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Conserved domains on  [gi|492395449|ref|WP_005830766|]
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MULTISPECIES: type II 3-dehydroquinate dehydratase [Bacteroides]

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;
2-136 7.72e-87

Dehydroquinase class II;


:

Pssm-ID: 460118  Cd Length: 138  Bit Score: 249.17  E-value: 7.72e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449    2 RIQIINGPNINLLGKREPSIYGSVTFEDYLAELRKKYAD--VQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHTS 79
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAElgVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 492395449   80 IALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEAL 136
Cdd:pfam01220  81 VALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEAL 137
 
Name Accession Description Interval E-value
DHquinase_II pfam01220
Dehydroquinase class II;
2-136 7.72e-87

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 249.17  E-value: 7.72e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449    2 RIQIINGPNINLLGKREPSIYGSVTFEDYLAELRKKYAD--VQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHTS 79
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAElgVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 492395449   80 IALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEAL 136
Cdd:pfam01220  81 VALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEAL 137
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-139 1.92e-86

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: 248.41  E-value: 1.92e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449   1 MRIQIINGPNINLLGKREPSIYGSVTFEDYLAELRKKYA--DVQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHT 78
Cdd:COG0757    2 MKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAelGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTHT 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492395449  79 SIALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEALKDY 139
Cdd:COG0757   82 SVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAEL 142
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
1-139 1.85e-85

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 246.12  E-value: 1.85e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449   1 MRIQIINGPNINLLGKREPSIYGSVTFEDYLAELRK--KYADVQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHT 78
Cdd:PRK05395   2 MKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEeaAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTHT 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492395449  79 SIALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEALKDY 139
Cdd:PRK05395  82 SVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAER 142
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
2-139 1.86e-80

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: 233.10  E-value: 1.86e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449   2 RIQIINGPNINLLGKREPSIYGSVTFEDYLAELRKKYA--DVQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHTS 79
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAelGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449  80 IALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEALKDY 139
Cdd:cd00466   81 IALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALASL 140
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
2-139 1.22e-64

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: 193.33  E-value: 1.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449    2 RIQIINGPNINLLGKREPSIYGSVTFEDYLAELRK--KYADVQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHTS 79
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETfaAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449   80 IALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEALKDY 139
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEI 140
 
Name Accession Description Interval E-value
DHquinase_II pfam01220
Dehydroquinase class II;
2-136 7.72e-87

Dehydroquinase class II;


Pssm-ID: 460118  Cd Length: 138  Bit Score: 249.17  E-value: 7.72e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449    2 RIQIINGPNINLLGKREPSIYGSVTFEDYLAELRKKYAD--VQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHTS 79
Cdd:pfam01220   1 KILVLNGPNLNLLGTREPEIYGSTTLADIEAALRELAAElgVELEFFQSNHEGELIDRIHEARGGVDGIIINPGAYTHTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 492395449   80 IALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEAL 136
Cdd:pfam01220  81 VALRDALAAVEIPVVEVHLSNIHAREEFRHHSYISPVAVGVIAGFGADGYLLALEAL 137
AroQ COG0757
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1-139 1.92e-86

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: 248.41  E-value: 1.92e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449   1 MRIQIINGPNINLLGKREPSIYGSVTFEDYLAELRKKYA--DVQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHT 78
Cdd:COG0757    2 MKILVLNGPNLNLLGTREPEIYGSTTLADIEALLRELAAelGVEVEFFQSNHEGELIDWIHEARDGVDGIIINPGAYTHT 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492395449  79 SIALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEALKDY 139
Cdd:COG0757   82 SVALRDALAAVEIPVIEVHLSNIHAREEFRHHSYISPVATGVIAGFGADGYLLALRALAEL 142
PRK05395 PRK05395
type II 3-dehydroquinate dehydratase;
1-139 1.85e-85

type II 3-dehydroquinate dehydratase;


Pssm-ID: 235443  Cd Length: 146  Bit Score: 246.12  E-value: 1.85e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449   1 MRIQIINGPNINLLGKREPSIYGSVTFEDYLAELRK--KYADVQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHT 78
Cdd:PRK05395   2 MKILVLNGPNLNLLGTREPEIYGSTTLADIEALLEEeaAELGVELEFFQSNHEGELIDRIHEARDGADGIIINPGAYTHT 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492395449  79 SIALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEALKDY 139
Cdd:PRK05395  82 SVALRDALAAVSIPVIEVHLSNIHAREEFRHHSYISDVAVGVICGFGADGYLLALEALAER 142
DHQase_II cd00466
Dehydroquinase (DHQase), type II. Dehydroquinase (or 3-dehydroquinate dehydratase) catalyzes ...
2-139 1.86e-80

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: 233.10  E-value: 1.86e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449   2 RIQIINGPNINLLGKREPSIYGSVTFEDYLAELRKKYA--DVQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHTS 79
Cdd:cd00466    1 KILVLNGPNLNLLGKREPEIYGTTTLADIEALLRELAAelGVEVEFFQSNHEGELIDWIHEARDGADGIIINPGAYTHTS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449  80 IALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEALKDY 139
Cdd:cd00466   81 IALRDALAAVSIPVIEVHISNIHAREEFRHHSVISPVATGVIAGLGADGYRLALEALASL 140
aroQ TIGR01088
3-dehydroquinate dehydratase, type II; This model specifies the type II enzyme. The type I ...
2-139 1.22e-64

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: 193.33  E-value: 1.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449    2 RIQIINGPNINLLGKREPSIYGSVTFEDYLAELRK--KYADVQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHTS 79
Cdd:TIGR01088   1 KILVLNGPNLNMLGLREPGVYGSQTLEEIVEIIETfaAQLNVELEFFQSNSEGQLIDKIHEAEGQYDGIIINPGALTHTS 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449   80 IALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEALKDY 139
Cdd:TIGR01088  81 VALRDALAAVSLPVVEVHLSNVHAREEFRHHSYTAPVAGGVIVGLGAQGYLLALRYLVEI 140
PRK13015 PRK13015
3-dehydroquinate dehydratase; Reviewed
1-136 4.33e-60

3-dehydroquinate dehydratase; Reviewed


Pssm-ID: 237270  Cd Length: 146  Bit Score: 182.09  E-value: 4.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492395449   1 MRIQIINGPNINLLGKREPSIYGSVTFEDYLAELRKKYA--DVQIDYFQSNIEGELIDKIQQVGFDVDGIILNAGAYTHT 78
Cdd:PRK13015   2 GKILVLNGPNLNLLGTREPAIYGHETLADVEALCRAAAEalGLEVEFRQSNHEGELIDWIHEARGDVAGIVINPGAYTHT 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492395449  79 SIALQDAIRSVTSPVVEVHISNVHAREAFRHVSMISCACKGVILGFGLNSYRLAMEAL 136
Cdd:PRK13015  82 SVAIRDALAALELPVIEVHISNVHAREAFRHHSYVSAIADGVICGLGTEGYRLALRRL 139
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
21-80 5.09e-03

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 35.38  E-value: 5.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492395449  21 IYGSVT-FEDYLAELRKKYAdVQIDYFQSNIEG-----ELIDKIQQVGFDVDGIILNAGAYTHTSI 80
Cdd:cd05352   38 IYNSAPrAEEKAEELAKKYG-VKTKAYKCDVSSqesveKTFKQIQKDFGKIDILIANAGITVHKPA 102
 
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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