NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|243065266|gb|EES47452|]
View 

3-dehydroquinate dehydratase, type II [Burkholderia mallei PRL-20]

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;
58-204 8.80e-100

type II 3-dehydroquinate dehydratase;


:

Pssm-ID: 235443  Cd Length: 146  Bit Score: 285.02  E-value: 8.80e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266  58 MTRLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGsDGTAFILINPAAYT 137
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEAR-DGADGIIINPGAYT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 243065266 138 HTSVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDKLQGA 204
Cdd:PRK05395  80 HTSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLSAS 146
 
Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
58-204 8.80e-100

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 285.02  E-value: 8.80e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266  58 MTRLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGsDGTAFILINPAAYT 137
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEAR-DGADGIIINPGAYT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 243065266 138 HTSVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDKLQGA 204
Cdd:PRK05395  80 HTSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLSAS 146
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
58-202 7.83e-96

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: 274.98  E-value: 7.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266  58 MTRLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGsDGTAFILINPAAYT 137
Cdd:COG0757    1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEAR-DGVDGIIINPGAYT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 243065266 138 HTSVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDKLQ 202
Cdd:COG0757   80 HTSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAELLS 144
DHquinase_II pfam01220
Dehydroquinase class II;
60-198 1.16e-93

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 269.20  E-value: 1.16e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266   60 RLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGsDGTAFILINPAAYTHT 139
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEAR-GGVDGIIINPGAYTHT 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 243065266  140 SVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYAL 198
Cdd:pfam01220  80 SVALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
60-200 2.06e-86

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: 2.06e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266  60 RLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGsDGTAFILINPAAYTHT 139
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEAR-DGADGIIINPGAYTHT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 243065266 140 SVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDK 200
Cdd:cd00466   80 SIALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALASL 140
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
60-201 2.98e-73

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: 217.98  E-value: 2.98e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266   60 RLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQaaGSDGTA-FILINPAAYTH 138
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIH--EAEGQYdGIIINPGALTH 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 243065266  139 TSVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDKL 201
Cdd:TIGR01088  79 TSVALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEIL 141
 
Name Accession Description Interval E-value
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
58-204 8.80e-100

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 285.02  E-value: 8.80e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266  58 MTRLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGsDGTAFILINPAAYT 137
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEAR-DGADGIIINPGAYT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 243065266 138 HTSVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDKLQGA 204
Cdd:PRK05395  80 HTSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAERLSAS 146
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
58-202 7.83e-96

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: 274.98  E-value: 7.83e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266  58 MTRLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGsDGTAFILINPAAYT 137
Cdd:COG0757    1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEAR-DGVDGIIINPGAYT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 243065266 138 HTSVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDKLQ 202
Cdd:COG0757   80 HTSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAELLS 144
DHquinase_II pfam01220
Dehydroquinase class II;
60-198 1.16e-93

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 269.20  E-value: 1.16e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266   60 RLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGsDGTAFILINPAAYTHT 139
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEAR-GGVDGIIINPGAYTHT 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 243065266  140 SVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYAL 198
Cdd:pfam01220  80 SVALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
60-200 2.06e-86

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: 2.06e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266  60 RLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGsDGTAFILINPAAYTHT 139
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEAR-DGADGIIINPGAYTHT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 243065266 140 SVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDK 200
Cdd:cd00466   80 SIALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALASL 140
PRK13015 PRK13015
3-dehydroquinate dehydratase; Reviewed
58-204 9.26e-74

3-dehydroquinate dehydratase; Reviewed


Pssm-ID: 237270  Cd Length: 146  Bit Score: 219.45  E-value: 9.26e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266  58 MTRLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQAAGSDGTAfILINPAAYT 137
Cdd:PRK13015   1 KGKILVLNGPNLNLLGTREPAIYGHETLADVEALCRAAAEALGLEVEFRQSNHEGELIDWIHEARGDVAG-IVINPGAYT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 243065266 138 HTSVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDKLQGA 204
Cdd:PRK13015  80 HTSVAIRDALAALELPVIEVHISNVHAREAFRHHSYVSAIADGVICGLGTEGYRLALRRLATLLQAG 146
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
60-201 2.98e-73

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: 217.98  E-value: 2.98e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 243065266   60 RLLVLHGPNLNLLGTREPEVYGRVTLEQIDQALAARAQEAGAELESFQSNHEGALVDRVQaaGSDGTA-FILINPAAYTH 138
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIH--EAEGQYdGIIINPGALTH 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 243065266  139 TSVAIRDALAGVGIPFVEIHLSNVHRREPFRHHSYFSDQAEGVICGLGWKGYLYALEYALDKL 201
Cdd:TIGR01088  79 TSVALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEIL 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH