ID C3YD55_BRAFL Unreviewed; 290 AA.
AC C3YD55;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=BRAFLDRAFT_279937 {ECO:0000313|EMBL:EEN61666.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN61666.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN61666.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN61666.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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; GG666503; EEN61666.1; -; Genomic_DNA.
DR RefSeq; XP_002605656.1; XM_002605610.1.
DR AlphaFoldDB; C3YD55; -.
DR eggNOG; KOG1573; Eukaryota.
DR InParanoid; C3YD55; -.
DR UniPathway; UPA00111; UER00527.
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 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}.
SQ SEQUENCE 290 AA; 33777 MW; 8D5B5C40C104943F CRC64;
MTTILDPSPV HRPDMEGCDK NFRNFEVCNQ NSEEVNSHTD QVRNTYQLMH THQTVDFVRR
KMEQWCKLDH AQMTMLECLE ELNNLVDESD PDVDVPNIYH AFQTAESIRE KHPDNDWLQL
TGLIHDAGKI MAIWGEPQWC VVGDTFPTGC LPAESVVFRH STFQDNPDMK DPKFNTKLGM
YEENCGLDKV LMSWGHDEYM YRVLKGNNAK LPEEALYAIR FHSFYPWHGS GDYDYLSCNV
PFRLTVPNRC VFSCSKFDLY SKADDLPDID ALKPYYQGLI DKYIPGKLRW
//