ID   MIOX_BOVIN              Reviewed;         285 AA.
AC   A7MBE4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Kidney;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC151511; AAI51512.1; -; mRNA.
DR   RefSeq; NP_001094535.1; NM_001101065.1.
DR   RefSeq; XP_010804139.1; XM_010805837.1.
DR   AlphaFoldDB; A7MBE4; -.
DR   SMR; A7MBE4; -.
DR   STRING; 9913.ENSBTAP00000003315; -.
DR   PaxDb; A7MBE4; -.
DR   Ensembl; ENSBTAT00000064388; ENSBTAP00000055546; ENSBTAG00000002559.
DR   GeneID; 508591; -.
DR   KEGG; bta:508591; -.
DR   CTD; 55586; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002559; -.
DR   VGNC; VGNC:97286; MIOX.
DR   eggNOG; KOG1573; Eukaryota.
DR   GeneTree; ENSGT00390000016211; -.
DR   HOGENOM; CLU_050259_1_1_1; -.
DR   InParanoid; A7MBE4; -.
DR   OMA; RYNTKYG; -.
DR   OrthoDB; 1436589at2759; -.
DR   UniPathway; UPA00111; UER00527.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000002559; Expressed in cortex of kidney and 57 other tissues.
DR   ExpressionAtlas; A7MBE4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008199; F:ferric iron binding; ISS:UniProtKB.
DR   GO; GO:0050113; F:inositol oxygenase activity; ISS:UniProtKB.
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_0000328412"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  32973 MW;  CC9C772AF56DD5D6 CRC64;
     MKVAADPDPS LVSQRDMEPE AAKDKDSFRN YTSGPLLDRV FATYKLMHTW QTVDFVRRKH
     AQFGGFSYKR MTVMEAVDML DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG
     LLHDLGKVLA LAGEPQWAVV GDTFPVGCRP QASVVFRDCT FQDNPDLQDP LYSTELGMYQ
     PHCGLENVLM SWGHDEYMYR MMKFNKFALP PEAFYIIRFH SFYPWHKFGD YQQLCNEQDL
     AMLPWVQEFN KFDLYTKSSS LPDVAALRPY YQGLVDKYCP GILCW