myo-inositol oxygenase 1 [Arabidopsis thaliana]
inositol oxygenase( domain architecture ID 10524118)
inositol oxygenase catalyzes a unique four-electron dioxygen-dependent ring cleavage of myo-inositol to D-glucuronate
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
MIOX | pfam05153 | Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ... |
61-309 | 1.75e-167 | |||||
Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first committed step in the glucuronate-xylulose pathway, It is a di-iron oxygenase with a key role in inositol metabolism. The structure reveals a monomeric, single-domain protein with a mostly helical fold that is distantly related to the diverse HD domain superfamily. The structural core is of five alpha-helices that contribute six ligands, four His and two Asp, to the di-iron centre where the two iron atoms are bridged by a putative hydroxide ion and one of the Asp ligands. The substrate is myo-inositol is bound in a terminal substrate-binding mode to a di-iron cluster. Within the structure are two additional proteinous lids that cover and shield the enzyme's active site. : Pssm-ID: 461562 Cd Length: 249 Bit Score: 464.87 E-value: 1.75e-167
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Name | Accession | Description | Interval | E-value | |||||
MIOX | pfam05153 | Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ... |
61-309 | 1.75e-167 | |||||
Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first committed step in the glucuronate-xylulose pathway, It is a di-iron oxygenase with a key role in inositol metabolism. The structure reveals a monomeric, single-domain protein with a mostly helical fold that is distantly related to the diverse HD domain superfamily. The structural core is of five alpha-helices that contribute six ligands, four His and two Asp, to the di-iron centre where the two iron atoms are bridged by a putative hydroxide ion and one of the Asp ligands. The substrate is myo-inositol is bound in a terminal substrate-binding mode to a di-iron cluster. Within the structure are two additional proteinous lids that cover and shield the enzyme's active site. Pssm-ID: 461562 Cd Length: 249 Bit Score: 464.87 E-value: 1.75e-167
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Name | Accession | Description | Interval | E-value | |||||
MIOX | pfam05153 | Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ... |
61-309 | 1.75e-167 | |||||
Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first committed step in the glucuronate-xylulose pathway, It is a di-iron oxygenase with a key role in inositol metabolism. The structure reveals a monomeric, single-domain protein with a mostly helical fold that is distantly related to the diverse HD domain superfamily. The structural core is of five alpha-helices that contribute six ligands, four His and two Asp, to the di-iron centre where the two iron atoms are bridged by a putative hydroxide ion and one of the Asp ligands. The substrate is myo-inositol is bound in a terminal substrate-binding mode to a di-iron cluster. Within the structure are two additional proteinous lids that cover and shield the enzyme's active site. Pssm-ID: 461562 Cd Length: 249 Bit Score: 464.87 E-value: 1.75e-167
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Blast search parameters | ||||
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