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Conserved domains on  [gi|240296685|gb|EER47296|]
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3-dehydroquinate dehydratase [Actinobacillus minor NM305]

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;
1-146 3.59e-100

type II 3-dehydroquinate dehydratase;


:

Pssm-ID: 235443  Cd Length: 146  Bit Score: 283.48  E-value: 3.59e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685   1 MKKILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTH 80
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240296685  81 TSVAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVISQLEKE 146
Cdd:PRK05395  81 TSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLSAS 146
 
Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
1-146 3.59e-100

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 283.48  E-value: 3.59e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685   1 MKKILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTH 80
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240296685  81 TSVAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVISQLEKE 146
Cdd:PRK05395  81 TSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLSAS 146
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-145 1.03e-95

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: 272.29  E-value: 1.03e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685   1 MKKILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTH 80
Cdd:COG0757    1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240296685  81 TSVAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVISQLEK 145
Cdd:COG0757   81 TSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAELLSK 145
DHquinase_II pfam01220
Dehydroquinase class II;
3-140 3.24e-93

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 265.73  E-value: 3.24e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685    3 KILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTHTS 82
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240296685   83 VAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVI 140
Cdd:pfam01220  81 VALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
3-141 2.09e-87

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: 251.20  E-value: 2.09e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685   3 KILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTHTS 82
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTS 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 240296685  83 VAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVIS 141
Cdd:cd00466   81 IALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALAS 139
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
3-143 2.64e-76

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: 222.99  E-value: 2.64e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685    3 KILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTHTS 82
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240296685   83 VAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVISQL 143
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEIL 141
 
Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
1-146 3.59e-100

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 283.48  E-value: 3.59e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685   1 MKKILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTH 80
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240296685  81 TSVAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVISQLEKE 146
Cdd:PRK05395  81 TSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLSAS 146
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-145 1.03e-95

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: 272.29  E-value: 1.03e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685   1 MKKILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTH 80
Cdd:COG0757    1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240296685  81 TSVAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVISQLEK 145
Cdd:COG0757   81 TSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAELLSK 145
DHquinase_II pfam01220
Dehydroquinase class II;
3-140 3.24e-93

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 265.73  E-value: 3.24e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685    3 KILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTHTS 82
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 240296685   83 VAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVI 140
Cdd:pfam01220  81 VALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
3-141 2.09e-87

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: 251.20  E-value: 2.09e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685   3 KILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTHTS 82
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTS 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 240296685  83 VAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVIS 141
Cdd:cd00466   81 IALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALAS 139
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
3-143 2.64e-76

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: 222.99  E-value: 2.64e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685    3 KILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTHTS 82
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240296685   83 VAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVISQL 143
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEIL 141
PRK13015 PRK13015
3-dehydroquinate dehydratase; Reviewed
1-146 1.02e-74

3-dehydroquinate dehydratase; Reviewed


Pssm-ID: 237270  Cd Length: 146  Bit Score: 219.07  E-value: 1.02e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240296685   1 MKKILLLNGPNLNMLGKREPHIYGSQTLADIENHLQQLAEARGYCLEYFQANGEEPIINRIHQAFQNTDFIIINPGAFTH 80
Cdd:PRK13015   1 KGKILVLNGPNLNLLGTREPAIYGHETLADVEALCRAAAEALGLEVEFRQSNHEGELIDWIHEARGDVAGIVINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240296685  81 TSVAIRDALLAVAIPFVEVHLSNVHAREPFRHHSYLSDVAKGVICGLGAKGYEYALDFVISQLEKE 146
Cdd:PRK13015  81 TSVAIRDALAALELPVIEVHISNVHAREAFRHHSYVSAIADGVICGLGTEGYRLALRRLATLLQAG 146
 
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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