ID A0A1U9LGL0_9PROT Unreviewed; 341 AA.
AC A0A1U9LGL0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=A0U91_12745 {ECO:0000313|EMBL:AQT05571.1};
OS Acetobacter persici.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1076596 {ECO:0000313|EMBL:AQT05571.1, ECO:0000313|Proteomes:UP000189055};
RN [1] {ECO:0000313|EMBL:AQT05571.1, ECO:0000313|Proteomes:UP000189055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMW2.1084 {ECO:0000313|EMBL:AQT05571.1,
RC ECO:0000313|Proteomes:UP000189055};
RA Brandt J., Jakob F., Vogel R.F.;
RT "Acetic acid bacteria sequencing.";
RL Submitted (MAR-2016) 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; CP014687; AQT05571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9LGL0; -.
DR STRING; 1076596.A0U91_12745; -.
DR KEGG; aper:A0U91_12745; -.
DR Proteomes; UP000189055; 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..125
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 137..323
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 341 AA; 37183 MW; 3B1D14861FC741F8 CRC64;
MTVRLGFIGT GDLGADHVRR CANILSGATV SALYNRTQSK AQTVAEQFAP EALVTAIPEE
LIESPEVEAI VISSASQTHE DLVLKAIEAG KYVFCEKPLA TTADGCERIL HAESAAAKRL
VQVGFMRPYD EGYQNLKSLL THDAVGPVLM AHAAHRNPFS GPHYTREMLI SETLIHDINT
FHWLLGESFR TVQVFYPRPT SRADAALRDP QLVLLETSSG VLITVEVFVN CQFGYDVQCA
LIGENGELRL PEPARAALRK NGQTSVAIPM DCKERFATAY DRELQAFVDG VATGKLTGPD
SWAGYVASAT ADACIRAQKS GQKEAVQLIA QPEFYRNDTD V
//
