IOLG_LACCA
ID IOLG_LACCA Reviewed; 346 AA.
AC A5YBJ7;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE EC=1.1.1.18 {ECO:0000255|HAMAP-Rule:MF_01671};
DE EC=1.1.1.369 {ECO:0000255|HAMAP-Rule:MF_01671};
DE AltName: Full=Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE Short=MI 2-dehydrogenase/DCI 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
GN Name=iolG {ECO:0000255|HAMAP-Rule:MF_01671};
OS Lactobacillus casei.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1582;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BL23;
RX PubMed=17449687; DOI=10.1128/aem.00243-07;
RA Yebra M.J., Zuniga M., Beaufils S., Perez-Martinez G., Deutscher J.,
RA Monedero V.;
RT "Identification of a gene cluster allowing Lactobacillus casei BL23 the
RT utilization of myo-inositol.";
RL Appl. Environ. Microbiol. 73:3850-3858(2007).
CC -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) and D-chiro-
CC inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-
CC chiro-inositol (1KDCI), respectively. {ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-chiro-inositol + NAD(+) = H(+) + NADH + scyllo-inosine;
CC Xref=Rhea:RHEA:25832, ChEBI:CHEBI:15378, ChEBI:CHEBI:27372,
CC ChEBI:CHEBI:50920, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.369; Evidence={ECO:0000255|HAMAP-Rule:MF_01671};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 1/7. {ECO:0000255|HAMAP-
CC Rule:MF_01671}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01671}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000255|HAMAP-
CC Rule:MF_01671}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF382358; ABP57766.1; -; Genomic_DNA.
DR RefSeq; WP_003562987.1; NZ_MODS01000089.1.
DR AlphaFoldDB; A5YBJ7; -.
DR SMR; A5YBJ7; -.
DR STRING; 543734.LCABL_02210; -.
DR GeneID; 61268589; -.
DR eggNOG; COG0673; Bacteria.
DR OMA; VNCKYGY; -.
DR UniPathway; UPA00076; UER00143.
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 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 Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..346
FT /note="Inositol 2-dehydrogenase/D-chiro-inositol 3-
FT dehydrogenase"
FT /id="PRO_0000352572"
SQ SEQUENCE 346 AA; 37964 MW; 1FCB85142F4C942A CRC64;
MVVKVGVIGT GAMGRAHIDR LTNVLTGAEV VAVTDIDHEA AEAAVRDFHL NAKVYPDDTS
LLQDPDIDAV FVVSFGGAHE ATVLKALDTD KFIFTEKPLA TTLEGAKRIV DKELTKSKKV
IQVGFMRRYD QGIRALKEKL DTGIIGAPLV VRASHINPNV ASNYSNEMAI TDTLIHEIDE
MHWLLDDEYT SIQITYPRQS AEVRNEGLHD PQLATLTTKK GTVIQVLVHV TAQYGYEVKL
EVIGETGELQ LPNYGLGPIL RSNANQQTAV EMSWINRFIQ AYNTEVQEFI DQVAKSEPPV
GPSAWDGYIA AITAAAANRS QKDQETVLIN VAGTPTFYQN KNAIHA