ID A0A3T1B5X3_9ACTN Unreviewed; 339 AA.
AC A0A3T1B5X3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 ECO:0000313|EMBL:BBH70513.1};
GN ORFNames=ACTI_71980 {ECO:0000313|EMBL:BBH70513.1};
OS Actinoplanes sp. OR16.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=946334 {ECO:0000313|EMBL:BBH70513.1, ECO:0000313|Proteomes:UP000282692};
RN [1] {ECO:0000313|EMBL:BBH70513.1, ECO:0000313|Proteomes:UP000282692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:BBH70513.1,
RC ECO:0000313|Proteomes:UP000282692};
RA Kasai D.;
RT "Complete genome sequence of natural rubber degrading Actinoplanes sp.
RT strain OR16 isolated form botanical garden in Japan.";
RL Submitted (DEC-2018) 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}.
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DR EMBL; AP019371; BBH70513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T1B5X3; -.
DR OrthoDB; 256869at2; -.
DR Proteomes; UP000282692; Chromosome.
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..123
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 136..322
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 339 AA; 35994 MW; 8628841E3B72C7E2 CRC64;
MTKLRVGVVG AGMIGRDHVR RLTSVVAGAE VVAVADVDES AAAQVADACG ATVRPGDRLI
EDPDVDAVLV CSWGGTHEEY VLAAIAAGKP VFCEKPLAPT PEACLRIVEA EVARGHRLVQ
VGYMRRYDPA YRALRRELDS GSIGAPLMMH CAHRNAGVPG FYRAEDMIAD TAVHEIDMVR
WMFRTEVVAV RVLRPRASGN AGDLPDPMLL ILELAGGVLV DVEISVNVRY GYDIRGEILG
ENGTAALGES GLVAVRRDGR LASPVAGDWR ERFGAAYDAE LRSWVTGLRE GAAADGPSAW
DGYAAATVSA AAQSSLRTGE RVLISEIAKP ALYDGSTST
//
