAIDRIDLALVQALGRRMDYVKRASEFKRSHEAAIPAPERVAAVLPNAARWAEENGLDPPFVEglfaQIIHWYIA 80


                  .
gi 515652205   81 E 81
Cdd:TIGR01803  81 E 81
PRK07248 PRK07248
chorismate mutase;
4-78 1.70e-12

chorismate mutase;


Pssm-ID: 168880 [Multi-domain]  Cd Length: 87  Bit Score: 62.77  E-value: 1.70e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515652205   4 ELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIE---DILRRT 78
Cdd:PRK07248   2 DLEEIRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDKVSSLVENKAYQETIVAtfkDIMKRS 79
CM_P2 TIGR01807
chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of ...
 5-79 1.85e-12

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: 62.08  E-value: 1.85e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515652205    5 LNELRDQIDAVDKQMLDLLAQRLALVEKVGEVK--SEHGLPIYVPEREAAMLaSRRQEAEKIGVPPQLIEDILRRTM 79
Cdd:TIGR01807   1 LEELRNKIDAIDDRILDLLSERATYAQAVGELKgsGASGASFYRPEREAQVI-RRLQNLNKGPLDQEAIARIFREIM 76
PRK06285 PRK06285
chorismate mutase; Provisional
 4-89 1.46e-11

chorismate mutase; Provisional


Pssm-ID: 180509 [Multi-domain]  Cd Length: 96  Bit Score: 60.43  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205   4 ELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESY 83
Cdd:PRK06285   8 RLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNIDENIGLKIMKILMEHSK 87


                 ....*.
gi 515652205  84 ASEKDS 89
Cdd:PRK06285  88 ELQKEY 93
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
 1-55 3.04e-11

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


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 64.23  E-value: 3.04e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515652205   1 MAVELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLA 55
Cdd:PRK12595   2 MNEELEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLD 56
PRK07075 PRK07075
isochorismate lyase;
5-74 5.23e-11

isochorismate lyase;


Pssm-ID: 136191 [Multi-domain]  Cd Length: 101  Bit Score: 58.98  E-value: 5.23e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515652205   5 LNELRDQIDAVDKQMLDLLAQRLALVEKVGEVK-SEHGLPiyVPEREAAMLASRRQEAEKIGVPPQLIEDI 74
Cdd:PRK07075  10 LDDIREAIDRLDRDIIAALGRRMQYVKAASRFKpSEASIP--APERVAAMLPERRRWAEQAGLDADFVEKL 78
PRK08507 PRK08507
prephenate dehydrogenase; Validated
 101-335 8.11e-10

prephenate dehydrogenase; Validated


Pssm-ID: 181452 [Multi-domain]  Cd Length: 275  Bit Score: 59.14  E-value: 8.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 101 VVIVGgNGQLGGLFGRMFKLSGYEVKILG----------SQDWDRADEILD-----NAGLVVVTVPIHLTEGVIAKLGNL 165
Cdd:PRK08507   3 IGIIG-LGLMGGSLGLALKEKGLISKVYGydhnelhlkkALELGLVDEIVSfeelkKCDVIFLAIPVDAIIEILPKLLDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 166 PSDCILCDLTSIKSKPLQAMMNMHQGPVVGLHPM-----FGPD--VPSLAK-QVIVYSDGRGSESYQW--LLNQFGIWGA 235
Cdd:PRK08507  82 KENTTIIDLGSTKAKIIESVPKHIRKNFIAAHPMagtenSGPKaaIKGLYEgKVVVLCDVEKSGEKHQerAKEIFSGLGM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 236 SLCQMDAAEHDHGMTLIQALRHFTSFAYGLH-LSKENPNidQLLKLSSPIYRleiAMVgRLFAQDPNLYGDIILSSDENI 314
Cdd:PRK08507 162 RIVYMDAKEHDLHAAYISHLPHIISFALANTvLKEEDER--NIFDLAGGGFR---SMS-RLAKSSPAMWSDIFKQNKENV 235

                        250       260
                 ....*....|....*....|..
gi 515652205 315 -EMIRRFHSRFGEALEILDGKD 335
Cdd:PRK08507 236 lEAIDEFIKELEQFKQLIENED 257
PDH_C pfam20463
Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate ...
 241-345 1.06e-09

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: 55.08  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  241 DAAEHDHGMTLIQALRHFTSFAYGLHLSKENPNIDQLLKLSSPIYRLEIamvgRLFAQDPNLYGDIILSSDENI-EMIRR 319
Cdd:pfam20463   1 SPETHDRVVAVVSHLPHFVAIALAATLAELGVDIKEARKLASGGFRDMT----RIAGSNPELWADIQTHNARAVlEALDD 76

                          90       100
                  ....*....|....*....|....*.
gi 515652205  320 FHSRFGEALEILDGKDKAKFVDSFNQ 345
Cdd:pfam20463  77 FIAELKQLKELIRNGDWEELVEYMKE 102
PRK09239 PRK09239
chorismate mutase; Provisional
 4-81 4.82e-09

chorismate mutase; Provisional


Pssm-ID: 181719 [Multi-domain]  Cd Length: 104  Bit Score: 53.49  E-value: 4.82e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515652205   4 ELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRE 81
Cdd:PRK09239  11 ELAALRQSIDNIDAALIHMLAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQLAKDANLDPDFAEKFLNFIIKE 88
CM_mono_grmpos TIGR01805
monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade ...
 5-62 1.44e-08

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: 51.31  E-value: 1.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 515652205    5 LNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAE 62
Cdd:TIGR01805   1 LELIRKKIDEIDDKLVVLFEERMEVVKEIAAYKKKNGIPIFDSKREQEIIDKCTKNVE 58
PDH_N pfam02153
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ...
 143-202 1.98e-07

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: 50.08  E-value: 1.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515652205  143 AGLVVVTVPIHLTEGVIAKLG-NLPSDCILCDLTSIKSKPLQAM-MNMHQGPVVGLHPMFGP 202
Cdd:pfam02153  46 ADIVFLAVPVEQTLPVLKELApHLKEDALITDVGSVKVKIIRELeQHLPDKSFVPGHPMAGT 107
CM_P_1 TIGR01797
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ...
 5-87 6.39e-07

chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the chorismate mutase domain of the gamma and beta proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130856 [Multi-domain]  Cd Length: 83  Bit Score: 46.73  E-value: 6.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205    5 LNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESYA 84
Cdd:TIGR01797   1 LLALREKISAIDEKLLKLLAERRELAFEVGKSKLLSHRPVRDIERERDLLQRLITLGKAYHLDAHYITRLFQLIIEDSVL 80


                  ...
gi 515652205   85 SEK 87
Cdd:TIGR01797  81 TQQ 83
PRK09269 PRK09269
chorismate mutase; Provisional
 18-68 1.09e-06

chorismate mutase; Provisional


Pssm-ID: 236441  Cd Length: 193  Bit Score: 48.44  E-value: 1.09e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515652205  18 QMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPP 68
Cdd:PRK09269  36 PLVDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAPAHGVDP 86
PRK06545 PRK06545
prephenate dehydrogenase; Validated
 99-247 3.90e-06

prephenate dehydrogenase; Validated


Pssm-ID: 235824 [Multi-domain]  Cd Length: 359  Bit Score: 48.36  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  99 RSVVIVGgNGQLGGLFGRMFKLSGYEVKILgsqDWDRADEILD--------------------NAGLVVVTVPIHLTEGV 158
Cdd:PRK06545   1 RTVLIVG-LGLIGGSLALAIKAAGPDVFII---GYDPSAAQLAralgfgvidelaadlqraaaEADLIVLAVPVDATAAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 159 IAKLGN--LPSDCILCDLTSIKSKPLQA--MMNMHQGPVVGLHPMFG----------PDVPSLAKQVIVYSDGRGSESYQ 224
Cdd:PRK06545  77 LAELADleLKPGVIVTDVGSVKGAILAEaeALLGDLIRFVGGHPMAGshksgvaaarADLFENAPWVLTPDDHTDPDAVA 156

                        170       180
                 ....*....|....*....|...
gi 515652205 225 WLLNQFGIWGASLCQMDAAEHDH 247
Cdd:PRK06545 157 ELKDLLSGTGAKFVVLDAEEHDR 179
CM_mono2 TIGR01806
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ...
 18-87 5.24e-06

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: 45.11  E-value: 5.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205   18 QMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESYASEK 87
Cdd:TIGR01806   8 QLVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQINANKAIQY 77
PRK06034 PRK06034
hypothetical protein; Provisional
 5-79 6.65e-06

hypothetical protein; Provisional


Pssm-ID: 235680 [Multi-domain]  Cd Length: 279  Bit Score: 47.40  E-value: 6.65e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515652205   5 LNELRDQIDAVDKQMLDLLAQRLALVEKVGEVK--SEHGLPiYVPEREAAMLasRR-QEAEKIGVPPQLIEDILRRTM 79
Cdd:PRK06034  11 LAELRWEIDAIDEELHQLLMERGDIIDRLIAVKrtQEVGSA-FRPGREADMM--RRlVSRHRGILPLDTVESIWRVII 85
pheA PRK10622
bifunctional chorismate mutase/prephenate dehydratase; Provisional
 8-54 1.36e-05

bifunctional chorismate mutase/prephenate dehydratase; Provisional


Pssm-ID: 182594 [Multi-domain]  Cd Length: 386  Bit Score: 46.65  E-value: 1.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 515652205   8 LRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAML 54
Cdd:PRK10622  10 LREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLL 56
PRK08055 PRK08055
chorismate mutase; Provisional
 13-84 1.78e-05

chorismate mutase; Provisional


Pssm-ID: 236143  Cd Length: 181  Bit Score: 44.68  E-value: 1.78e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515652205  13 DAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGVPPQLIEDILRRTMRESYA 84
Cdd:PRK08055  24 AVSLGALATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLDPESIKPFIVAQMDAAKA 95
PRK07857 PRK07857
chorismate mutase;
2-66 5.04e-05

chorismate mutase;


Pssm-ID: 236117  Cd Length: 106  Bit Score: 41.99  E-value: 5.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515652205   2 AVELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAMLASRRQEAEKIGV 66
Cdd:PRK07857  27 DAEIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIERYREELGPEGK 91
PRK06444 PRK06444
prephenate dehydrogenase; Provisional
 101-260 3.95e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 102381 [Multi-domain]  Cd Length: 197  Bit Score: 40.99  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 101 VVIVGGNGQLGGLFGRMFKLSGYEVKIlgsqdwdradeilDNAGLVVVTVPIHLTEGVIAKlgnlpSDCILCDLTSIKSk 180
Cdd:PRK06444   3 EIIIGKNGRLGRVLCSILDDNGLGVYI-------------KKADHAFLSVPIDAALNYIES-----YDNNFVEISSVKW- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 181 PLQAmmnmHQGPVVGLHPMFGPDV--PSLAKQVIVYSDGRGSESYQWLLNQFGIWgaSLCQMDAAEHDHGMTLIQALRHF 258
Cdd:PRK06444  64 PFKK----YSGKIVSIHPLFGPMSynDGVHRTVIFINDISRDNYLNEINEMFRGY--HFVEMTADEHDLLMSEIMVKPYI 137


                 ..
gi 515652205 259 TS 260
Cdd:PRK06444 138 IS 139
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 96-314 4.04e-04

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 42.29  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  96 PELRSVVIVGgNGQLGGLFGRMFKLSGYEVKILGSqdwDRADEILDNA--------------------GLVVVTVPIHLT 155
Cdd:PRK14806   1 PLFGRVVVIG-LGLIGGSFAKALRERGLAREVVAV---DRRAKSLELAvslgvidrgeedlaeavsgaDVIVLAVPVLAM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 156 EGVIAKLGNLPS-DCILCDLTSIKSKPLQAMMNMHQG-P--VVGLHPMFGPDVPS-LAKQVIVYSDGRG-----SESYQW 225
Cdd:PRK14806  77 EKVLADLKPLLSeHAIVTDVGSTKGNVVDAARAVFGElPagFVPGHPIAGSEKSGvHAANADLFRNHKViltplAETDPA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 226 LLNQF-GIW---GASLCQMDAAEHDHGMTLIQALRHFTSFAYGLHLSKENPNIDqllklsspIYRLeiAMVG-----RLF 296
Cdd:PRK14806 157 ALARVdRLWravGADVLHMDVAHHDEVLAATSHLPHLLAFSLVDQLANREDNLD--------IFRY--AAGGfrdftRIA 226

                        250
                 ....*....|....*...
gi 515652205 297 AQDPNLYGDIILSSDENI 314
Cdd:PRK14806 227 ASDPVMWHDIFLANKEAV 244
PLN02712 PLN02712
arogenate dehydrogenase
 93-329 7.39e-04

arogenate dehydrogenase


Pssm-ID: 215382 [Multi-domain]  Cd Length: 667  Bit Score: 41.51  E-value: 7.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205  93 CLNPELRSVVIVGGNGQLGGLFGRMFKLSGYEV------------KILGSQDWDRADEILD-NAGLVVVTVPIHLTEGVI 159
Cdd:PLN02712 363 CVNDGSKLKIAIVGFGNFGQFLAKTMVKQGHTVlaysrsdysdeaQKLGVSYFSDADDLCEeHPEVILLCTSILSTEKVL 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 160 AKL--GNLPSDCILCDLTSIKSKPlQAMMNMHQGP---VVGLHPMFGPD--------VPSLAKQVIVYSDGRGSESYQWL 226
Cdd:PLN02712 443 KSLpfQRLKRSTLFVDVLSVKEFP-RNLFLQHLPQdfdILCTHPMFGPEsgkngwnnLAFVFDKVRIGSDDRRVSRCDSF 521

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 227 LNQFGIWGASLCQMDAAEHD-HGmtliqALRHFTSFAYGLHLSKenpnidqLLKLSSPI----YRLEIAMVGRLFAQDPN 301
Cdd:PLN02712 522 LDIFAREGCRMVEMSCAEHDwHA-----AGSQFITHTMGRLLEK-------LGLESTPIntkgYETLLNLVENTAGDSFD 589

                        250       260
                 ....*....|....*....|....*...
gi 515652205 302 LYGDIILSSDENIEMIRRFHSRFgEALE 329
Cdd:PLN02712 590 LYYGLFMYNVNAMEQLERLDLAF-ESLK 616
PLN02256 PLN02256
arogenate dehydrogenase
 146-312 1.61e-03

arogenate dehydrogenase


Pssm-ID: 215144 [Multi-domain]  Cd Length: 304  Bit Score: 40.03  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 146 VVVTVPIHLTEGVIAKLG--NLPSDCILCDLTSIKSKPLQAMMNM--HQGPVVGLHPMFGPD--------VPSLAKQVIV 213
Cdd:PLN02256  96 VLLCTSILSTEAVLRSLPlqRLKRSTLFVDVLSVKEFPKNLLLQVlpEEFDILCTHPMFGPEsgkggwagLPFVYDKVRI 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515652205 214 YSDGRGSESYQWLLNQFGIWGASLCQMDAAEHD----------HGM--------------------TLIQALRHFT--SF 261
Cdd:PLN02256 176 GDEGEREARCERFLDIFEEEGCRMVEMSCEEHDryaagsqfitHTVgrilgkmelestpintkgyeTLLRLVENTSsdSF 255

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515652205 262 A--YGLHlsKENPNIDQLLKlsspiyRLEIAM---VGRLFAQDPNLYGDIILSSDE 312
Cdd:PLN02256 256 DlyYGLF--MYNPNATEELE------RLELAFdsvKKQLFGRLHDVLRKQLFEGSP 303
PRK06443 PRK06443
chorismate mutase; Validated
 3-53 2.41e-03

chorismate mutase; Validated


Pssm-ID: 235801  Cd Length: 177  Bit Score: 38.35  E-value: 2.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515652205   3 VELNELRDQIDAVDKQMLDLLAQRLALVEKVGEVKSEHGLPIYVPEREAAM 53
Cdd:PRK06443   5 IDMEDLRSEILENTMDIIELIEKRRELARMIGIIKMRNGLSIRDSERENYV 55
 
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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