ID MIOX_DICDI Reviewed; 292 AA. AC Q54GH4; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 24-JAN-2024, entry version 93. 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=DDB_G0290161; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). 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; AAFI02000158; EAL62352.1; -; Genomic_DNA. DR RefSeq; XP_635854.1; XM_630762.1. DR AlphaFoldDB; Q54GH4; -. DR SMR; Q54GH4; -. DR STRING; 44689.Q54GH4; -. DR PaxDb; 44689-DDB0235367; -. DR EnsemblProtists; EAL62352; EAL62352; DDB_G0290161. DR GeneID; 8627510; -. DR KEGG; ddi:DDB_G0290161; -. DR dictyBase; DDB_G0290161; miox. DR eggNOG; KOG1573; Eukaryota. DR HOGENOM; CLU_050259_1_0_1; -. DR InParanoid; Q54GH4; -. DR OMA; RYNTKYG; -. DR PhylomeDB; Q54GH4; -. DR Reactome; R-DDI-1855183; Synthesis of IP2, IP, and Ins in the cytosol. DR UniPathway; UPA00111; UER00527. DR PRO; PR:Q54GH4; -. DR Proteomes; UP000002195; Chromosome 5. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050113; F:inositol oxygenase activity; IBA:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016701; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen; ISS:dictyBase. DR GO; GO:0019310; P:inositol catabolic process; ISS:dictyBase. 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 3: Inferred from homology; KW Cytoplasm; Iron; Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1..292 FT /note="Inositol oxygenase" FT /id="PRO_0000328413" FT BINDING 33 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 88..90 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 101 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 128 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 129 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 129 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 132 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 149..150 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 201 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 227..228 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 227 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000250" SQ SEQUENCE 292 AA; 34801 MW; 4F4D1E483BECFF8E CRC64; MIETRTTTST SEIKHDNSLK TGFEITKEVE EFRNYENSED RVSEAYRNSH TYQTYDYATE KKKQYSQLDT SIKMGLWEAA ELLNTIIDES DPDSNIPQIN HCLQTAEAIR KVYPDSKYDW FHLTGFIHDL GKVLLSKKFK EQPQWATVGD TFPLGCKFDE SNIFYEFFKM NPDYNDSKYN SECGIYKKNI GLENVTMSWG HDEYFYLVCV GNKCLLPKES LYMIRFHSFY PWHRHNKYTH LTNEEDEKML NWVKEFNKFD LYSKDSEPVD VESLKPYYQS LISKYFPNEL HW //