ID G8A523_FLAVE Unreviewed; 722 AA.
AC G8A523;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Inositol oxygenase {ECO:0000256|ARBA:ARBA00019269};
DE EC=1.13.99.1 {ECO:0000256|ARBA:ARBA00011919};
DE AltName: Full=Myo-inositol oxygenase {ECO:0000256|ARBA:ARBA00029668};
OS Flammulina velutipes (Agaricus velutipes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Flammulina.
OX NCBI_TaxID=38945 {ECO:0000313|EMBL:ADX07297.1};
RN [1] {ECO:0000313|EMBL:ADX07297.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KACC 42777 {ECO:0000313|EMBL:ADX07297.1};
RA Yoon H., Kim J.-G., Lee B.-M., Kong W.-S., Lee C.-S., Choi J.-W.;
RT "Useful genes from Flammulina velutipes.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into D-
CC glucuronate; D-glucuronate from myo-inositol: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005167}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the myo-inositol oxygenase family.
CC {ECO:0000256|ARBA:ARBA00005286}.
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DR EMBL; GU169862; ADX07297.1; -; mRNA.
DR AlphaFoldDB; G8A523; -.
DR UniPathway; UPA00111; UER00527.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050113; F:inositol oxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 722 AA; 83064 MW; CDE38930BC90F5EB CRC64;
MPEHVNFKVL MATVLRGPKE SLASVRQLEE YFNKRMVFVG RHVLPAIRHH LKRINMISLE
TADWPASPEI QNALSCFGMS ALMFERYKRE NVDFTPQVKE EITEPLWPLI RDWSLYFIQR
SRVLEENSEP RNLDLIFLLE RVLSSFVRWI NVGIRYVRPG PYMDEFLMTI THLWVRCSAE
LDISIPAMAD VLTASMSQEP SPGRFGPVSN TFTSKPPRDV AITVMNTAHN SIMSELVGYD
IMTWMTRLAR RMTSKRAAFE FNIFEEEIEG VGSSIQLVFG AIHSLLILGY VALVQALESH
VLEAAINSEI YLVRYFSEDS QYIESLRQQV AQILDGVVHF LDFRSVLNIA RRDIRHIEAS
GVEEYIATGS SLLHKWLEFK DIVRSHQDAV ALYKDVILAK CANPQNVSEL TGSTDTRRTV
HRFAVNVQRS ALWLGGVIVN VLKGKAKIAK DAEWNDKSTF DENKDKGQFR QYEEACERVK
KFYYEQHEKQ TMDFNIKARV NFRKNVRARM GVWEAMEKLN TLVDNSDPDT DVSQIEHLLQ
TAEAIRRDGK PEWMQVVGLV HDLGKLLYIF GSEGQWDVVG DTFVVGCQFS DKIIYPGSFA
NNPDSEDPIY STEYGVYKPH CGLENVMLSW GHDEYLYHVF KEQSSLPEEG LAMIRYHSFY
PWHREGAYAH LTNAADEKAL AAVRAFNPYD LYSKSDDPVD PAKLKPYYQG LIEIFFPEEI
VW
//