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Conserved domains on  [gi|15832716|ref|NP_311489|]
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chorismate mutase and prephenate dehydratase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

bifunctional chorismate mutase/prephenate dehydratase( domain architecture ID 11484831)

bifunctional chorismate mutase/prephenate dehydratase catalyzes the formation of prephenate from chorismate and the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pheA PRK10622
bifunctional chorismate mutase/prephenate dehydratase; Provisional
 1-386 0e+00

bifunctional chorismate mutase/prephenate dehydratase; Provisional


:

Pssm-ID: 182594 [Multi-domain]  Cd Length: 386  Bit Score: 820.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716    1 MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80
Cdd:PRK10622   1 MTSENPLLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716   81 IEDSVLTQQALLQQHLNKINPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVVPIEN 160
Cdd:PRK10622  81 IEDSVLTQQALLQQHLNKTNPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVLPIEN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  161 TSSGAINDVYDLLQHTSLSIVGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEK 240
Cdd:PRK10622 161 TSSGAINDVYDLLQHTSLSIVGEMTLPIDHCVLVSGTTDLSTIETVYSHPQPFQQCSQFLNRYPHWKIEYTESTAAAMEK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  241 VAQAKSPHVAALGSEAGGTLYGLQVLERIEANQRQNFTRFVVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN 320
Cdd:PRK10622 241 VAQANSPHVAALGSEAGGALYGLQVLERNLANQQQNITRFIVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832716  321 HNLIMTRLESRPIHGNPWEEMFYLDIQANLESAEMQKALKELGEITRSMKVLGCYPSENVVPVDPT 386
Cdd:PRK10622 321 HNLIMTKLESRPIHGNPWEEMFYLDVQANLRSAEMQKALKELGEITRSLKVLGCYPSENVVPVDPT 386
 
Name Accession Description Interval E-value
pheA PRK10622
bifunctional chorismate mutase/prephenate dehydratase; Provisional
 1-386 0e+00

bifunctional chorismate mutase/prephenate dehydratase; Provisional


Pssm-ID: 182594 [Multi-domain]  Cd Length: 386  Bit Score: 820.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716    1 MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80
Cdd:PRK10622   1 MTSENPLLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716   81 IEDSVLTQQALLQQHLNKINPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVVPIEN 160
Cdd:PRK10622  81 IEDSVLTQQALLQQHLNKTNPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVLPIEN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  161 TSSGAINDVYDLLQHTSLSIVGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEK 240
Cdd:PRK10622 161 TSSGAINDVYDLLQHTSLSIVGEMTLPIDHCVLVSGTTDLSTIETVYSHPQPFQQCSQFLNRYPHWKIEYTESTAAAMEK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  241 VAQAKSPHVAALGSEAGGTLYGLQVLERIEANQRQNFTRFVVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN 320
Cdd:PRK10622 241 VAQANSPHVAALGSEAGGALYGLQVLERNLANQQQNITRFIVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832716  321 HNLIMTRLESRPIHGNPWEEMFYLDIQANLESAEMQKALKELGEITRSMKVLGCYPSENVVPVDPT 386
Cdd:PRK10622 321 HNLIMTKLESRPIHGNPWEEMFYLDVQANLRSAEMQKALKELGEITRSLKVLGCYPSENVVPVDPT 386
PheA2 COG0077
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ...
 103-380 7.76e-129

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


Pssm-ID: 439847 [Multi-domain]  Cd Length: 274  Bit Score: 370.97  E-value: 7.76e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 103 SARIAFLGPKGSYSHLAARQYAARHFEqfiESGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVG 182
Cdd:COG0077   1 MMRIAYLGPEGTFSHQAARKYFGPDAE---LVPCPSFEDVFEAVESGEADYGVVPIENSIEGSVNETLDLLLESDLKIVG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 183 EMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRY-PHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLY 261
Cdd:COG0077  78 EVVLPIHHCLLARPGTKLEDIKTVYSHPQALAQCREFLREHlPGAELVPVSSTAAAARLVAEEGDPGAAAIASELAAELY 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 262 GLQVLER-IEaNQRQNFTRFVVLARKaiNVSDQVPAKTTLLMATGQQAGALVEALLVLRNHNLIMTRLESRPIHGNPWEE 340
Cdd:COG0077 158 GLEVLAEnIE-DNPNNTTRFLVLGRE--PAAPTGADKTSLVFSLPNRPGALYKALGVFATRGINLTKIESRPIKGGLWEY 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15832716 341 MFYLDIQANLESAEMQKALKELGEITRSMKVLGCYPSENV 380
Cdd:COG0077 235 VFFIDVEGHIDDPRVAEALEELKRLTEFLKILGSYPRADL 274
PBP2_Ct-PDT_like cd13631
Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, ...
 103-287 1.51e-90

Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, subgroup 2; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270349 [Multi-domain]  Cd Length: 182  Bit Score: 270.05  E-value: 1.51e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 103 SARIAFLGPKGSYSHLAARQYaarhFEQFIESGCAK-FADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIV 181
Cdd:cd13631   1 MKRVAYQGVPGAYSHLAARKY----FGEDEEVPCCKtFEDVFEAVESGEADYGVLPIENSSAGSINEVYDLLLEYDLYIV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 182 GEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLY 261
Cdd:cd13631  77 GEIFLPIEHCLLALPGAKLEDIKEVYSHPQALAQCSKFLKKHPGIKLVPYYDTAGAAKKVAEEGDKTVAAIASELAAELY 156

                       170       180
                ....*....|....*....|....*.
gi 15832716 262 GLQVLERIEANQRQNFTRFVVLARKA 287
Cdd:cd13631 157 GLEILAENIQDNKNNYTRFLILSRKP 182
PDT pfam00800
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ...
 106-286 7.08e-79

Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein catalyzes the decarboxylation of prephenate to phenylpyruvate.


Pssm-ID: 425875 [Multi-domain]  Cd Length: 181  Bit Score: 240.52  E-value: 7.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716   106 IAFLGPKGSYSHLAARQYAARHFEqFIEsgCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEMT 185
Cdd:pfam00800   1 IAYLGPPGTFSHQAALKYFGEDAE-LVP--CPSIEDVFEAVENGEADYGVVPIENSLEGSVNETLDLLLKSDLKIVGEVY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716   186 LTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNR-YPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLYGLQ 264
Cdd:pfam00800  78 LPIHHCLLARPGTDLEDIKTVYSHPQALAQCREFLEEhLPGVERVPVSSTAEAAKKVAAEGDPGAAAIASERAAELYGLK 157

                         170       180
                  ....*....|....*....|...
gi 15832716   265 VL-ERIEaNQRQNFTRFVVLARK 286
Cdd:pfam00800 158 VLaENIE-DNPNNTTRFLVLGKE 179
CM_P_1 TIGR01797
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ...
 7-89 1.33e-41

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: 141.11  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716     7 LLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVL 86
Cdd:TIGR01797   1 LLALREKISAIDEKLLKLLAERRELAFEVGKSKLLSHRPVRDIERERDLLQRLITLGKAYHLDAHYITRLFQLIIEDSVL 80


                  ...
gi 15832716    87 TQQ 89
Cdd:TIGR01797  81 TQQ 83
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 11-89 4.03e-21

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: 86.48  E-value: 4.03e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832716     11 REKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQ 89
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
 
Name Accession Description Interval E-value
pheA PRK10622
bifunctional chorismate mutase/prephenate dehydratase; Provisional
 1-386 0e+00

bifunctional chorismate mutase/prephenate dehydratase; Provisional


Pssm-ID: 182594 [Multi-domain]  Cd Length: 386  Bit Score: 820.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716    1 MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80
Cdd:PRK10622   1 MTSENPLLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716   81 IEDSVLTQQALLQQHLNKINPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVVPIEN 160
Cdd:PRK10622  81 IEDSVLTQQALLQQHLNKTNPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVLPIEN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  161 TSSGAINDVYDLLQHTSLSIVGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEK 240
Cdd:PRK10622 161 TSSGAINDVYDLLQHTSLSIVGEMTLPIDHCVLVSGTTDLSTIETVYSHPQPFQQCSQFLNRYPHWKIEYTESTAAAMEK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  241 VAQAKSPHVAALGSEAGGTLYGLQVLERIEANQRQNFTRFVVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN 320
Cdd:PRK10622 241 VAQANSPHVAALGSEAGGALYGLQVLERNLANQQQNITRFIVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832716  321 HNLIMTRLESRPIHGNPWEEMFYLDIQANLESAEMQKALKELGEITRSMKVLGCYPSENVVPVDPT 386
Cdd:PRK10622 321 HNLIMTKLESRPIHGNPWEEMFYLDVQANLRSAEMQKALKELGEITRSLKVLGCYPSENVVPVDPT 386
PheA2 COG0077
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ...
 103-380 7.76e-129

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


Pssm-ID: 439847 [Multi-domain]  Cd Length: 274  Bit Score: 370.97  E-value: 7.76e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 103 SARIAFLGPKGSYSHLAARQYAARHFEqfiESGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVG 182
Cdd:COG0077   1 MMRIAYLGPEGTFSHQAARKYFGPDAE---LVPCPSFEDVFEAVESGEADYGVVPIENSIEGSVNETLDLLLESDLKIVG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 183 EMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRY-PHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLY 261
Cdd:COG0077  78 EVVLPIHHCLLARPGTKLEDIKTVYSHPQALAQCREFLREHlPGAELVPVSSTAAAARLVAEEGDPGAAAIASELAAELY 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 262 GLQVLER-IEaNQRQNFTRFVVLARKaiNVSDQVPAKTTLLMATGQQAGALVEALLVLRNHNLIMTRLESRPIHGNPWEE 340
Cdd:COG0077 158 GLEVLAEnIE-DNPNNTTRFLVLGRE--PAAPTGADKTSLVFSLPNRPGALYKALGVFATRGINLTKIESRPIKGGLWEY 234

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15832716 341 MFYLDIQANLESAEMQKALKELGEITRSMKVLGCYPSENV 380
Cdd:COG0077 235 VFFIDVEGHIDDPRVAEALEELKRLTEFLKILGSYPRADL 274
PBP2_Ct-PDT_like cd13631
Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, ...
 103-287 1.51e-90

Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, subgroup 2; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270349 [Multi-domain]  Cd Length: 182  Bit Score: 270.05  E-value: 1.51e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 103 SARIAFLGPKGSYSHLAARQYaarhFEQFIESGCAK-FADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIV 181
Cdd:cd13631   1 MKRVAYQGVPGAYSHLAARKY----FGEDEEVPCCKtFEDVFEAVESGEADYGVLPIENSSAGSINEVYDLLLEYDLYIV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 182 GEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLY 261
Cdd:cd13631  77 GEIFLPIEHCLLALPGAKLEDIKEVYSHPQALAQCSKFLKKHPGIKLVPYYDTAGAAKKVAEEGDKTVAAIASELAAELY 156

                       170       180
                ....*....|....*....|....*.
gi 15832716 262 GLQVLERIEANQRQNFTRFVVLARKA 287
Cdd:cd13631 157 GLEILAENIQDNKNNYTRFLILSRKP 182
PDT pfam00800
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ...
 106-286 7.08e-79

Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein catalyzes the decarboxylation of prephenate to phenylpyruvate.


Pssm-ID: 425875 [Multi-domain]  Cd Length: 181  Bit Score: 240.52  E-value: 7.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716   106 IAFLGPKGSYSHLAARQYAARHFEqFIEsgCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEMT 185
Cdd:pfam00800   1 IAYLGPPGTFSHQAALKYFGEDAE-LVP--CPSIEDVFEAVENGEADYGVVPIENSLEGSVNETLDLLLKSDLKIVGEVY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716   186 LTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNR-YPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLYGLQ 264
Cdd:pfam00800  78 LPIHHCLLARPGTDLEDIKTVYSHPQALAQCREFLEEhLPGVERVPVSSTAEAAKKVAAEGDPGAAAIASERAAELYGLK 157

                         170       180
                  ....*....|....*....|...
gi 15832716   265 VL-ERIEaNQRQNFTRFVVLARK 286
Cdd:pfam00800 158 VLaENIE-DNPNNTTRFLVLGKE 179
PBP2_PDT_like cd13532
Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic ...
 105-286 5.75e-72

Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270250 [Multi-domain]  Cd Length: 184  Bit Score: 222.79  E-value: 5.75e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 105 RIAFLGPKGSYSHLAARQYAArHFEQFIEsgCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLL-QHTSLSIVGE 183
Cdd:cd13532   3 KVAYLGPEGTYSHQAALQLFG-DSVELLP--LPSISDVFEAVESGEADYGVVPIENSTEGSVVETLDLLrDRPDVKIVGE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 184 MTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRY-PHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLYG 262
Cdd:cd13532  80 VYLPIHHCLLGRPGADLSEIKRVYSHPQALGQCRNFLSEHlPGAERIDVSSTAEAAELVAEDPSGTAAAIASELAAELYG 159

                       170       180
                ....*....|....*....|....
gi 15832716 263 LQVLERIEANQRQNFTRFVVLARK 286
Cdd:cd13532 160 LEILAENIQDEKDNTTRFLVLGRR 183
PRK11898 PRK11898
prephenate dehydratase; Provisional
 103-377 8.39e-69

prephenate dehydratase; Provisional


Pssm-ID: 237013 [Multi-domain]  Cd Length: 283  Bit Score: 218.15  E-value: 8.39e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  103 SARIAFLGPKGSYSHLAARQYAARHFEQFIESgCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLL-QHTSLSIV 181
Cdd:PRK11898   1 MMKIAYLGPEGTFTEAAALKFFPADGEAELVP-YDSIPDVLDAVEAGEVDYAVVPIENSIEGSVNPTLDYLaHGSPLQIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  182 GEMTLTIDHCLLVSgTTDLSTINTVYSHPQPFQQCSKFLNR-YPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTL 260
Cdd:PRK11898  80 AEIVLPIAQHLLVH-PGHAAKIRTVYSHPQALAQCRKWLAEhLPGAELEPANSTAAAAQYVAEHPDEPIAAIASELAAEL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  261 YGLQVLERIEANQRQNFTRFVVLARKAINVS-DQVPAKTTL-LMATGQQAGALVEALLVL--RNHNLimTRLESRPIHGN 336
Cdd:PRK11898 159 YGLEILAEDIQDYPNNRTRFWLLGRKKPPPPlRTGGDKTSLvLTLPNNLPGALYKALSEFawRGINL--TRIESRPTKTG 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 15832716  337 PWEEMFYLDIQANLESAEMQKALKELGEITRSMKVLGCYPS 377
Cdd:PRK11898 237 LGTYFFFIDVEGHIDDVLVAEALKELEALGEDVKVLGSYPV 277
PBP2_PDT_1 cd13630
Catalytic domain of prephenate dehydratase and similar proteins, subgroup 1; the type 2 ...
 105-287 1.25e-61

Catalytic domain of prephenate dehydratase and similar proteins, subgroup 1; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270348 [Multi-domain]  Cd Length: 180  Bit Score: 196.13  E-value: 1.25e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 105 RIAFLGPKGSYSHLAARQYAArHFEQFIEsgCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEM 184
Cdd:cd13630   3 KVAYLGPEGTFSHQAALKYFG-SSVELVP--CPTIEDVFRAVEKGEADYGVVPVENSTEGSVNETLDLLLESDLKICGEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 185 TLTIDHCLLvSGTTDLSTINTVYSHPQPFQQCSKFLNR-YPHWKIEYTESTSAAMEKVAQakSPHVAALGSEAGGTLYGL 263
Cdd:cd13630  80 VLPIHHCLL-SRSGDLSDIKRVYSHPQALAQCRKWLRRnLPNAELIPVSSTAEAARLAAE--DPGAAAIASERAAELYGL 156

                       170       180
                ....*....|....*....|....
gi 15832716 264 QVLERIEANQRQNFTRFVVLARKA 287
Cdd:cd13630 157 PVLAENIEDRPDNTTRFLVIGREP 180
PBP2_Sa-PDT_like cd13633
Catalytic domain of prephenate dehydratase from Staphylococcus aureus and similar proteins, ...
 105-286 4.77e-61

Catalytic domain of prephenate dehydratase from Staphylococcus aureus and similar proteins, subgroup 4; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270351 [Multi-domain]  Cd Length: 184  Bit Score: 194.65  E-value: 4.77e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 105 RIAFLGPKGSYSHLAARQYAARHFEQFIesGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTS-LSIVGE 183
Cdd:cd13633   3 KIGYLGPKGTFSEEAALALFGGEEAELV--PYPTIPDVIEAVAEGEVDYGVVPIENSIEGSVNLTLDLLAHEVdLPIQGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 184 MTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNR-YPHWKIEYTESTSAAMEKVAQAKSPhVAALGSEAGGTLYG 262
Cdd:cd13633  81 IILPIRQNLLVRPGVDLSDITKVYSHPQALAQCRQFLRRnLPGAELEYTGSTAEAARLVAESPEG-WAAIGTLRAAELYG 159

                       170       180
                ....*....|....*....|....*
gi 15832716 263 LQVLER-IEANQRqNFTRFVVLARK 286
Cdd:cd13633 160 LEILAEdIQDYPN-NFTRFVVLGKE 183
PLN02317 PLN02317
arogenate dehydratase
 100-376 1.72e-60

arogenate dehydratase


Pssm-ID: 215181 [Multi-domain]  Cd Length: 382  Bit Score: 199.96  E-value: 1.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  100 NPHSARIAFLGPKGSYSHLAARqyaaRHFEQFIESGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLS 179
Cdd:PLN02317  91 HGSKLRVAYQGVPGAYSEAAAR----KAYPNCEAVPCEQFEAAFQAVELWLADRAVLPIENSLGGSIHRNYDLLLRHRLH 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  180 IVGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYpHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGT 259
Cdd:PLN02317 167 IVGEVQLPVHHCLLALPGVRKEELKRVISHPQALAQCENTLTKL-GVVREAVDDTAGAAKMVAANGLRDTAAIASARAAE 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  260 LYGLQVL-ERIEaNQRQNFTRFVVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLV--LRNHNLimTRLESRPIHGN 336
Cdd:PLN02317 246 LYGLDILaEGIQ-DDSDNVTRFLMLAREPIIPRTDRPFKTSIVFSLEEGPGVLFKALAVfaLRDINL--TKIESRPQRKR 322

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15832716  337 P--------------WEEMFYLDIQANLESAEMQKALKELGEITRSMKVLGCYP 376
Cdd:PLN02317 323 PlrvvddsnsgtakyFDYLFYVDFEASMADPRAQNALAHLQEFATFLRVLGSYP 376
PRK11899 PRK11899
prephenate dehydratase; Provisional
 105-377 1.00e-59

prephenate dehydratase; Provisional


Pssm-ID: 237014 [Multi-domain]  Cd Length: 279  Bit Score: 194.72  E-value: 1.00e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  105 RIAFLGPKGSYSHLAARQYaarhFEQFIESGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEM 184
Cdd:PRK11899   6 RIAFQGEPGANSHLACRDA----FPDMEPLPCATFEDAFEAVESGEADLAMIPIENSLAGRVADIHHLLPESGLHIVGEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  185 TLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLnRYPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLYGLQ 264
Cdd:PRK11899  82 FLPIRHQLMALPGATLEEIKTVHSHPHALGQCRKII-RALGLKPVVAADTAGAARLVAERGDPSMAALASRLAAELYGLD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  265 VLERIEANQRQNFTRFVVLARKAINVS-DQVPAKTTLLMATGQQAGALVEALLVLRNHNLIMTRLESRPIHGNPWEEMFY 343
Cdd:PRK11899 161 ILAENIEDADHNTTRFVVLSREADWAArGDGPIVTTFVFRVRNIPAALYKALGGFATNGVNMTKLESYMVGGSFTATQFY 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 15832716  344 LDIQANLESAEMQKALKELGEITRSMKVLGCYPS 377
Cdd:PRK11899 241 ADIEGHPEDRNVALALEELRFFSEEVRILGVYPA 274
CM_P_1 TIGR01797
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ...
 7-89 1.33e-41

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: 141.11  E-value: 1.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716     7 LLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVL 86
Cdd:TIGR01797   1 LLALREKISAIDEKLLKLLAERRELAFEVGKSKLLSHRPVRDIERERDLLQRLITLGKAYHLDAHYITRLFQLIIEDSVL 80


                  ...
gi 15832716    87 TQQ 89
Cdd:TIGR01797  81 TQQ 83
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 1-180 1.34e-37

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: 133.35  E-value: 1.34e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716   1 MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80
Cdd:COG1605   1 MSESESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716  81 IEDSVLTQQALLQqhlnkinphsaRIAFLGPKGSYSHLAARQyaaRHFEQFIESGCAKFADIFNQVETGQADYAVVPIEN 160
Cdd:COG1605  81 ISESIALQEKLLA-----------EVAYLGPEGGFTGQAAGK---HFGGSAASLPAAAIDEVFREVEAGGAAYGVVPVEN 146

                       170       180
                ....*....|....*....|
gi 15832716 161 TSSGAINDVYDLLQHTSLSI 180
Cdd:COG1605 147 STEGGVVETLDLLLASPLKI 166
ACT_CM-PDT cd04905
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) ...
 297-376 1.31e-32

C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme; The C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme, found in plants, fungi, bacteria, and archaea. The P-protein of E. coli (CM-PDT, PheA) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153177 [Multi-domain]  Cd Length: 80  Bit Score: 117.22  E-value: 1.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 297 KTTLLMATGQQAGALVEALLVLRNHNLIMTRLESRPIHGNPWEEMFYLDIQANLESAEMQKALKELGEITRSMKVLGCYP 376
Cdd:cd04905   1 KTSIVFTLPNKPGALYDVLGVFAERGINLTKIESRPSKGGLWEYVFFIDFEGHIEDPNVAEALEELKRLTEFVKVLGSYP 80
PBP2_Aa-PDT_like cd13632
Catalytic domain of prephenate dehydratase from Arthrobacter aurescens and similar proteins, ...
 103-285 5.78e-30

Catalytic domain of prephenate dehydratase from Arthrobacter aurescens and similar proteins, subgroup 3; the type 2 periplasmic binding protein fold; Prephenate dehydratase (PDT, EC:4.2.1.51) converts prephenate to phenylpyruvate through dehydration and decarboxylation reactions. PDT plays a key role in the biosynthesis of L-Phe in organisms that utilize the shikimate pathway. PDT is allosterically regulated by L-Phe and other amino acids. The catalytic PDT domain consists of two similar subdomains with a cleft in between, which hosts the highly conserved active site. In gram-postive bacteria and archaea, PDT is a monofunctional enzyme, consisting of a catalytic domain (PDT domain) and a regulatory domain (ACT) (aspartokinase, chorismate mustase domain). In gram-negative bacteria, PDT exists as fusion protein with chorismate mutase (CM), forming a bifunctional enzyme, P-protein (PheA). The CM in the P-protein catalyzes the pericycle isomerization of chorismate to prephenate that serves as a substrate for PDT. The CM and PDT are essentail enzymes for the biosynthesis of aromatic amino acids in microorganisms but are not found in humans. Thus, both CM and PDT can potentially serve as drug targets against microbial pathogens. The PDT domain has the same structural fold as the type 2 periplasmic binding proteins (PBP2), many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270350 [Multi-domain]  Cd Length: 183  Bit Score: 113.79  E-value: 5.78e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 103 SARIAFLGPKGSYSHLAARQYAARHFEQFIEsgCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTS-LSIV 181
Cdd:cd13632   1 MTRLAYLGPEGTFTEAALLQLAGADGAELVP--CDSVPAALDAVRSGEADAAVVPIENSVEGGVTATLDALADGDpLVIV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716 182 GEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNR-YPHWKIEYTESTSAAMEKVAQakSPHVAALGSEAGGTL 260
Cdd:cd13632  79 AEVLVPIAFDLAVRPGTTLADVRTVATHPHALAQCRGWLAEnLPGAEFVPASSNAAAARDVAE--GEYDAALAPPIAAEL 156

                       170       180
                ....*....|....*....|....*.
gi 15832716 261 YGLQVL-ERIEANQRQnFTRFVVLAR 285
Cdd:cd13632 157 YGLEVLaDDVADNPGA-VTRFVLVGR 181
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 11-89 6.88e-23

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: 91.02  E-value: 6.88e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832716    11 REKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQ 89
Cdd:pfam01817   1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
ACT_AAAH-PDT-like cd04880
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ...
 299-373 7.32e-23

ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes appear to be regulated, in part, by the phosphorylation of serine residues N-terminal of the ACT domain. Also included in this CD are the C-terminal ACT domains of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme found in plants, fungi, bacteria, and archaea. The P-protein of Escherichia coli (CM-PDT) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153152 [Multi-domain]  Cd Length: 75  Bit Score: 91.02  E-value: 7.32e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832716 299 TLLMATGQQAGALVEALLVLRNHNLIMTRLESRPIHGNPWEEMFYLDIQANLESAEMQKALKELGEITRSMKVLG 373
Cdd:cd04880   1 SLVFSLKNKPGALAKALKVFAERGINLTKIESRPSRKGLWEYEFFVDFEGHIDDPDVKEALEELKRVTEDVKVLG 75
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 11-89 4.03e-21

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: 86.48  E-value: 4.03e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832716     11 REKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQ 89
Cdd:smart00830   1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
PRK06285 PRK06285
chorismate mutase; Provisional
 3-92 4.43e-11

chorismate mutase; Provisional


Pssm-ID: 180509 [Multi-domain]  Cd Length: 96  Bit Score: 58.89  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716    3 SENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIE 82
Cdd:PRK06285   5 AEKRLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNIDENIGLKIMKILME 84

                         90
                 ....*....|
gi 15832716   83 DSVLTQQALL 92
Cdd:PRK06285  85 HSKELQKEYL 94
PRK09269 PRK09269
chorismate mutase; Provisional
 15-94 8.72e-09

chorismate mutase; Provisional


Pssm-ID: 236441  Cd Length: 193  Bit Score: 54.99  E-value: 8.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716   15 SALDEkLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQALLQQ 94
Cdd:PRK09269  32 SALTP-LVDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAPAHGVDPDYVRRFFRDQIEANKLVQYALLAR 110
PRK12595 PRK12595
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
 2-96 1.55e-06

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


Pssm-ID: 183614 [Multi-domain]  Cd Length: 360  Bit Score: 49.59  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716    2 TSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAhHLDAHYITRLFQLII 81
Cdd:PRK12595   1 MMNEELEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLDMIAENNEG-PFEDSTIQHLFKEIF 79

                         90
                 ....*....|....*
gi 15832716   82 EDSVLTQQALLQQHL 96
Cdd:PRK12595  80 KASLELQEDDNRKAL 94
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 1-122 2.19e-06

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 49.11  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832716    1 MTSEnpLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80
Cdd:PRK11199   1 MVAE--LTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15832716   81 IEDSVLTQQallQQHLNKINPHSARIAFLGPKGSYSHLAARQ 122
Cdd:PRK11199  79 MRESYSSEN---DKGFKTLNPDLRPVVIVGGKGQLGRLFAKM 117
CM_M_hiGC-arch TIGR01808
monofunctional chorismate mutase, high GC gram positive type; This model represents the ...
 10-63 1.42e-05

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


Pssm-ID: 130867 [Multi-domain]  Cd Length: 74  Bit Score: 42.59  E-value: 1.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15832716    10 LREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLG 63
Cdd:TIGR01808   5 LREEIDRLDAEILALVKRRAEISQAIGKARMASGGTRLVHSREMKVIERYSELG 58
PRK09239 PRK09239
chorismate mutase; Provisional
 7-85 6.11e-05

chorismate mutase; Provisional


Pssm-ID: 181719 [Multi-domain]  Cd Length: 104  Bit Score: 41.93  E-value: 6.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832716    7 LLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSV 85
Cdd:PRK09239  12 LAALRQSIDNIDAALIHMLAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQLAKDANLDPDFAEKFLNFIIKEVI 90
PRK07248 PRK07248
chorismate mutase;
10-58 1.51e-04

chorismate mutase;


Pssm-ID: 168880 [Multi-domain]  Cd Length: 87  Bit Score: 40.05  E-value: 1.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 15832716   10 LREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLER 58
Cdd:PRK07248   6 IRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDK 54
PRK06443 PRK06443
chorismate mutase; Validated
 10-52 5.72e-04

chorismate mutase; Validated


Pssm-ID: 235801  Cd Length: 177  Bit Score: 40.27  E-value: 5.72e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15832716   10 LREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRE 52
Cdd:PRK06443  10 LRSEILENTMDIIELIEKRRELARMIGIIKMRNGLSIRDSERE 52
Phe4hydrox_tetr TIGR01268
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form ...
 296-345 6.78e-04

phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form of phenylalanine-4-hydroxylase, as found in metazoans. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. It is closely related to metazoan tyrosine 3-monooxygenase and tryptophan 5-monoxygenase, and more distantly to monomeric phenylalanine-4-hydroxylases of some Gram-negative bacteria. The member of this family from Drosophila has been described as having both phenylalanine-4-hydroxylase and tryptophan 5-monoxygenase activity (. However, a Drosophila member of the tryptophan 5-monoxygenase clade has subsequently been discovered.


Pssm-ID: 130335 [Multi-domain]  Cd Length: 436  Bit Score: 41.36  E-value: 6.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15832716   296 AKTTLLMATGQQAGALVEALLVLRNHNLIMTRLESRPIHGNPWEEMFYLD 345
Cdd:TIGR01268  15 AKTSLIFSLKEEAGALAETLKLFQAHDVNLTHIESRPSKTHPGEYEFFVE 64
PRK07857 PRK07857
chorismate mutase;
9-58 8.47e-04

chorismate mutase;


Pssm-ID: 236117  Cd Length: 106  Bit Score: 38.52  E-value: 8.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 15832716    9 ALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLER 58
Cdd:PRK07857  32 ELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIER 81
PRK06034 PRK06034
hypothetical protein; Provisional
 7-58 6.10e-03

hypothetical protein; Provisional


Pssm-ID: 235680 [Multi-domain]  Cd Length: 279  Bit Score: 38.15  E-value: 6.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15832716    7 LLALREKISALDEKLLALLAERRELAVEVGKAKLLSH-----RPVRDIDRERDLLER 58
Cdd:PRK06034  11 LAELRWEIDAIDEELHQLLMERGDIIDRLIAVKRTQEvgsafRPGREADMMRRLVSR 67
 
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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