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Conserved domains on  [gi|530420829|ref|XP_005261982|]
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inositol oxygenase isoform X1 [Homo sapiens]

Protein Classification

inositol oxygenase( domain architecture ID 10524118)

inositol oxygenase catalyzes a unique four-electron dioxygen-dependent ring cleavage of myo-inositol to D-glucuronate

Graphical summary

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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 ...
 1-239 1.82e-166

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: 459.10  E-value: 1.82e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420829    1 MHTHQTVDFVRSKHAQFGGFSYKKMTVMEAVDLLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLG 80
Cdd:pfam05153  11 QHTKQTVDFVLKMREQFGKFTRAKMTIWEALELLNTLVDESDPDTDLPQIQHLLQTAEAIRRDHPDPDWMHLTGLIHDLG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420829   81 KVLALF-GEPQWAVVGDTFPVGCRPQASVVFcDSTFQDNPDLQDPRYSTELGMYQPHCGLDRVLMSWGHDEYMYQVMKFN 159
Cdd:pfam05153  91 KVLLFFgGEPQWAVVGDTFPVGCAFDESIVY-PESFKGNPDYNNPKYNTKLGIYQPGCGLDNVLMSWGHDEYLYQVLKFN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420829  160 KFSLPPEAFYMIRFHSFYPWHTGRDYQQLCSQQDLAMLPWVREFNKFDLYTKCPDLPDVDKLRPYYQGLIDKYCPGILSW 239
Cdd:pfam05153 170 KSTLPEEALYMIRYHSFYPWHREGAYTHLMNEEDEEMLKWVKAFNKYDLYSKSDDPPDVEALKPYYQSLIDKYFPGVLEW 249
 
Name Accession Description Interval E-value
MIOX pfam05153
Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ...
 1-239 1.82e-166

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: 459.10  E-value: 1.82e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420829    1 MHTHQTVDFVRSKHAQFGGFSYKKMTVMEAVDLLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLG 80
Cdd:pfam05153  11 QHTKQTVDFVLKMREQFGKFTRAKMTIWEALELLNTLVDESDPDTDLPQIQHLLQTAEAIRRDHPDPDWMHLTGLIHDLG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420829   81 KVLALF-GEPQWAVVGDTFPVGCRPQASVVFcDSTFQDNPDLQDPRYSTELGMYQPHCGLDRVLMSWGHDEYMYQVMKFN 159
Cdd:pfam05153  91 KVLLFFgGEPQWAVVGDTFPVGCAFDESIVY-PESFKGNPDYNNPKYNTKLGIYQPGCGLDNVLMSWGHDEYLYQVLKFN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420829  160 KFSLPPEAFYMIRFHSFYPWHTGRDYQQLCSQQDLAMLPWVREFNKFDLYTKCPDLPDVDKLRPYYQGLIDKYCPGILSW 239
Cdd:pfam05153 170 KSTLPEEALYMIRYHSFYPWHREGAYTHLMNEEDEEMLKWVKAFNKYDLYSKSDDPPDVEALKPYYQSLIDKYFPGVLEW 249
 
Name Accession Description Interval E-value
MIOX pfam05153
Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ...
 1-239 1.82e-166

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: 459.10  E-value: 1.82e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420829    1 MHTHQTVDFVRSKHAQFGGFSYKKMTVMEAVDLLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLG 80
Cdd:pfam05153  11 QHTKQTVDFVLKMREQFGKFTRAKMTIWEALELLNTLVDESDPDTDLPQIQHLLQTAEAIRRDHPDPDWMHLTGLIHDLG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420829   81 KVLALF-GEPQWAVVGDTFPVGCRPQASVVFcDSTFQDNPDLQDPRYSTELGMYQPHCGLDRVLMSWGHDEYMYQVMKFN 159
Cdd:pfam05153  91 KVLLFFgGEPQWAVVGDTFPVGCAFDESIVY-PESFKGNPDYNNPKYNTKLGIYQPGCGLDNVLMSWGHDEYLYQVLKFN 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530420829  160 KFSLPPEAFYMIRFHSFYPWHTGRDYQQLCSQQDLAMLPWVREFNKFDLYTKCPDLPDVDKLRPYYQGLIDKYCPGILSW 239
Cdd:pfam05153 170 KSTLPEEALYMIRYHSFYPWHREGAYTHLMNEEDEEMLKWVKAFNKYDLYSKSDDPPDVEALKPYYQSLIDKYFPGVLEW 249
 
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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