ID H2ULN7_TAKRU Unreviewed; 278 AA.
AC H2ULN7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 55.
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 Name=miox {ECO:0000313|Ensembl:ENSTRUP00000037858.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000037858.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000037858.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000037858.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 AlphaFoldDB; H2ULN7; -.
DR STRING; 31033.ENSTRUP00000037858; -.
DR Ensembl; ENSTRUT00000037994.3; ENSTRUP00000037858.3; ENSTRUG00000014819.3.
DR eggNOG; KOG1573; Eukaryota.
DR GeneTree; ENSGT00390000016211; -.
DR HOGENOM; CLU_050259_1_0_1; -.
DR InParanoid; H2ULN7; -.
DR OMA; RYNTKYG; -.
DR OrthoDB; 66304at2759; -.
DR TreeFam; TF300089; -.
DR UniPathway; UPA00111; UER00527.
DR Proteomes; UP000005226; Chromosome 9.
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 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:UP000005226}.
SQ SEQUENCE 278 AA; 32584 MW; 9E37293CD8C6A30C CRC64;
MKILGPDPSL EYPPNPEKEK YRNFESGALI DRVFKTYKVM HTKQTVDFVK QKHAEWNGCT
HAQMRMMDAI MALDQLVDES DPDVDFPNSF HAFQTAEGIR QAHPDKDWFQ LVGLIHDVGK
IMAVWNEPQW AVVGDTFPVG CKFQNSIVYR NDSFQDNPDD KNPSYNTECG MYAPNCGLEK
VYMSWGHDEY LYQVMKFNNC SIPEEGLYMI RFHSFYPWHS HGDYTHLCNH KDLNMLPWVQ
EFNKFDLYTK TTEMPDVEGL KPYYQSLIDK YCPGVLKW
//
