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Database: UniProt
Entry: H3GB48_PHYRM
LinkDB: H3GB48_PHYRM
Original site: H3GB48_PHYRM 
ID   H3GB48_PHYRM            Unreviewed;       294 AA.
AC   H3GB48;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Inositol oxygenase {ECO:0000256|ARBA:ARBA00019269, ECO:0000256|RuleBase:RU367039};
DE            EC=1.13.99.1 {ECO:0000256|ARBA:ARBA00011919, ECO:0000256|RuleBase:RU367039};
DE   AltName: Full=Myo-inositol oxygenase {ECO:0000256|ARBA:ARBA00029668, ECO:0000256|RuleBase:RU367039};
OS   Phytophthora ramorum (Sudden oak death agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra72460, ECO:0000313|Proteomes:UP000005238};
RN   [1] {ECO:0000313|Proteomes:UP000005238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
RN   [2] {ECO:0000313|EnsemblProtists:Phyra72460}
RP   IDENTIFICATION.
RC   STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra72460};
RG   EnsemblProtists;
RL   Submitted (JUN-2015) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00000486,
CC         ECO:0000256|RuleBase:RU367039};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|RuleBase:RU367039};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000256|RuleBase:RU367039};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D-
CC       glucuronate; D-glucuronate from myo-inositol: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005167, ECO:0000256|RuleBase:RU367039}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU367039}.
CC   -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC       {ECO:0000256|ARBA:ARBA00005286, ECO:0000256|RuleBase:RU367039}.
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DR   EMBL; DS567182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3GB48; -.
DR   STRING; 164328.H3GB48; -.
DR   EnsemblProtists; Phyra72460; Phyra72460; Phyra72460.
DR   VEuPathDB; FungiDB:PSURA_72460; -.
DR   eggNOG; KOG1573; Eukaryota.
DR   HOGENOM; CLU_050259_1_0_1; -.
DR   InParanoid; H3GB48; -.
DR   OMA; RYNTKYG; -.
DR   UniPathway; UPA00111; UER00527.
DR   Proteomes; UP000005238; Unassembled WGS sequence.
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:0019310; P:inositol catabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367039};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU367039};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367039};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU367039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005238}.
SQ   SEQUENCE   294 AA;  33693 MW;  8313AC2244E7767C CRC64;
     MAGDSIAVHK PALEVTGKVT AGKAEEEFRN YKDSDRHALV SRHYACMRKN QTVAFQEKMQ
     AKYGSFANTK MTVWEAFTAL KGYVDSSDPD SSLPNLEHML QTAEGIRAAG HPDWFQLVGL
     LHDMGKIQYL WGHAEDGQEG TADGDQWALG GDTWVVGCKI PDSVVFPEFN GTNPDMSDSR
     YNTDNGMYEP HCGFQNLKFA WGHDEYLYQM LKFNETTIPD EGLAMIRYHS CYPWHNKKEY
     AHLMSENDDE LLDWVLEFNK FDLYTKADVR PDVEELWPYY QGLIDKYLPG KLSW
//
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