![](files/infoQ.gif)
inositol oxygenase [Rattus norvegicus]
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
![](files/help.png)
Name | Accession | Description | Interval | E-value | |||||
MIOX | pfam05153 | Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ... |
37-285 | 5.16e-172 | |||||
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: 475.28 E-value: 5.16e-172
|
|||||||||
Name | Accession | Description | Interval | E-value | |||||
MIOX | pfam05153 | Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ... |
37-285 | 5.16e-172 | |||||
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: 475.28 E-value: 5.16e-172
|
|||||||||
Name | Accession | Description | Interval | E-value | |||||
MIOX | pfam05153 | Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ... |
37-285 | 5.16e-172 | |||||
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: 475.28 E-value: 5.16e-172
|
|||||||||
Blast search parameters | ||||
|