NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|258583963|gb|EEW08754|]
View 

3-dehydroquinate dehydratase [Vibrio mimicus VM603]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
4-149 2.26e-98

type II 3-dehydroquinate dehydratase;


:

Pssm-ID: 235443  Cd Length: 146  Bit Score: 278.86  E-value: 2.26e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963   4 KSRILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTH 83
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583963  84 TSVALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIRALQAK 149
Cdd:PRK05395  81 TSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLSAS 146
 
Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
4-149 2.26e-98

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 278.86  E-value: 2.26e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963   4 KSRILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTH 83
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583963  84 TSVALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIRALQAK 149
Cdd:PRK05395  81 TSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLSAS 146
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
4-148 7.47e-94

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: 267.67  E-value: 7.47e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963   4 KSRILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTH 83
Cdd:COG0757    1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583963  84 TSVALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIRALQA 148
Cdd:COG0757   81 TSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAELLSK 145
DHquinase_II pfam01220
Dehydroquinase class II;
6-143 1.13e-91

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 261.88  E-value: 1.13e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963    6 RILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTHTS 85
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 258583963   86 VALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAI 143
Cdd:pfam01220  81 VALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
6-144 2.68e-84

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: 243.11  E-value: 2.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963   6 RILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTHTS 85
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTS 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 258583963  86 VALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIR 144
Cdd:cd00466   81 IALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALAS 139
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
6-146 8.00e-84

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: 242.25  E-value: 8.00e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963    6 RILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTHTS 85
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258583963   86 VALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIRAL 146
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEIL 141
 
Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
4-149 2.26e-98

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 278.86  E-value: 2.26e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963   4 KSRILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTH 83
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583963  84 TSVALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIRALQAK 149
Cdd:PRK05395  81 TSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLSAS 146
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
4-148 7.47e-94

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: 267.67  E-value: 7.47e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963   4 KSRILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTH 83
Cdd:COG0757    1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 258583963  84 TSVALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIRALQA 148
Cdd:COG0757   81 TSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAELLSK 145
DHquinase_II pfam01220
Dehydroquinase class II;
6-143 1.13e-91

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 261.88  E-value: 1.13e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963    6 RILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTHTS 85
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 258583963   86 VALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAI 143
Cdd:pfam01220  81 VALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
6-144 2.68e-84

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: 243.11  E-value: 2.68e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963   6 RILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTHTS 85
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTS 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 258583963  86 VALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIR 144
Cdd:cd00466   81 IALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALAS 139
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
6-146 8.00e-84

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: 242.25  E-value: 8.00e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963    6 RILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTHTS 85
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 258583963   86 VALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIRAL 146
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEIL 141
PRK13015 PRK13015
3-dehydroquinate dehydratase; Reviewed
4-149 3.06e-74

3-dehydroquinate dehydratase; Reviewed


Pssm-ID: 237270  Cd Length: 146  Bit Score: 218.30  E-value: 3.06e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963   4 KSRILVLNGPNLNLLGLREPAHYGSQTLEQIVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPAAFTH 83
Cdd:PRK13015   1 KGKILVLNGPNLNLLGTREPAIYGHETLADVEALCRAAAEALGLEVEFRQSNHEGELIDWIHEARGDVAGIVINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 258583963  84 TSVALRDALLGVAIPFIEVHLSNVHAREPFRHHSYLSDKAQGVICGLGAQGYEFALSAAIRALQAK 149
Cdd:PRK13015  81 TSVAIRDALAALELPVIEVHISNVHAREAFRHHSYVSAIADGVICGLGTEGYRLALRRLATLLQAG 146
COG2984 COG2984
ABC-type uncharacterized transport system, periplasmic component [General function prediction ...
34-147 2.77e-03

ABC-type uncharacterized transport system, periplasmic component [General function prediction only];


Pssm-ID: 442223  Cd Length: 284  Bit Score: 36.43  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 258583963  34 IVSTLRDQAQKAGIELEHLQSNREYELIEAIHQAFGKVDFIIINPaafTHTSVALRDALLGVA----IPFIEVHLSNVha 109
Cdd:COG2984  149 QVEELKKAAKKLGLELVEATVTSSNEIQQALQSLAGKVDAIYVPT---DNTVVSALEAIAKVAarakIPVFGGDDSSV-- 223
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 258583963 110 repfrhhsylsdkAQGVICGLGAQGYEFALSAAIRALQ 147
Cdd:COG2984  224 -------------KAGALAGYGIDYYELGRQAAEMALR 248
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH