ID   MIOX_DANRE              Reviewed;         278 AA.
AC   Q4V8T0;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Inositol oxygenase;
DE            EC=1.13.99.1;
DE   AltName: Full=Myo-inositol oxygenase;
DE            Short=MI oxygenase;
GN   Name=miox; ORFNames=zgc:114168;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Larva;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2005) 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; BC097218; AAH97218.1; -; mRNA.
DR   RefSeq; NP_001025437.1; NM_001030266.1.
DR   AlphaFoldDB; Q4V8T0; -.
DR   SMR; Q4V8T0; -.
DR   STRING; 7955.ENSDARP00000115890; -.
DR   PaxDb; 7955-ENSDARP00000115890; -.
DR   GeneID; 571850; -.
DR   KEGG; dre:571850; -.
DR   AGR; ZFIN:ZDB-GENE-050913-113; -.
DR   CTD; 55586; -.
DR   ZFIN; ZDB-GENE-050913-113; miox.
DR   eggNOG; KOG1573; Eukaryota.
DR   InParanoid; Q4V8T0; -.
DR   OrthoDB; 66304at2759; -.
DR   Reactome; R-DRE-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR   UniPathway; UPA00111; UER00527.
DR   PRO; PR:Q4V8T0; -.
DR   Proteomes; UP000000437; Chromosome 18.
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:SF0; INOSITOL OXYGENASE; 1.
DR   PANTHER; PTHR12588; MYOINOSITOL OXYGENASE; 1.
DR   Pfam; PF05153; MIOX; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..278
FT                   /note="Inositol oxygenase"
FT                   /id="PRO_0000079153"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         78..80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         213..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   278 AA;  32735 MW;  77473AF42E647FD0 CRC64;
     MGPDPSLAYR PECHEKDKTE FRNFENGDLF DRVFNTYKLM HTHQTLDFVK QKHQVWSNCS
     HFSLSMMDSI DSLDELVDES DPDVDFPNSF HAFQTAEGIR REHPDKDWFQ LVGLIHDVGK
     VMALYSEPQW AVVGDTYPVG CKFQNSIVFR NSTFEGNPDG KNPAPNTEFG IYEPQCGLDK
     VLMSWGHDEY LYRVMKFNKC TIPEEGLYMI RFHSFYPWHS NGDYMHLCNE KDQQMLPWVK
     EFNKFDLYTK STELPDVERL KPYYQSLIDK YCPGVLQW
//