ID   MIOX_PONAB              Reviewed;         285 AA.
AC   Q5REY9;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Inositol oxygenase;
DE            EC=1.13.99.1;
DE   AltName: Full=Myo-inositol oxygenase;
DE            Short=MI oxygenase;
GN   Name=MIOX;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=myo-inositol + O2 = D-glucuronate + H(+) + H2O;
CC         Xref=Rhea:RHEA:23696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17268, ChEBI:CHEBI:58720;
CC         EC=1.13.99.1;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D-
CC       glucuronate; D-glucuronate from myo-inositol: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; CR857374; CAH89668.1; -; mRNA.
DR   RefSeq; NP_001124754.1; NM_001131282.2.
DR   AlphaFoldDB; Q5REY9; -.
DR   SMR; Q5REY9; -.
DR   STRING; 9601.ENSPPYP00000013373; -.
DR   Ensembl; ENSPPYT00000013919; ENSPPYP00000013373; ENSPPYG00000011988.
DR   GeneID; 100171604; -.
DR   KEGG; pon:100171604; -.
DR   CTD; 55586; -.
DR   eggNOG; KOG1573; Eukaryota.
DR   GeneTree; ENSGT00390000016211; -.
DR   HOGENOM; CLU_050259_1_0_1; -.
DR   InParanoid; Q5REY9; -.
DR   OMA; RYNTKYG; -.
DR   OrthoDB; 1436589at2759; -.
DR   TreeFam; TF300089; -.
DR   UniPathway; UPA00111; UER00527.
DR   Proteomes; UP000001595; Chromosome 22.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IEA:Ensembl.
DR   GO; GO:0008199; F:ferric iron binding; ISS:UniProtKB.
DR   GO; GO:0050113; F:inositol oxygenase activity; ISS:UniProtKB.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:Ensembl.
DR   GO; GO:0019310; P:inositol catabolic process; ISS:UniProtKB.
DR   InterPro; IPR007828; Inositol_oxygenase.
DR   PANTHER; PTHR12588; PTHR12588; 1.
DR   Pfam; PF05153; MIOX; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Iron; Metal-binding; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..285
FT                   /note="Inositol oxygenase"
FT                   /id="PRO_0000079151"
FT   BINDING         29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141..142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         220..221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXN4"
SQ   SEQUENCE   285 AA;  32944 MW;  D4481A96F29069D6 CRC64;
     MKVTVGPDPS LVYRPDVDPE MAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH
     AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG
     LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ
     PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGSD YQQLCSQQDL
     AMLPWVQEFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW