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Conserved domains on  [gi|47523014|ref|NP_999267|]
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inositol oxygenase [Sus scrofa]

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 ...
 34-282 8.56e-168

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: 464.49  E-value: 8.56e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523014    34 LDRVFRTYKLMHTWQTVDFVRKKHAQFGGFSYKRMTVLEAVDMLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWF 113
Cdd:pfam05153   1 KDRVREFYKEQHTKQTVDFVLKMREQFGKFTRAKMTIWEALELLNTLVDESDPDTDLPQIQHLLQTAEAIRRDHPDPDWM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523014   114 HLVGLLHDLGKVLVL-AGEPQWAVVGDTFPVGCRPQASVVFcDSTFQDNPDLQDPVYSTELGMYQPHCGLENALMSWGHD 192
Cdd:pfam05153  81 HLTGLIHDLGKVLLFfGGEPQWAVVGDTFPVGCAFDESIVY-PESFKGNPDYNNPKYNTKLGIYQPGCGLDNVLMSWGHD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523014   193 EYMYQMMKFNKFSLPGEAFYIIRFHSFYPWHTGGDYRQLCNEQDLAMLPWVQEFNKFDLYTKGSDMPDVDELRPYYQGLI 272
Cdd:pfam05153 160 EYLYQVLKFNKSTLPEEALYMIRYHSFYPWHREGAYTHLMNEEDEEMLKWVKAFNKYDLYSKSDDPPDVEALKPYYQSLI 239

                         250
                  ....*....|
gi 47523014   273 DKYCPGVLCW 282
Cdd:pfam05153 240 DKYFPGVLEW 249
 
Name Accession Description Interval E-value
MIOX pfam05153
Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ...
 34-282 8.56e-168

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: 464.49  E-value: 8.56e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523014    34 LDRVFRTYKLMHTWQTVDFVRKKHAQFGGFSYKRMTVLEAVDMLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWF 113
Cdd:pfam05153   1 KDRVREFYKEQHTKQTVDFVLKMREQFGKFTRAKMTIWEALELLNTLVDESDPDTDLPQIQHLLQTAEAIRRDHPDPDWM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523014   114 HLVGLLHDLGKVLVL-AGEPQWAVVGDTFPVGCRPQASVVFcDSTFQDNPDLQDPVYSTELGMYQPHCGLENALMSWGHD 192
Cdd:pfam05153  81 HLTGLIHDLGKVLLFfGGEPQWAVVGDTFPVGCAFDESIVY-PESFKGNPDYNNPKYNTKLGIYQPGCGLDNVLMSWGHD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523014   193 EYMYQMMKFNKFSLPGEAFYIIRFHSFYPWHTGGDYRQLCNEQDLAMLPWVQEFNKFDLYTKGSDMPDVDELRPYYQGLI 272
Cdd:pfam05153 160 EYLYQVLKFNKSTLPEEALYMIRYHSFYPWHREGAYTHLMNEEDEEMLKWVKAFNKYDLYSKSDDPPDVEALKPYYQSLI 239

                         250
                  ....*....|
gi 47523014   273 DKYCPGVLCW 282
Cdd:pfam05153 240 DKYFPGVLEW 249
 
Name Accession Description Interval E-value
MIOX pfam05153
Myo-inositol oxygenase; MIOX is the enzyme myo-inositol oxygenase. It catalyzes the first ...
 34-282 8.56e-168

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: 464.49  E-value: 8.56e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523014    34 LDRVFRTYKLMHTWQTVDFVRKKHAQFGGFSYKRMTVLEAVDMLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWF 113
Cdd:pfam05153   1 KDRVREFYKEQHTKQTVDFVLKMREQFGKFTRAKMTIWEALELLNTLVDESDPDTDLPQIQHLLQTAEAIRRDHPDPDWM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523014   114 HLVGLLHDLGKVLVL-AGEPQWAVVGDTFPVGCRPQASVVFcDSTFQDNPDLQDPVYSTELGMYQPHCGLENALMSWGHD 192
Cdd:pfam05153  81 HLTGLIHDLGKVLLFfGGEPQWAVVGDTFPVGCAFDESIVY-PESFKGNPDYNNPKYNTKLGIYQPGCGLDNVLMSWGHD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523014   193 EYMYQMMKFNKFSLPGEAFYIIRFHSFYPWHTGGDYRQLCNEQDLAMLPWVQEFNKFDLYTKGSDMPDVDELRPYYQGLI 272
Cdd:pfam05153 160 EYLYQVLKFNKSTLPEEALYMIRYHSFYPWHREGAYTHLMNEEDEEMLKWVKAFNKYDLYSKSDDPPDVEALKPYYQSLI 239

                         250
                  ....*....|
gi 47523014   273 DKYCPGVLCW 282
Cdd:pfam05153 240 DKYFPGVLEW 249
HDOD pfam08668
HDOD domain;
100-135 6.41e-03

HDOD domain;


Pssm-ID: 430141 [Multi-domain]  Cd Length: 196  Bit Score: 36.82  E-value: 6.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 47523014   100 AEGIRKAHPDKdwFHLVGLLHDLGKVLVLAGEPQWA 135
Cdd:pfam08668 110 ARRLGLDDPEE--AFLAGLLHDIGKLILLSLLPDKY 143
 
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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