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Conserved domains on  [gi|657148510|gb|AID25607|]
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bifunctional chorismate mutase/prephenate dehydratase [Salmonella bongori serovar 48:z41:-- str. RKS3044]

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: 775.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510   1 MTSENPLLALRDKISALDEELLALLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLV 80
Cdd:PRK10622   1 MTSENPLLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510  81 IEDSVLTQQALLQQHLNNTYPHSARVAFLGPKGSYSHLAARQYAARHFEQFIERGCAKFADIFQQVETGQADYAVVPIEN 160
Cdd:PRK10622  81 IEDSVLTQQALLQQHLNKTNPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVLPIEN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 161 TSSGAINDVYDLLQHTSLSIVGEMTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRYPHWKINYTESTSAAMEK 240
Cdd:PRK10622 161 TSSGAINDVYDLLQHTSLSIVGEMTLPIDHCVLVSGTTDLSTIETVYSHPQPFQQCSQFLNRYPHWKIEYTESTAAAMEK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 241 VAQENSPRVAALGSEAGGMLHGLQVLERIAANQTQNITRFLVLARKAINVSAQVPAKTTLLIATGQQAGALVEALLVLRN 320
Cdd:PRK10622 241 VAQANSPHVAALGSEAGGALYGLQVLERNLANQQQNITRFIVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657148510 321 HNLIMTKLESRPIHGNPWEEMFYLDIQANLESQVMQSALKELGEITRSMKVLGCYPSENVVPVEPA 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: 775.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510   1 MTSENPLLALRDKISALDEELLALLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLV 80
Cdd:PRK10622   1 MTSENPLLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510  81 IEDSVLTQQALLQQHLNNTYPHSARVAFLGPKGSYSHLAARQYAARHFEQFIERGCAKFADIFQQVETGQADYAVVPIEN 160
Cdd:PRK10622  81 IEDSVLTQQALLQQHLNKTNPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVLPIEN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 161 TSSGAINDVYDLLQHTSLSIVGEMTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRYPHWKINYTESTSAAMEK 240
Cdd:PRK10622 161 TSSGAINDVYDLLQHTSLSIVGEMTLPIDHCVLVSGTTDLSTIETVYSHPQPFQQCSQFLNRYPHWKIEYTESTAAAMEK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 241 VAQENSPRVAALGSEAGGMLHGLQVLERIAANQTQNITRFLVLARKAINVSAQVPAKTTLLIATGQQAGALVEALLVLRN 320
Cdd:PRK10622 241 VAQANSPHVAALGSEAGGALYGLQVLERNLANQQQNITRFIVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657148510 321 HNLIMTKLESRPIHGNPWEEMFYLDIQANLESQVMQSALKELGEITRSMKVLGCYPSENVVPVEPA 386
Cdd:PRK10622 321 HNLIMTKLESRPIHGNPWEEMFYLDVQANLRSAEMQKALKELGEITRSLKVLGCYPSENVVPVDPT 386
PheA2 COG0077
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ...
 103-380 4.27e-124

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: 359.03  E-value: 4.27e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 103 SARVAFLGPKGSYSHLAARQYAARHFEqfiERGCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVG 182
Cdd:COG0077    1 MMRIAYLGPEGTFSHQAARKYFGPDAE---LVPCPSFEDVFEAVESGEADYGVVPIENSIEGSVNETLDLLLESDLKIVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 183 EMTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRY-PHWKINYTESTSAAMEKVAQENSPRVAALGSEAGGMLH 261
Cdd:COG0077   78 EVVLPIHHCLLARPGTKLEDIKTVYSHPQALAQCREFLREHlPGAELVPVSSTAAAARLVAEEGDPGAAAIASELAAELY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 262 GLQVLERIAANQTQNITRFLVLARKaiNVSAQVPAKTTLLIATGQQAGALVEALLVLRNHNLIMTKLESRPIHGNPWEEM 341
Cdd:COG0077  158 GLEVLAENIEDNPNNTTRFLVLGRE--PAAPTGADKTSLVFSLPNRPGALYKALGVFATRGINLTKIESRPIKGGLWEYV 235

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 657148510 342 FYLDIQANLESQVMQSALKELGEITRSMKVLGCYPSENV 380
Cdd:COG0077  236 FFIDVEGHIDDPRVAEALEELKRLTEFLKILGSYPRADL 274
PBP2_Ct-PDT_like cd13631
Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, ...
 103-287 9.35e-87

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: 260.42  E-value: 9.35e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 103 SARVAFLGPKGSYSHLAARQYaarhFEQFIERGCAK-FADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIV 181
Cdd:cd13631    1 MKRVAYQGVPGAYSHLAARKY----FGEDEEVPCCKtFEDVFEAVESGEADYGVLPIENSSAGSINEVYDLLLEYDLYIV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 182 GEMTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRYPHWKINYTESTSAAMEKVAQENSPRVAALGSEAGGMLH 261
Cdd:cd13631   77 GEIFLPIEHCLLALPGAKLEDIKEVYSHPQALAQCSKFLKKHPGIKLVPYYDTAGAAKKVAEEGDKTVAAIASELAAELY 156

                        170       180
                 ....*....|....*....|....*.
gi 657148510 262 GLQVLERIAANQTQNITRFLVLARKA 287
Cdd:cd13631  157 GLEILAENIQDNKNNYTRFLILSRKP 182
PDT pfam00800
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ...
 106-286 4.30e-76

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: 233.20  E-value: 4.30e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510  106 VAFLGPKGSYSHLAARQYAARHFEqfiERGCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEMT 185
Cdd:pfam00800   1 IAYLGPPGTFSHQAALKYFGEDAE---LVPCPSIEDVFEAVENGEADYGVVPIENSLEGSVNETLDLLLKSDLKIVGEVY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510  186 VTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSR-YPHWKINYTESTSAAMEKVAQENSPRVAALGSEAGGMLHGLQ 264
Cdd:pfam00800  78 LPIHHCLLARPGTDLEDIKTVYSHPQALAQCREFLEEhLPGVERVPVSSTAEAAKKVAAEGDPGAAAIASERAAELYGLK 157

                         170       180
                  ....*....|....*....|..
gi 657148510  265 VLERIAANQTQNITRFLVLARK 286
Cdd:pfam00800 158 VLAENIEDNPNNTTRFLVLGKE 179
CM_P_1 TIGR01797
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ...
 7-89 9.53e-31

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: 112.60  E-value: 9.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510    7 LLALRDKISALDEELLALLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLVIEDSVL 86
Cdd:TIGR01797   1 LLALREKISAIDEKLLKLLAERRELAFEVGKSKLLSHRPVRDIERERDLLQRLITLGKAYHLDAHYITRLFQLIIEDSVL 80


                  ...
gi 657148510   87 TQQ 89
Cdd:TIGR01797  81 TQQ 83
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 24-89 3.18e-12

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: 61.83  E-value: 3.18e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657148510    24 LLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLVIEDSVLTQQ 89
Cdd:smart00830  14 LLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 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: 775.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510   1 MTSENPLLALRDKISALDEELLALLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLV 80
Cdd:PRK10622   1 MTSENPLLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510  81 IEDSVLTQQALLQQHLNNTYPHSARVAFLGPKGSYSHLAARQYAARHFEQFIERGCAKFADIFQQVETGQADYAVVPIEN 160
Cdd:PRK10622  81 IEDSVLTQQALLQQHLNKTNPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVLPIEN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 161 TSSGAINDVYDLLQHTSLSIVGEMTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRYPHWKINYTESTSAAMEK 240
Cdd:PRK10622 161 TSSGAINDVYDLLQHTSLSIVGEMTLPIDHCVLVSGTTDLSTIETVYSHPQPFQQCSQFLNRYPHWKIEYTESTAAAMEK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 241 VAQENSPRVAALGSEAGGMLHGLQVLERIAANQTQNITRFLVLARKAINVSAQVPAKTTLLIATGQQAGALVEALLVLRN 320
Cdd:PRK10622 241 VAQANSPHVAALGSEAGGALYGLQVLERNLANQQQNITRFIVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRN 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657148510 321 HNLIMTKLESRPIHGNPWEEMFYLDIQANLESQVMQSALKELGEITRSMKVLGCYPSENVVPVEPA 386
Cdd:PRK10622 321 HNLIMTKLESRPIHGNPWEEMFYLDVQANLRSAEMQKALKELGEITRSLKVLGCYPSENVVPVDPT 386
PheA2 COG0077
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ...
 103-380 4.27e-124

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: 359.03  E-value: 4.27e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 103 SARVAFLGPKGSYSHLAARQYAARHFEqfiERGCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVG 182
Cdd:COG0077    1 MMRIAYLGPEGTFSHQAARKYFGPDAE---LVPCPSFEDVFEAVESGEADYGVVPIENSIEGSVNETLDLLLESDLKIVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 183 EMTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRY-PHWKINYTESTSAAMEKVAQENSPRVAALGSEAGGMLH 261
Cdd:COG0077   78 EVVLPIHHCLLARPGTKLEDIKTVYSHPQALAQCREFLREHlPGAELVPVSSTAAAARLVAEEGDPGAAAIASELAAELY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 262 GLQVLERIAANQTQNITRFLVLARKaiNVSAQVPAKTTLLIATGQQAGALVEALLVLRNHNLIMTKLESRPIHGNPWEEM 341
Cdd:COG0077  158 GLEVLAENIEDNPNNTTRFLVLGRE--PAAPTGADKTSLVFSLPNRPGALYKALGVFATRGINLTKIESRPIKGGLWEYV 235

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 657148510 342 FYLDIQANLESQVMQSALKELGEITRSMKVLGCYPSENV 380
Cdd:COG0077  236 FFIDVEGHIDDPRVAEALEELKRLTEFLKILGSYPRADL 274
PBP2_Ct-PDT_like cd13631
Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, ...
 103-287 9.35e-87

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: 260.42  E-value: 9.35e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 103 SARVAFLGPKGSYSHLAARQYaarhFEQFIERGCAK-FADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIV 181
Cdd:cd13631    1 MKRVAYQGVPGAYSHLAARKY----FGEDEEVPCCKtFEDVFEAVESGEADYGVLPIENSSAGSINEVYDLLLEYDLYIV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 182 GEMTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRYPHWKINYTESTSAAMEKVAQENSPRVAALGSEAGGMLH 261
Cdd:cd13631   77 GEIFLPIEHCLLALPGAKLEDIKEVYSHPQALAQCSKFLKKHPGIKLVPYYDTAGAAKKVAEEGDKTVAAIASELAAELY 156

                        170       180
                 ....*....|....*....|....*.
gi 657148510 262 GLQVLERIAANQTQNITRFLVLARKA 287
Cdd:cd13631  157 GLEILAENIQDNKNNYTRFLILSRKP 182
PDT pfam00800
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ...
 106-286 4.30e-76

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: 233.20  E-value: 4.30e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510  106 VAFLGPKGSYSHLAARQYAARHFEqfiERGCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEMT 185
Cdd:pfam00800   1 IAYLGPPGTFSHQAALKYFGEDAE---LVPCPSIEDVFEAVENGEADYGVVPIENSLEGSVNETLDLLLKSDLKIVGEVY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510  186 VTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSR-YPHWKINYTESTSAAMEKVAQENSPRVAALGSEAGGMLHGLQ 264
Cdd:pfam00800  78 LPIHHCLLARPGTDLEDIKTVYSHPQALAQCREFLEEhLPGVERVPVSSTAEAAKKVAAEGDPGAAAIASERAAELYGLK 157

                         170       180
                  ....*....|....*....|..
gi 657148510  265 VLERIAANQTQNITRFLVLARK 286
Cdd:pfam00800 158 VLAENIEDNPNNTTRFLVLGKE 179
PBP2_PDT_like cd13532
Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic ...
 105-286 4.46e-69

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: 215.47  E-value: 4.46e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 105 RVAFLGPKGSYSHLAARQYAArHFEQFIErgCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLL-QHTSLSIVGE 183
Cdd:cd13532    3 KVAYLGPEGTYSHQAALQLFG-DSVELLP--LPSISDVFEAVESGEADYGVVPIENSTEGSVVETLDLLrDRPDVKIVGE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 184 MTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRY-PHWKINYTESTSAAMEKVAQENSPRVAALGSEAGGMLHG 262
Cdd:cd13532   80 VYLPIHHCLLGRPGADLSEIKRVYSHPQALGQCRNFLSEHlPGAERIDVSSTAEAAELVAEDPSGTAAAIASELAAELYG 159

                        170       180
                 ....*....|....*....|....
gi 657148510 263 LQVLERIAANQTQNITRFLVLARK 286
Cdd:cd13532  160 LEILAENIQDEKDNTTRFLVLGRR 183
PRK11898 PRK11898
prephenate dehydratase; Provisional
 103-377 4.04e-65

prephenate dehydratase; Provisional


Pssm-ID: 237013 [Multi-domain]  Cd Length: 283  Bit Score: 208.91  E-value: 4.04e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 103 SARVAFLGPKGSYSHLAARQYAARHFEQFIERgCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLL-QHTSLSIV 181
Cdd:PRK11898   1 MMKIAYLGPEGTFTEAAALKFFPADGEAELVP-YDSIPDVLDAVEAGEVDYAVVPIENSIEGSVNPTLDYLaHGSPLQIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 182 GEMTVTIDHCVLVSgTTDLNTIETVYSHPQPFQQCSKFLSR-YPHWKINYTESTSAAMEKVAQENSPRVAALGSEAGGML 260
Cdd:PRK11898  80 AEIVLPIAQHLLVH-PGHAAKIRTVYSHPQALAQCRKWLAEhLPGAELEPANSTAAAAQYVAEHPDEPIAAIASELAAEL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 261 HGLQVLERIAANQTQNITRFLVLARKAINVSA-QVPAKTTLLIATGQ-QAGALVEALLVL--RNHNLimTKLESRPIHGN 336
Cdd:PRK11898 159 YGLEILAEDIQDYPNNRTRFWLLGRKKPPPPLrTGGDKTSLVLTLPNnLPGALYKALSEFawRGINL--TRIESRPTKTG 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 657148510 337 PWEEMFYLDIQANLESQVMQSALKELGEITRSMKVLGCYPS 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 1.24e-59

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: 191.12  E-value: 1.24e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 105 RVAFLGPKGSYSHLAARQYAArHFEQFIErgCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEM 184
Cdd:cd13630    3 KVAYLGPEGTFSHQAALKYFG-SSVELVP--CPTIEDVFRAVEKGEADYGVVPVENSTEGSVNETLDLLLESDLKICGEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 185 TVTIDHCvLVSGTTDLNTIETVYSHPQPFQQCSKFLSR-YPHWKINYTESTSAAMEKVAQEnsPRVAALGSEAGGMLHGL 263
Cdd:cd13630   80 VLPIHHC-LLSRSGDLSDIKRVYSHPQALAQCRKWLRRnLPNAELIPVSSTAEAARLAAED--PGAAAIASERAAELYGL 156

                        170       180
                 ....*....|....*....|....
gi 657148510 264 QVLERIAANQTQNITRFLVLARKA 287
Cdd:cd13630  157 PVLAENIEDRPDNTTRFLVIGREP 180
PLN02317 PLN02317
arogenate dehydratase
 105-376 3.37e-59

arogenate dehydratase


Pssm-ID: 215181 [Multi-domain]  Cd Length: 382  Bit Score: 196.49  E-value: 3.37e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 105 RVAFLGPKGSYSHLAARqyaaRHFEQFIERGCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEM 184
Cdd:PLN02317  96 RVAYQGVPGAYSEAAAR----KAYPNCEAVPCEQFEAAFQAVELWLADRAVLPIENSLGGSIHRNYDLLLRHRLHIVGEV 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 185 TVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRYpHWKINYTESTSAAMEKVAQENSPRVAALGSEAGGMLHGLQ 264
Cdd:PLN02317 172 QLPVHHCLLALPGVRKEELKRVISHPQALAQCENTLTKL-GVVREAVDDTAGAAKMVAANGLRDTAAIASARAAELYGLD 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 265 VLERIAANQTQNITRFLVLARKAINVSAQVPAKTTLLIATGQQAGALVEALLV--LRNHNLimTKLESRPIHGNP----- 337
Cdd:PLN02317 251 ILAEGIQDDSDNVTRFLMLAREPIIPRTDRPFKTSIVFSLEEGPGVLFKALAVfaLRDINL--TKIESRPQRKRPlrvvd 328

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 657148510 338 ---------WEEMFYLDIQANLESQVMQSALKELGEITRSMKVLGCYP 376
Cdd:PLN02317 329 dsnsgtakyFDYLFYVDFEASMADPRAQNALAHLQEFATFLRVLGSYP 376
PRK11899 PRK11899
prephenate dehydratase; Provisional
 105-377 5.58e-56

prephenate dehydratase; Provisional


Pssm-ID: 237014 [Multi-domain]  Cd Length: 279  Bit Score: 185.09  E-value: 5.58e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 105 RVAFLGPKGSYSHLAARQYaarhFEQFIERGCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEM 184
Cdd:PRK11899   6 RIAFQGEPGANSHLACRDA----FPDMEPLPCATFEDAFEAVESGEADLAMIPIENSLAGRVADIHHLLPESGLHIVGEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 185 TVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSRYpHWK-INYTESTSAAMEkVAQENSPRVAALGSEAGGMLHGL 263
Cdd:PRK11899  82 FLPIRHQLMALPGATLEEIKTVHSHPHALGQCRKIIRAL-GLKpVVAADTAGAARL-VAERGDPSMAALASRLAAELYGL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 264 QVLERIAANQTQNITRFLVLARKAINVSA-QVPAKTTLLIATGQQAGALVEALLVLRNHNLIMTKLESRPIHGNPWEEMF 342
Cdd:PRK11899 160 DILAENIEDADHNTTRFVVLSREADWAARgDGPIVTTFVFRVRNIPAALYKALGGFATNGVNMTKLESYMVGGSFTATQF 239

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 657148510 343 YLDIQANLESQVMQSALKELGEITRSMKVLGCYPS 377
Cdd:PRK11899 240 YADIEGHPEDRNVALALEELRFFSEEVRILGVYPA 274
PBP2_Sa-PDT_like cd13633
Catalytic domain of prephenate dehydratase from Staphylococcus aureus and similar proteins, ...
 105-286 2.41e-55

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: 180.01  E-value: 2.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 105 RVAFLGPKGSYSHLAARQYAARhfEQFIERGCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTS-LSIVGE 183
Cdd:cd13633    3 KIGYLGPKGTFSEEAALALFGG--EEAELVPYPTIPDVIEAVAEGEVDYGVVPIENSIEGSVNLTLDLLAHEVdLPIQGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 184 MTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFL-SRYPHWKINYTESTSAAMEKVAQENSPrVAALGSEAGGMLHG 262
Cdd:cd13633   81 IILPIRQNLLVRPGVDLSDITKVYSHPQALAQCRQFLrRNLPGAELEYTGSTAEAARLVAESPEG-WAAIGTLRAAELYG 159

                        170       180
                 ....*....|....*....|....
gi 657148510 263 LQVLERIAANQTQNITRFLVLARK 286
Cdd:cd13633  160 LEILAEDIQDYPNNFTRFVVLGKE 183
ACT_CM-PDT cd04905
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) ...
 297-376 2.28e-31

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: 114.13  E-value: 2.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 297 KTTLLIATGQQAGALVEALLVLRNHNLIMTKLESRPIHGNPWEEMFYLDIQANLESQVMQSALKELGEITRSMKVLGCYP 376
Cdd:cd04905    1 KTSIVFTLPNKPGALYDVLGVFAERGINLTKIESRPSKGGLWEYVFFIDFEGHIEDPNVAEALEELKRLTEFVKVLGSYP 80
CM_P_1 TIGR01797
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ...
 7-89 9.53e-31

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: 112.60  E-value: 9.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510    7 LLALRDKISALDEELLALLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLVIEDSVL 86
Cdd:TIGR01797   1 LLALREKISAIDEKLLKLLAERRELAFEVGKSKLLSHRPVRDIERERDLLQRLITLGKAYHLDAHYITRLFQLIIEDSVL 80


                  ...
gi 657148510   87 TQQ 89
Cdd:TIGR01797  81 TQQ 83
PBP2_Aa-PDT_like cd13632
Catalytic domain of prephenate dehydratase from Arthrobacter aurescens and similar proteins, ...
 103-285 8.42e-27

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: 105.32  E-value: 8.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 103 SARVAFLGPKGSYSHLAARQYAARHFEQFIErgCAKFADIFQQVETGQADYAVVPIENTSSGAINDVYDLLQHTS-LSIV 181
Cdd:cd13632    1 MTRLAYLGPEGTFTEAALLQLAGADGAELVP--CDSVPAALDAVRSGEADAAVVPIENSVEGGVTATLDALADGDpLVIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510 182 GEMTVTIDHCVLVSGTTDLNTIETVYSHPQPFQQCSKFLSR-YPHWKINYTESTSAAMEKVAqenSPRV-AALGSEAGGM 259
Cdd:cd13632   79 AEVLVPIAFDLAVRPGTTLADVRTVATHPHALAQCRGWLAEnLPGAEFVPASSNAAAARDVA---EGEYdAALAPPIAAE 155

                        170       180
                 ....*....|....*....|....*..
gi 657148510 260 LHGLQVL-ERIAANQtQNITRFLVLAR 285
Cdd:cd13632  156 LYGLEVLaDDVADNP-GAVTRFVLVGR 181
PheA COG1605
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ...
 1-180 5.81e-26

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: 102.54  E-value: 5.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510   1 MTSENPLLALRDKISALDEELLALLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLV 80
Cdd:COG1605    1 MSESESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510  81 IEDSVLTQQALLQqhlnntyphsaRVAFLGPKGSYSHLAARQyaaRHFEQFIERGCAKFADIFQQVETGQADYAVVPIEN 160
Cdd:COG1605   81 ISESIALQEKLLA-----------EVAYLGPEGGFTGQAAGK---HFGGSAASLPAAAIDEVFREVEAGGAAYGVVPVEN 146

                        170       180
                 ....*....|....*....|
gi 657148510 161 TSSGAINDVYDLLQHTSLSI 180
Cdd:COG1605  147 STEGGVVETLDLLLASPLKI 166
ACT_AAAH-PDT-like cd04880
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ...
 299-373 2.29e-22

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: 89.48  E-value: 2.29e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657148510 299 TLLIATGQQAGALVEALLVLRNHNLIMTKLESRPIHGNPWEEMFYLDIQANLESQVMQSALKELGEITRSMKVLG 373
Cdd:cd04880    1 SLVFSLKNKPGALAKALKVFAERGINLTKIESRPSRKGLWEYEFFVDFEGHIDDPDVKEALEELKRVTEDVKVLG 75
CM_2 smart00830
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ...
 24-89 3.18e-12

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: 61.83  E-value: 3.18e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657148510    24 LLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLVIEDSVLTQQ 89
Cdd:smart00830  14 LLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
CM_2 pfam01817
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ...
 24-89 5.46e-12

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: 60.97  E-value: 5.46e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657148510   24 LLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLVIEDSVLTQQ 89
Cdd:pfam01817  14 LLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
PRK09269 PRK09269
chorismate mutase; Provisional
 28-94 1.98e-06

chorismate mutase; Provisional


Pssm-ID: 236441  Cd Length: 193  Bit Score: 48.06  E-value: 1.98e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 657148510  28 RRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLVIEDSVLTQQALLQQ 94
Cdd:PRK09269  44 RLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAPAHGVDPDYVRRFFRDQIEANKLVQYALLAR 110
PRK06285 PRK06285
chorismate mutase; Provisional
 3-84 3.41e-04

chorismate mutase; Provisional


Pssm-ID: 180509 [Multi-domain]  Cd Length: 96  Bit Score: 39.25  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657148510   3 SENPLLALRDKISALDEELLALLAKRRALAIEVGKAKLLSHRPVRDIDRERALLDRLIYLGKAHHLDAHYITRLFQLVIE 82
Cdd:PRK06285   5 AEKRLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNIDENIGLKIMKILME 84


                 ..
gi 657148510  83 DS 84
Cdd:PRK06285  85 HS 86
Phe4hydrox_tetr TIGR01268
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form ...
 296-345 7.34e-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: 7.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 657148510  296 AKTTLLIATGQQAGALVEALLVLRNHNLIMTKLESRPIHGNPWEEMFYLD 345
Cdd:TIGR01268  15 AKTSLIFSLKEEAGALAETLKLFQAHDVNLTHIESRPSKTHPGEYEFFVE 64
 
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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