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Database: UniProt
Entry: F4RWG7_MELLP
LinkDB: F4RWG7_MELLP
Original site: F4RWG7_MELLP 
ID   F4RWG7_MELLP            Unreviewed;       298 AA.
AC   F4RWG7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 37.
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};
GN   ORFNames=MELLADRAFT_109435 {ECO:0000313|EMBL:EGG03324.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; GL883125; EGG03324.1; -; Genomic_DNA.
DR   RefSeq; XP_007413459.1; XM_007413397.1.
DR   AlphaFoldDB; F4RWG7; -.
DR   STRING; 747676.F4RWG7; -.
DR   EnsemblFungi; EGG03324; EGG03324; MELLADRAFT_109435.
DR   GeneID; 18923763; -.
DR   KEGG; mlr:MELLADRAFT_109435; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_109435; -.
DR   eggNOG; KOG1573; Eukaryota.
DR   HOGENOM; CLU_050259_0_1_1; -.
DR   InParanoid; F4RWG7; -.
DR   OrthoDB; 66304at2759; -.
DR   UniPathway; UPA00111; UER00527.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050113; F:inositol oxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
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:UP000001072}.
SQ   SEQUENCE   298 AA;  35122 MW;  2FBE16D499064F13 CRC64;
     MSAKVDPLPL TMEDEVDKIE INQNPNKNNI SNQDEGLQKS FRDYEKACDR VKNFYEEQHT
     NQTFEFNLQV RERFKKREKR KMTIFEALEV LDGLVDESDP DMELGQLDHL LQTAEAIRKD
     GKPDWMQVVG LIHDLGKLMH LFRPEGEESR QWDVVGDTFV VGAKFSDKII YPNTFSKNPD
     WNDPVYSSEY GVYEPNCGME NVLLSWGHDE YLYNVLKDKC LLPKEGLAMI RFHSFYPWHR
     DGAYRQFMNE GDQKLLEAVI SFNPYDLYSK STIRPDPVKL RPYYQSIVEK YFPEEIEF
//
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