MULTISPECIES: type II 3-dehydroquinate dehydratase [Bacteroides]
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
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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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Blast search parameters | ||||
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