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Database: UniProt
Entry: A0A124E074_9MYCO
LinkDB: A0A124E074_9MYCO
Original site: A0A124E074_9MYCO 
ID   A0A124E074_9MYCO        Unreviewed;       346 AA.
AC   A0A124E074;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Inositol 2-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
DE            EC=1.1.1.18 {ECO:0000256|HAMAP-Rule:MF_01671};
DE   AltName: Full=Myo-inositol 2-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
DE            Short=MI 2-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
GN   Name=iolG {ECO:0000256|HAMAP-Rule:MF_01671};
GN   ORFNames=RMCB_3739 {ECO:0000313|EMBL:GAS89643.1};
OS   Mycolicibacterium brisbanense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS89643.1, ECO:0000313|Proteomes:UP000069620};
RN   [1] {ECO:0000313|EMBL:GAS89643.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM15654 {ECO:0000313|EMBL:GAS89643.1};
RA   Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT   "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT   thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT   M. brisbanense, and M. novocastrense.";
RL   Genome Announc. 4:e00322-16(2016).
CC   -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-
CC       inositol (2KMI or 2-inosose). {ECO:0000256|HAMAP-Rule:MF_01671}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose;
CC         Xref=Rhea:RHEA:16949, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC         ChEBI:CHEBI:17811, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.18;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01671};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01671}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01671}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAS89643.1}.
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DR   EMBL; BCSX01000034; GAS89643.1; -; Genomic_DNA.
DR   RefSeq; WP_062829992.1; NZ_JACKTM010000019.1.
DR   AlphaFoldDB; A0A124E074; -.
DR   STRING; 146020.RMCB_3739; -.
DR   OrthoDB; 256869at2; -.
DR   Proteomes; UP000069620; Unassembled WGS sequence.
DR   GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01671; IolG; 1.
DR   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR023794; MI/DCI_dehydrogenase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43593; -; 1.
DR   PANTHER; PTHR43593:SF1; INOSITOL 2-DEHYDROGENASE; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01671};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01671}.
FT   DOMAIN          4..124
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          137..335
FT                   /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02894"
SQ   SEQUENCE   346 AA;  36961 MW;  2541290480BAFE4B CRC64;
     MSDLRIAVLG VGIMGADHVE RLATRISGAR VTVVNDFLTE KAEAVAAGVP GCRAVGDPLD
     AIADPDVDAV VLATPGPTHD KQLLACLDHV KPVLCEKPLT TDVESSLEVV KREAELGRRL
     IQVGFMRRFD DEYMQLKALM DAGEFGQPLV LHCVHRNPAV PPSFDSSMVV KDSLVHEVDV
     TRFLFDEEIA SIQIIKPATN PGAPQGIQDP QIAIMRTTSG KHVDVELFVT TGVAYEVRTE
     LVGEMGSAFI GLDVGLIRKG GQAGPGTWGG QITPGFRERF GRAYDTEFQR WVNAVRRGQA
     TGDYTDGPSA WDGYAAAAVC AAGVESLQSG QPVDVSMVDR ASIPGA
//
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