ID A0A1X0HHX5_9MYCO Unreviewed; 339 AA.
AC A0A1X0HHX5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=BST36_06885 {ECO:0000313|EMBL:ORB25746.1};
OS Mycolicibacterium moriokaense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=39691 {ECO:0000313|EMBL:ORB25746.1, ECO:0000313|Proteomes:UP000192354};
RN [1] {ECO:0000313|EMBL:ORB25746.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP105393 {ECO:0000313|EMBL:ORB25746.1};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:ORB25746.1}.
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DR EMBL; MVIB01000005; ORB25746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0HHX5; -.
DR OrthoDB; 256869at2; -.
DR Proteomes; UP000192354; 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..328
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 339 AA; 36049 MW; 27E5C13458B84641 CRC64;
MTDLRVAVLG VGVMGADHVA RLNSRISGAR AAVVNDYVTE KAEQIAATIP GCRAVVDPLD
AIADPDVDAV VLATPGPTHE KQLLACLEHA KPVLCEKPLT TDVETSLAVV KREAELGKRL
IQVGFMRRFD HEYAQLKALL DGGELGRPLV LHCAHRNPAV PPTFDSAMVV RDSLVHEVDV
TRFLFDEEIA SIQIIKPAAN PGAPQGLADP QIAIMRTTSG KHVDVELFVT TGVAYEVRTE
VVAEKGSATI GLDVGLIRKS APGHWGGEIA PGFRERFGQA YDTEFQRWVD AVNAGVNLDG
PGAWDGYAAA AVCEAGVESL NSGLPVEVKM VDRASIDGA
//
