GenomeNet

Database: UniProt
Entry: C3YD55_BRAFL
LinkDB: C3YD55_BRAFL
Original site: C3YD55_BRAFL 
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}.
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; 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
//
DBGET integrated database retrieval system