ID A0A327Z747_9ACTN Unreviewed; 318 AA.
AC A0A327Z747;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=B0I29_116173 {ECO:0000313|EMBL:RAK30514.1};
OS Actinoplanes lutulentus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1287878 {ECO:0000313|EMBL:RAK30514.1, ECO:0000313|Proteomes:UP000249341};
RN [1] {ECO:0000313|EMBL:RAK30514.1, ECO:0000313|Proteomes:UP000249341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7090 {ECO:0000313|EMBL:RAK30514.1,
RC ECO:0000313|Proteomes:UP000249341};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-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}.
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:RAK30514.1}.
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DR EMBL; QLMJ01000016; RAK30514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327Z747; -.
DR OrthoDB; 256869at2; -.
DR Proteomes; UP000249341; 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}; Reference proteome {ECO:0000313|Proteomes:UP000249341}.
FT DOMAIN 2..120
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 138..307
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 318 AA; 33985 MW; D018618894D7BA3D CRC64;
MLRVGVIGTG MIGQDHIRRL TSVLSGARVV AVTDVDTTLA AGVGAAVGAA VHPTGEDVIA
ACDAVLVCSW GPSHEQYVLA AIDAGKPVFC EKPLATTASA CRRIVDAEVA CGRRLVQVGF
MRRFDDAYRK LRNEAGGGAI GAPLLMHCAH RNRDVPAYYR TEMAIVDTAV HEFDMVRWMF
GEDIVAIRVL VPRSNRNGAG LQDPLLIILE LANGIIVDVE TSVNIRYGYD IRGEIVGENG
TLTLGGPVAV DWRDRFQAAY DTELQEWIDA LGVSGHPTGP SAWDGYAATA VCEAGVQSLR
TGSRVEVALA ERPSLFLS
//
