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Conserved domains on  [gi|343781041|pdb|2Y77|A]
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Chain A, 3-DEHYDROQUINATE DEHYDRATASE

Protein Classification

type II 3-dehydroquinate dehydratase( domain architecture ID 10792487)

type II 3-dehydroquinate dehydratase reversibly catalyzes the conversion of dehydroquinate to dehydroshikimate, the third step in the biosynthetic shikimate pathway

EC:  4.2.1.10
Gene Ontology:  GO:0003855
SCOP:  4003733

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
5-145 1.60e-83

type II 3-dehydroquinate dehydratase;


:

Pssm-ID: 235443  Cd Length: 146  Bit Score: 241.50  E-value: 1.60e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A         5 VNVINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSV 84
Cdd:PRK05395   4 ILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTHTSV 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
2Y77_A        85 ALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHVG 145
Cdd:PRK05395  84 ALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLS 144
 
Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
5-145 1.60e-83

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 241.50  E-value: 1.60e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A         5 VNVINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSV 84
Cdd:PRK05395   4 ILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTHTSV 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
2Y77_A        85 ALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHVG 145
Cdd:PRK05395  84 ALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLS 144
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
7-145 5.88e-82

3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440520  Cd Length: 145  Bit Score: 237.23  E-value: 5.88e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A        7 VINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSVAL 86
Cdd:COG0757   6 VLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTHTSVAL 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
2Y77_A       87 RDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHVG 145
Cdd:COG0757  86 RDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAELLS 144
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
5-143 3.10e-80

Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes the reversible dehydration of 3-dehydroquinate to form 3-dehydroshikimate. This reaction is part of two metabolic pathways: the biosynthetic shikimate pathway and the catabolic quinate pathway. There are two types of DHQases, which are distinct from each other in amino acid sequence and three-dimensional structure. Type I enzymes usually catalyze the biosynthetic reaction using a syn elimination mechanism. In contrast, type II enzymes, found in the quinate pathway of fungi and in the shikimate pathway of many bacteria, are dodecameric enzymes that employ an anti elimination reaction mechanism.


Pssm-ID: 238262  Cd Length: 140  Bit Score: 232.71  E-value: 3.10e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A        5 VNVINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSV 84
Cdd:cd00466   2 ILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTSI 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
2Y77_A       85 ALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEH 143
Cdd:cd00466  82 ALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALASL 140
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
4-144 4.79e-78

3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I enzyme, often found as part of a multifunctional protein, is described by TIGR01093. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130160  Cd Length: 141  Bit Score: 227.61  E-value: 4.79e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A          4 IVNVINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTS 83
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
2Y77_A         84 VALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHV 144
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEIL 141
DHquinase_II pfam01220
Dehydroquinase class II;
7-141 2.46e-77

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 225.28  E-value: 2.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A          7 VINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSVAL 86
Cdd:pfam01220   4 VLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTSVAL 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
2Y77_A         87 RDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLA 141
Cdd:pfam01220  84 RDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
 
Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
5-145 1.60e-83

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 241.50  E-value: 1.60e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A         5 VNVINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSV 84
Cdd:PRK05395   4 ILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTHTSV 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
2Y77_A        85 ALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHVG 145
Cdd:PRK05395  84 ALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLS 144
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
7-145 5.88e-82

3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440520  Cd Length: 145  Bit Score: 237.23  E-value: 5.88e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A        7 VINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSVAL 86
Cdd:COG0757   6 VLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTHTSVAL 85
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
2Y77_A       87 RDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHVG 145
Cdd:COG0757  86 RDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAELLS 144
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
5-143 3.10e-80

Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes the reversible dehydration of 3-dehydroquinate to form 3-dehydroshikimate. This reaction is part of two metabolic pathways: the biosynthetic shikimate pathway and the catabolic quinate pathway. There are two types of DHQases, which are distinct from each other in amino acid sequence and three-dimensional structure. Type I enzymes usually catalyze the biosynthetic reaction using a syn elimination mechanism. In contrast, type II enzymes, found in the quinate pathway of fungi and in the shikimate pathway of many bacteria, are dodecameric enzymes that employ an anti elimination reaction mechanism.


Pssm-ID: 238262  Cd Length: 140  Bit Score: 232.71  E-value: 3.10e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A        5 VNVINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSV 84
Cdd:cd00466   2 ILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTSI 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
2Y77_A       85 ALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEH 143
Cdd:cd00466  82 ALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALASL 140
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
4-144 4.79e-78

3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I enzyme, often found as part of a multifunctional protein, is described by TIGR01093. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 130160  Cd Length: 141  Bit Score: 227.61  E-value: 4.79e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A          4 IVNVINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTS 83
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
2Y77_A         84 VALRDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAEHV 144
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEIL 141
DHquinase_II pfam01220
Dehydroquinase class II;
7-141 2.46e-77

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 225.28  E-value: 2.46e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A          7 VINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSVAL 86
Cdd:pfam01220   4 VLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTSVAL 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
2Y77_A         87 RDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLA 141
Cdd:pfam01220  84 RDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
PRK13015 PRK13015
3-dehydroquinate dehydratase; Reviewed
7-142 1.84e-62

3-dehydroquinate dehydratase; Reviewed


Pssm-ID: 237270  Cd Length: 146  Bit Score: 188.25  E-value: 1.84e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Y77_A         7 VINGPNLGRLGRREPAVYGGTTHDELVALIEREAAELGLKAVVRQSDSEAQLLDWIHQAADAAEPVILNAGGLTHTSVAL 86
Cdd:PRK13015   6 VLNGPNLNLLGTREPAIYGHETLADVEALCRAAAEALGLEVEFRQSNHEGELIDWIHEARGDVAGIVINPGAYTHTSVAI 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
2Y77_A        87 RDACAELSAPLIEVHISNVHAREEFRRHSYLSPIATGVIVGLGIQGYLLALRYLAE 142
Cdd:PRK13015  86 RDALAALELPVIEVHISNVHAREAFRHHSYVSAIADGVICGLGTEGYRLALRRLAT 141
 
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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