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Conserved domains on  [gi|256580497|gb|ACU91632|]
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3-dehydroquinate dehydratase, type II [Capnocytophaga ochracea DSM 7271]

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
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-139 2.62e-72

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: 212.58  E-value: 2.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497   1 MKKIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHRKYP--DIELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTH 78
Cdd:COG0757    1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAelGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256580497  79 TSIAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFID 139
Cdd:COG0757   81 TSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAE 141
 
Name Accession Description Interval E-value
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-139 2.62e-72

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: 212.58  E-value: 2.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497   1 MKKIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHRKYP--DIELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTH 78
Cdd:COG0757    1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAelGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256580497  79 TSIAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFID 139
Cdd:COG0757   81 TSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAE 141
DHquinase_II pfam01220
Dehydroquinase class II;
3-138 3.84e-71

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 209.49  E-value: 3.84e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497    3 KIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHRKYPD--IELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTHTS 80
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAElgVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 256580497   81 IAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFI 138
Cdd:pfam01220  81 VALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
1-139 2.69e-69

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 205.29  E-value: 2.69e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497   1 MKKIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHR--KYPDIELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTH 78
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEeaAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256580497  79 TSIAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFID 139
Cdd:PRK05395  81 TSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAE 141
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
3-139 1.59e-64

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: 193.04  E-value: 1.59e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497   3 KIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHRKYP--DIELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTHTS 80
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAelGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTS 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 256580497  81 IAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFID 139
Cdd:cd00466   81 IALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALAS 139
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
3-139 1.05e-53

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: 165.59  E-value: 1.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497    3 KIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHR--KYPDIELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTHTS 80
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETfaAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 256580497   81 IAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFID 139
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVE 139
 
Name Accession Description Interval E-value
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-139 2.62e-72

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: 212.58  E-value: 2.62e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497   1 MKKIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHRKYP--DIELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTH 78
Cdd:COG0757    1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAelGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256580497  79 TSIAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFID 139
Cdd:COG0757   81 TSVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAE 141
DHquinase_II pfam01220
Dehydroquinase class II;
3-138 3.84e-71

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 209.49  E-value: 3.84e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497    3 KIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHRKYPD--IELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTHTS 80
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAElgVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 256580497   81 IAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFI 138
Cdd:pfam01220  81 VALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEALA 138
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
1-139 2.69e-69

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 205.29  E-value: 2.69e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497   1 MKKIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHR--KYPDIELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTH 78
Cdd:PRK05395   1 MMKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEeaAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTH 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256580497  79 TSIAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFID 139
Cdd:PRK05395  81 TSVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAE 141
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
3-139 1.59e-64

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: 193.04  E-value: 1.59e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497   3 KIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHRKYP--DIELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTHTS 80
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAelGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTS 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 256580497  81 IAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFID 139
Cdd:cd00466   81 IALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALAS 139
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
3-139 1.05e-53

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: 165.59  E-value: 1.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497    3 KIIIINGPNLNLLGIREPSVYGNQTFEDYLKELHR--KYPDIELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYTHTS 80
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETfaAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 256580497   81 IAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFID 139
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVE 139
PRK13015 PRK13015
3-dehydroquinate dehydratase; Reviewed
1-138 3.20e-50

3-dehydroquinate dehydratase; Reviewed


Pssm-ID: 237270  Cd Length: 146  Bit Score: 157.05  E-value: 3.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256580497   1 MKKIIIINGPNLNLLGIREPSVYGNQTFEDyLKELHRKYPD---IELYYFQSNYEGALIDKLHQIGFEYDGIILNAGAYT 77
Cdd:PRK13015   1 KGKILVLNGPNLNLLGTREPAIYGHETLAD-VEALCRAAAEalgLEVEFRQSNHEGELIDWIHEARGDVAGIVINPGAYT 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256580497  78 HTSIAVADAVAAITTPVVEVHISNTFTRETFRHQSFLSPVVKGVIGGFGLKSYELALQSFI 138
Cdd:PRK13015  80 HTSVAIRDALAALELPVIEVHISNVHAREAFRHHSYVSAIADGVICGLGTEGYRLALRRLA 140
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
2-70 3.79e-03

ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 35.96  E-value: 3.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256580497   2 KKIIIINGPNlnllgIREPSVYGNQTFEDYLKELHRKYPDIELYYFQSNYEGA--LIDKLHQIGFEYDGII 70
Cdd:cd06291  113 KKILHIGGPS-----NNSPANERYRGFEDALKEAGIEYEIIEIDENDFSEEDAyeLAKELLEKYPDIDGIF 178
 
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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