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Conserved domains on  [gi|1952624783|ref|WP_199728725|]
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type II 3-dehydroquinate dehydratase [Corallococcus sp. CA053C]

Protein Classification

type II 3-dehydroquinate dehydratase( domain architecture ID 10472006)

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
DHquinase_II pfam01220
Dehydroquinase class II;
4-132 6.24e-48

Dehydroquinase class II;


:

Pssm-ID: 460118  Cd Length: 138  Bit Score: 157.49  E-value: 6.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   4 KLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FTS 80
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSttLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYtHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952624783  81 YALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALETF 132
Cdd:pfam01220  81 VALRDALAAVEIPVVEVhLSNIHAREefrhhSYISPVAVGVIAGF-GADGYLLALEAL 137
 
Name Accession Description Interval E-value
DHquinase_II pfam01220
Dehydroquinase class II;
4-132 6.24e-48

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 157.49  E-value: 6.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   4 KLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FTS 80
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSttLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYtHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952624783  81 YALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALETF 132
Cdd:pfam01220  81 VALRDALAAVEIPVVEVhLSNIHAREefrhhSYISPVAVGVIAGF-GADGYLLALEAL 137
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
3-130 8.39e-39

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: 134.00  E-value: 8.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   3 MKLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FT 79
Cdd:COG0757     2 MKILVLNGPNLNLLGTREPEIYGSttLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYtHT 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952624783  80 SYALKEALEAVGLPAIEVLLKPP-ARE-----SVVAEACAMQVLGLhGFEPYLQALE 130
Cdd:COG0757    82 SVALRDALAAVEIPVIEVHLSNIhAREefrhhSYISPVATGVIAGF-GADGYLLALR 137
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
3-130 1.64e-37

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 130.94  E-value: 1.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   3 MKLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FT 79
Cdd:PRK05395    2 MKILVLNGPNLNLLGTREPEIYGSttLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYtHT 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952624783  80 SYALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALE 130
Cdd:PRK05395   82 SVALRDALAAVSIPVIEVhLSNIHAREefrhhSYISDVAVGVICGF-GADGYLLALE 137
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
4-130 1.36e-36

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: 128.32  E-value: 1.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   4 KLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FTS 80
Cdd:cd00466     1 KILVLNGPNLNLLGKREPEIYGTttLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYtHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952624783  81 YALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALE 130
Cdd:cd00466    81 IALRDALAAVSIPVIEVhISNIHAREefrhhSVISPVATGVIAGL-GADGYRLALE 135
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
4-130 1.12e-29

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: 110.12  E-value: 1.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   4 KLLVLHGPNLNLLGEREDAAGGRLS--DLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FTS 80
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTleEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALtHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952624783  81 YALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALE 130
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVhLSNVHAREefrhhSYTAPVAGGVIVGL-GAQGYLLALR 135
 
Name Accession Description Interval E-value
DHquinase_II pfam01220
Dehydroquinase class II;
4-132 6.24e-48

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 157.49  E-value: 6.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   4 KLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FTS 80
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSttLADIEAALRELAAELGVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYtHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952624783  81 YALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALETF 132
Cdd:pfam01220  81 VALRDALAAVEIPVVEVhLSNIHAREefrhhSYISPVAVGVIAGF-GADGYLLALEAL 137
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
3-130 8.39e-39

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: 134.00  E-value: 8.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   3 MKLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FT 79
Cdd:COG0757     2 MKILVLNGPNLNLLGTREPEIYGSttLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYtHT 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952624783  80 SYALKEALEAVGLPAIEVLLKPP-ARE-----SVVAEACAMQVLGLhGFEPYLQALE 130
Cdd:COG0757    82 SVALRDALAAVEIPVIEVHLSNIhAREefrhhSYISPVATGVIAGF-GADGYLLALR 137
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
3-130 1.64e-37

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 130.94  E-value: 1.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   3 MKLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FT 79
Cdd:PRK05395    2 MKILVLNGPNLNLLGTREPEIYGSttLADIEALLEEEAAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYtHT 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1952624783  80 SYALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALE 130
Cdd:PRK05395   82 SVALRDALAAVSIPVIEVhLSNIHAREefrhhSYISDVAVGVICGF-GADGYLLALE 137
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
4-130 1.36e-36

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: 128.32  E-value: 1.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   4 KLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FTS 80
Cdd:cd00466     1 KILVLNGPNLNLLGKREPEIYGTttLADIEALLRELAAELGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYtHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952624783  81 YALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALE 130
Cdd:cd00466    81 IALRDALAAVSIPVIEVhISNIHAREefrhhSVISPVATGVIAGL-GADGYRLALE 135
PRK13015 PRK13015
3-dehydroquinate dehydratase; Reviewed
3-134 1.13e-30

3-dehydroquinate dehydratase; Reviewed


Pssm-ID: 237270  Cd Length: 146  Bit Score: 113.14  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   3 MKLLVLHGPNLNLLGEREDAAGGR--LSDLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FT 79
Cdd:PRK13015    2 GKILVLNGPNLNLLGTREPAIYGHetLADVEALCRAAAEALGLEVEFRQSNHEGELIDWIHEARGDVAGIVINPGAYtHT 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952624783  80 SYALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALETFSS 134
Cdd:PRK13015   82 SVAIRDALAALELPVIEVhISNVHAREafrhhSYVSAIADGVICGL-GTEGYRLALRRLAT 141
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
4-130 1.12e-29

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: 110.12  E-value: 1.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952624783   4 KLLVLHGPNLNLLGEREDAAGGRLS--DLDAALRAKAKALGLELKIVQSNHEGVLIDTLHAERKNVEGILINPAGL-FTS 80
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTleEIVEIIETFAAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALtHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952624783  81 YALKEALEAVGLPAIEV-LLKPPARE-----SVVAEACAMQVLGLhGFEPYLQALE 130
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVhLSNVHAREefrhhSYTAPVAGGVIVGL-GAQGYLLALR 135
 
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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