MIOX_PIG
ID MIOX_PIG Reviewed; 282 AA.
AC Q8WN98;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Inositol oxygenase;
DE EC=1.13.99.1;
DE AltName: Full=Aldehyde reductase-like 6;
DE AltName: Full=Myo-inositol oxygenase;
DE Short=MI oxygenase;
GN Name=MIOX; Synonyms=ALDRL6;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Kidney;
RX PubMed=11716759; DOI=10.1042/0264-6021:3600313;
RA Arner R.J., Prabhu K.S., Thompson J.T., Hildenbrandt G.R., Liken A.D.,
RA Reddy C.C.;
RT "Myo-inositol oxygenase: molecular cloning and expression of a unique
RT enzyme that oxidizes myo-inositol and d-chiro-inositol.";
RL Biochem. J. 360:313-320(2001).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermolabile.;
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D-
CC glucuronate; D-glucuronate from myo-inositol: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Kidney specific.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC {ECO:0000305}.
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DR EMBL; AF401311; AAL39076.1; -; mRNA.
DR RefSeq; NP_999267.1; NM_214102.2.
DR AlphaFoldDB; Q8WN98; -.
DR SMR; Q8WN98; -.
DR STRING; 9823.ENSSSCP00000001029; -.
DR PaxDb; Q8WN98; -.
DR PeptideAtlas; Q8WN98; -.
DR PRIDE; Q8WN98; -.
DR GeneID; 397189; -.
DR KEGG; ssc:397189; -.
DR CTD; 55586; -.
DR eggNOG; KOG1573; Eukaryota.
DR InParanoid; Q8WN98; -.
DR OrthoDB; 1436589at2759; -.
DR BRENDA; 1.13.99.1; 6170.
DR SABIO-RK; Q8WN98; -.
DR UniPathway; UPA00111; UER00527.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016234; C:inclusion body; IDA:UniProtKB.
DR GO; GO:0008199; F:ferric iron binding; ISS:UniProtKB.
DR GO; GO:0050113; F:inositol oxygenase activity; ISS:UniProtKB.
DR GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; IDA:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; TAS:UniProtKB.
DR GO; GO:0019310; P:inositol catabolic process; IDA:UniProtKB.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; TAS:UniProtKB.
DR GO; GO:0061024; P:membrane organization; TAS:UniProtKB.
DR InterPro; IPR007828; Inositol_oxygenase.
DR PANTHER; PTHR12588; PTHR12588; 1.
DR Pfam; PF05153; MIOX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Metal-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..282
FT /note="Inositol oxygenase"
FT /id="PRO_0000079150"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82..84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138..139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXN4"
SQ SEQUENCE 282 AA; 32653 MW; 0B9D4D54A3AE5DE0 CRC64;
MKDPDPSQVY RPDMDPEAAK DKGSFRNYTS GPLLDRVFRT YKLMHTWQTV DFVRKKHAQF
GGFSYKRMTV LEAVDMLDGL VDESDPDVDF PNSFHAFQTA EGIRKAHPDK DWFHLVGLLH
DLGKVLVLAG EPQWAVVGDT FPVGCRPQAS VVFCDSTFQD NPDLQDPVYS TELGMYQPHC
GLENALMSWG HDEYMYQMMK FNKFSLPGEA FYIIRFHSFY PWHTGGDYRQ LCNEQDLAML
PWVQEFNKFD LYTKGSDMPD VDELRPYYQG LIDKYCPGVL CW
