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Conserved domains on  [gi|1893019181|ref|WP_185133766|]
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prephenate dehydratase domain-containing protein [Chryseobacterium indologenes]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDT pfam00800
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ...
 38-216 1.85e-59

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: 184.67  E-value: 1.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  38 IAYLGPPASFTHSAAGKKFPSQ-TLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFpDIMIEDSLELP 116
Cdd:pfam00800   1 IAYLGPPGTFSHQAALKYFGEDaELVPCPSIEDVFEAVENGEADYGVVPIENSLEGSVNETLDLLLKS-DLKIVGEVYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 117 ISQNLMVVPGTVA--IKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLKVI 194
Cdd:pfam00800  80 IHHCLLARPGTDLedIKTVYSHPQALAQCREFLEEHLPGVERVPVSSTAEAAKKVAAEGDPGAAAIASERAAELYGLKVL 159

                         170       180
                  ....*....|....*....|..
gi 1893019181 195 NTDIQDDKNNRTMFIIISKKNK 216
Cdd:pfam00800 160 AENIEDNPNNTTRFLVLGKEKA 181
 
Name Accession Description Interval E-value
PDT pfam00800
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ...
 38-216 1.85e-59

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: 184.67  E-value: 1.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  38 IAYLGPPASFTHSAAGKKFPSQ-TLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFpDIMIEDSLELP 116
Cdd:pfam00800   1 IAYLGPPGTFSHQAALKYFGEDaELVPCPSIEDVFEAVENGEADYGVVPIENSLEGSVNETLDLLLKS-DLKIVGEVYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 117 ISQNLMVVPGTVA--IKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLKVI 194
Cdd:pfam00800  80 IHHCLLARPGTDLedIKTVYSHPQALAQCREFLEEHLPGVERVPVSSTAEAAKKVAAEGDPGAAAIASERAAELYGLKVL 159

                         170       180
                  ....*....|....*....|..
gi 1893019181 195 NTDIQDDKNNRTMFIIISKKNK 216
Cdd:pfam00800 160 AENIEDNPNNTTRFLVLGKEKA 181
PheA2 COG0077
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ...
 37-217 1.18e-58

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: 185.69  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHSAAGKKF-PSQTLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTeKALIAFPDIMIEDSLEL 115
Cdd:COG0077     3 RIAYLGPEGTFSHQAARKYFgPDAELVPCPSFEDVFEAVESGEADYGVVPIENSIEGSVNET-LDLLLESDLKIVGEVVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 116 PISQNLMVVPGTVA--IKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLKV 193
Cdd:COG0077    82 PIHHCLLARPGTKLedIKTVYSHPQALAQCREFLREHLPGAELVPVSSTAAAARLVAEEGDPGAAAIASELAAELYGLEV 161

                         170       180
                  ....*....|....*....|....
gi 1893019181 194 INTDIQDDKNNRTMFIIISKKNKE 217
Cdd:COG0077   162 LAENIEDNPNNTTRFLVLGREPAA 185
PRK11898 PRK11898
prephenate dehydratase; Provisional
 37-217 5.24e-57

prephenate dehydratase; Provisional


Pssm-ID: 237013 [Multi-domain]  Cd Length: 283  Bit Score: 181.94  E-value: 5.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHSAAGKKFPSQ---TLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFPDIMIEDSL 113
Cdd:PRK11898    3 KIAYLGPEGTFTEAAALKFFPADgeaELVPYDSIPDVLDAVEAGEVDYAVVPIENSIEGSVNPTLDYLAHGSPLQIVAEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 114 ELPISQNLMVVPGTVA-IKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLK 192
Cdd:PRK11898   83 VLPIAQHLLVHPGHAAkIRTVYSHPQALAQCRKWLAEHLPGAELEPANSTAAAAQYVAEHPDEPIAAIASELAAELYGLE 162

                         170       180
                  ....*....|....*....|....*
gi 1893019181 193 VINTDIQDDKNNRTMFIIISKKNKE 217
Cdd:PRK11898  163 ILAEDIQDYPNNRTRFWLLGRKKPP 187
PBP2_PDT_like cd13532
Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic ...
 37-215 1.10e-55

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: 175.41  E-value: 1.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHSAAGKKFP-SQTLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFPDIMIEDSLEL 115
Cdd:cd13532     3 KVAYLGPEGTYSHQAALQLFGdSVELLPLPSISDVFEAVESGEADYGVVPIENSTEGSVVETLDLLRDRPDVKIVGEVYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 116 PISQNLMVVPGT--VAIKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLKV 193
Cdd:cd13532    83 PIHHCLLGRPGAdlSEIKRVYSHPQALGQCRNFLSEHLPGAERIDVSSTAEAAELVAEDPSGTAAAIASELAAELYGLEI 162

                         170       180
                  ....*....|....*....|..
gi 1893019181 194 INTDIQDDKNNRTMFIIISKKN 215
Cdd:cd13532   163 LAENIQDEKDNTTRFLVLGRRE 184
 
Name Accession Description Interval E-value
PDT pfam00800
Prephenate dehydratase; This protein is involved in Phenylalanine biosynthesis. This protein ...
 38-216 1.85e-59

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: 184.67  E-value: 1.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  38 IAYLGPPASFTHSAAGKKFPSQ-TLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFpDIMIEDSLELP 116
Cdd:pfam00800   1 IAYLGPPGTFSHQAALKYFGEDaELVPCPSIEDVFEAVENGEADYGVVPIENSLEGSVNETLDLLLKS-DLKIVGEVYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 117 ISQNLMVVPGTVA--IKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLKVI 194
Cdd:pfam00800  80 IHHCLLARPGTDLedIKTVYSHPQALAQCREFLEEHLPGVERVPVSSTAEAAKKVAAEGDPGAAAIASERAAELYGLKVL 159

                         170       180
                  ....*....|....*....|..
gi 1893019181 195 NTDIQDDKNNRTMFIIISKKNK 216
Cdd:pfam00800 160 AENIEDNPNNTTRFLVLGKEKA 181
PheA2 COG0077
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ...
 37-217 1.18e-58

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: 185.69  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHSAAGKKF-PSQTLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTeKALIAFPDIMIEDSLEL 115
Cdd:COG0077     3 RIAYLGPEGTFSHQAARKYFgPDAELVPCPSFEDVFEAVESGEADYGVVPIENSIEGSVNET-LDLLLESDLKIVGEVVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 116 PISQNLMVVPGTVA--IKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLKV 193
Cdd:COG0077    82 PIHHCLLARPGTKLedIKTVYSHPQALAQCREFLREHLPGAELVPVSSTAAAARLVAEEGDPGAAAIASELAAELYGLEV 161

                         170       180
                  ....*....|....*....|....
gi 1893019181 194 INTDIQDDKNNRTMFIIISKKNKE 217
Cdd:COG0077   162 LAENIEDNPNNTTRFLVLGREPAA 185
PRK11898 PRK11898
prephenate dehydratase; Provisional
 37-217 5.24e-57

prephenate dehydratase; Provisional


Pssm-ID: 237013 [Multi-domain]  Cd Length: 283  Bit Score: 181.94  E-value: 5.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHSAAGKKFPSQ---TLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFPDIMIEDSL 113
Cdd:PRK11898    3 KIAYLGPEGTFTEAAALKFFPADgeaELVPYDSIPDVLDAVEAGEVDYAVVPIENSIEGSVNPTLDYLAHGSPLQIVAEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 114 ELPISQNLMVVPGTVA-IKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLK 192
Cdd:PRK11898   83 VLPIAQHLLVHPGHAAkIRTVYSHPQALAQCRKWLAEHLPGAELEPANSTAAAAQYVAEHPDEPIAAIASELAAELYGLE 162

                         170       180
                  ....*....|....*....|....*
gi 1893019181 193 VINTDIQDDKNNRTMFIIISKKNKE 217
Cdd:PRK11898  163 ILAEDIQDYPNNRTRFWLLGRKKPP 187
PBP2_PDT_like cd13532
Catalytic domain of prephenate dehydratase and similar proteins; the type 2 periplasmic ...
 37-215 1.10e-55

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: 175.41  E-value: 1.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHSAAGKKFP-SQTLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFPDIMIEDSLEL 115
Cdd:cd13532     3 KVAYLGPEGTYSHQAALQLFGdSVELLPLPSISDVFEAVESGEADYGVVPIENSTEGSVVETLDLLRDRPDVKIVGEVYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 116 PISQNLMVVPGT--VAIKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLKV 193
Cdd:cd13532    83 PIHHCLLGRPGAdlSEIKRVYSHPQALGQCRNFLSEHLPGAERIDVSSTAEAAELVAEDPSGTAAAIASELAAELYGLEI 162

                         170       180
                  ....*....|....*....|..
gi 1893019181 194 INTDIQDDKNNRTMFIIISKKN 215
Cdd:cd13532   163 LAENIQDEKDNTTRFLVLGRRE 184
PBP2_Sa-PDT_like cd13633
Catalytic domain of prephenate dehydratase from Staphylococcus aureus and similar proteins, ...
 36-214 6.71e-53

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: 168.07  E-value: 6.71e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  36 EKIAYLGPPASFTHSAAGKKF--PSQTLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFPDIMIEDSL 113
Cdd:cd13633     2 KKIGYLGPKGTFSEEAALALFggEEAELVPYPTIPDVIEAVAEGEVDYGVVPIENSIEGSVNLTLDLLAHEVDLPIQGEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 114 ELPISQNLMVVPGTV--AIKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEKaAAIANTEAARLYKL 191
Cdd:cd13633    82 ILPIRQNLLVRPGVDlsDITKVYSHPQALAQCRQFLRRNLPGAELEYTGSTAEAARLVAESPEGW-AAIGTLRAAELYGL 160

                         170       180
                  ....*....|....*....|...
gi 1893019181 192 KVINTDIQDDKNNRTMFIIISKK 214
Cdd:cd13633   161 EILAEDIQDYPNNFTRFVVLGKE 183
PBP2_PDT_1 cd13630
Catalytic domain of prephenate dehydratase and similar proteins, subgroup 1; the type 2 ...
 37-215 1.04e-50

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: 162.62  E-value: 1.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHSAAGKKFPSQT-LVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFpDIMIEDSLEL 115
Cdd:cd13630     3 KVAYLGPEGTFSHQAALKYFGSSVeLVPCPTIEDVFRAVEKGEADYGVVPVENSTEGSVNETLDLLLES-DLKICGEVVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 116 PISQNLMVVPGTVA-IKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPE------EKaaaianteAARL 188
Cdd:cd13630    82 PIHHCLLSRSGDLSdIKRVYSHPQALAQCRKWLRRNLPNAELIPVSSTAEAARLAAEDPGaaaiasER--------AAEL 153

                         170       180
                  ....*....|....*....|....*..
gi 1893019181 189 YKLKVINTDIQDDKNNRTMFIIISKKN 215
Cdd:cd13630   154 YGLPVLAENIEDRPDNTTRFLVIGREP 180
PBP2_Ct-PDT_like cd13631
Catalytic domain of prephenate dehydratase from Chlorobium tepidum and similar proteins, ...
 37-214 2.62e-45

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: 148.71  E-value: 2.62e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHSAAGKKFP-SQTLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFpDIMIEDSLEL 115
Cdd:cd13631     3 RVAYQGVPGAYSHLAARKYFGeDEEVPCCKTFEDVFEAVESGEADYGVLPIENSSAGSINEVYDLLLEY-DLYIVGEIFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 116 PISQNLMVVPGTVA--IKKIYSHPQALRQSRRLIDSlYPAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLKV 193
Cdd:cd13631    82 PIEHCLLALPGAKLedIKEVYSHPQALAQCSKFLKK-HPGIKLVPYYDTAGAAKKVAEEGDKTVAAIASELAAELYGLEI 160

                         170       180
                  ....*....|....*....|.
gi 1893019181 194 INTDIQDDKNNRTMFIIISKK 214
Cdd:cd13631   161 LAENIQDNKNNYTRFLILSRK 181
PBP2_Aa-PDT_like cd13632
Catalytic domain of prephenate dehydratase from Arthrobacter aurescens and similar proteins, ...
 37-213 4.94e-32

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: 114.56  E-value: 4.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHsAAGKKFPSQ---TLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFPDIMIEDSL 113
Cdd:cd13632     3 RLAYLGPEGTFTE-AALLQLAGAdgaELVPCDSVPAALDAVRSGEADAAVVPIENSVEGGVTATLDALADGDPLVIVAEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 114 ELPISQNLMVVPGTV--AIKKIYSHPQALRQSRRLIDSLYPAIPRIEYSSTSAAAKWVSEHPEEkaAAIANTEAARLYKL 191
Cdd:cd13632    82 LVPIAFDLAVRPGTTlaDVRTVATHPHALAQCRGWLAENLPGAEFVPASSNAAAARDVAEGEYD--AALAPPIAAELYGL 159

                         170       180
                  ....*....|....*....|..
gi 1893019181 192 KVINTDIQDDKNNRTMFIIISK 213
Cdd:cd13632   160 EVLADDVADNPGAVTRFVLVGR 181
PRK11899 PRK11899
prephenate dehydratase; Provisional
 34-216 2.74e-24

prephenate dehydratase; Provisional


Pssm-ID: 237014 [Multi-domain]  Cd Length: 279  Bit Score: 96.88  E-value: 2.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  34 PSEKIAYLGPPASFTHSAAGKKFPSQTLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVvptekaliafPDI---MIE 110
Cdd:PRK11899    3 KTNRIAFQGEPGANSHLACRDAFPDMEPLPCATFEDAFEAVESGEADLAMIPIENSLAGRV----------ADIhhlLPE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 111 DSLE------LPISQNLMVVPGTV--AIKKIYSHPQALRQSRRLIDSLypAIPRIEYSSTSAAAKWVSEHPEEKAAAIAN 182
Cdd:PRK11899   73 SGLHivgeyfLPIRHQLMALPGATleEIKTVHSHPHALGQCRKIIRAL--GLKPVVAADTAGAARLVAERGDPSMAALAS 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1893019181 183 TEAARLYKLKVINTDIQDDKNNRTMFIIISKKNK 216
Cdd:PRK11899  151 RLAAELYGLDILAENIEDADHNTTRFVVLSREAD 184
PLN02317 PLN02317
arogenate dehydratase
 37-214 3.28e-24

arogenate dehydratase


Pssm-ID: 215181 [Multi-domain]  Cd Length: 382  Bit Score: 98.65  E-value: 3.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  37 KIAYLGPPASFTHSAAGKKFPSQTLVFQNSIEECFISVRSGIAEKAVVPLKNSIGGIVVPTEKALIAFpDIMIEDSLELP 116
Cdd:PLN02317   96 RVAYQGVPGAYSEAAARKAYPNCEAVPCEQFEAAFQAVELWLADRAVLPIENSLGGSIHRNYDLLLRH-RLHIVGEVQLP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 117 ISQNLMVVPGTVA--IKKIYSHPQALRQSRRLIDSLypAIPRIEYSSTSAAAKWVSEHPEEKAAAIANTEAARLYKLKVI 194
Cdd:PLN02317  175 VHHCLLALPGVRKeeLKRVISHPQALAQCENTLTKL--GVVREAVDDTAGAAKMVAANGLRDTAAIASARAAELYGLDIL 252

                         170       180
                  ....*....|....*....|
gi 1893019181 195 NTDIQDDKNNRTMFIIISKK 214
Cdd:PLN02317  253 AEGIQDDSDNVTRFLMLARE 272
pheA PRK10622
bifunctional chorismate mutase/prephenate dehydratase; Provisional
 28-214 2.40e-16

bifunctional chorismate mutase/prephenate dehydratase; Provisional


Pssm-ID: 182594 [Multi-domain]  Cd Length: 386  Bit Score: 76.69  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181  28 HLNKINP-SEKIAYLGPPASFTHSAAgKKFPSQTlvFQNSIE-------ECFISVRSGIAEKAVVPLKNSIGGIVVPTEK 99
Cdd:PRK10622   95 HLNKTNPhSARIAFLGPKGSYSHLAA-RQYAARH--FEQFIEsgcakfaDIFNQVETGQADYAVLPIENTSSGAINDVYD 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893019181 100 aLIAFPDIMIEDSLELPISQNLMVVPGT--VAIKKIYSHPQALRQSRRLIdSLYPAIpRIEYS-STSAAAKWVSEHPEEK 176
Cdd:PRK10622  172 -LLQHTSLSIVGEMTLPIDHCVLVSGTTdlSTIETVYSHPQPFQQCSQFL-NRYPHW-KIEYTeSTAAAMEKVAQANSPH 248

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1893019181 177 AAAIANTEAARLYKLKVINTDIQDDKNNRTMFIIISKK 214
Cdd:PRK10622  249 VAALGSEAGGALYGLQVLERNLANQQQNITRFIVLARK 286
 
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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