ID A0A0F7H9G3_SERFO Unreviewed; 337 AA.
AC A0A0F7H9G3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:VEI76904.1};
GN ORFNames=NCTC12965_01279 {ECO:0000313|EMBL:VTR21497.1},
GN NCTC13193_05556 {ECO:0000313|EMBL:VEI76904.1}, WN53_06440
GN {ECO:0000313|EMBL:AKG68798.1};
OS Serratia fonticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG68798.1, ECO:0000313|Proteomes:UP000034699};
RN [1] {ECO:0000313|EMBL:AKG68798.1, ECO:0000313|Proteomes:UP000034699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG68798.1,
RC ECO:0000313|Proteomes:UP000034699};
RA Chan K.-G., Ee R.;
RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VTR21497.1, ECO:0000313|Proteomes:UP000358076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12965 {ECO:0000313|EMBL:VTR21497.1,
RC ECO:0000313|Proteomes:UP000358076}, and NCTC13193
RC {ECO:0000313|EMBL:VEI76904.1, ECO:0000313|Proteomes:UP000270487};
RG Pathogen Informatics;
RL Submitted (MAY-2019) 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; CP011254; AKG68798.1; -; Genomic_DNA.
DR EMBL; LR134492; VEI76904.1; -; Genomic_DNA.
DR EMBL; CABEEZ010000025; VTR21497.1; -; Genomic_DNA.
DR RefSeq; WP_024482782.1; NZ_SUPV01000031.1.
DR AlphaFoldDB; A0A0F7H9G3; -.
DR STRING; 47917.AV650_04485; -.
DR GeneID; 30319795; -.
DR KEGG; sfw:WN53_06440; -.
DR PATRIC; fig|47917.8.peg.1337; -.
DR Proteomes; UP000034699; Chromosome.
DR Proteomes; UP000270487; Chromosome 1.
DR Proteomes; UP000358076; 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:UP000034699}.
FT DOMAIN 3..125
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 137..326
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
SQ SEQUENCE 337 AA; 36568 MW; 5F030833343BF6FB CRC64;
MTLNIGVIGT GAIGRDHIRR CSQVLQGSRV VAVNDINRDS AAKVVSELKL DAKVYDNAHD
LINSTDVQAV LVTSWGPSHE EFVLAAIAAG KPVFCEKPLA VTAQGCKNIV DAEAKHGKRL
VQVGFMRPYD QGYRALKQVL TSGQIGEPLM LHCAHRNPRV GEAYTTDMAI TDTLIHELDV
LRWLLDDDYV SVQVVFPRKS SKALPHLRDP QIVLMETAKG TRIDVEIFVN CQYGYDIQCE
VVGETGIAKL PEPSAVQMRS GAKLSTEILV DWKDRFIGAY DVELQAFIND VLAGKLTGPS
AWDGFAAAVA ADACIAAQNS GEVVPVTLPA RPGFYGK
//
