IOLG_RENSM
ID IOLG_RENSM Reviewed; 331 AA.
AC A9WKW2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Inositol 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE EC=1.1.1.18 {ECO:0000255|HAMAP-Rule:MF_01671};
DE AltName: Full=Myo-inositol 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
DE Short=MI 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01671};
GN Name=iolG {ECO:0000255|HAMAP-Rule:MF_01671};
GN OrderedLocusNames=RSal33209_0365;
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Renibacterium.
OX NCBI_TaxID=288705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235;
RX PubMed=18723615; DOI=10.1128/jb.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
CC -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-
CC inositol (2KMI or 2-inosose). {ECO:0000255|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:0000255|HAMAP-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}.
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DR EMBL; CP000910; ABY22120.1; -; Genomic_DNA.
DR AlphaFoldDB; A9WKW2; -.
DR SMR; A9WKW2; -.
DR STRING; 288705.RSal33209_0365; -.
DR PRIDE; A9WKW2; -.
DR EnsemblBacteria; ABY22120; ABY22120; RSal33209_0365.
DR KEGG; rsa:RSal33209_0365; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_0_1_11; -.
DR OMA; VNCKYGY; -.
DR Proteomes; UP000002007; 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 HAMAP; MF_01671; IolG; 1.
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 SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..331
FT /note="Inositol 2-dehydrogenase"
FT /id="PRO_0000352585"
SQ SEQUENCE 331 AA; 35267 MW; 5FE807A7AF86AA4C CRC64;
MNVAVIGAGR MGADHVRRLH ESINNATVAA VVDIDLDRAK AATEGTGALA VASLAEAFAV
EGVNAVLIAT PGFLHEEALY QALQRDVPIL CEKPMTPDAA SAWRVVQAEV ALGRQRIQVG
FMRQFDAGYQ SLKSEIEAGA AGSLLMLHCA NRNASTLADF TEPMLINDSV VHEFDAIRFF
TGEEITSVQV QVQVQVQVQV QVQRGKRSSL APEGISDPQH VLIETESGIL ADVEIFVNAR
YGYEVATQAV FENGVRSIGA GEVTPSFIER FAAAYDAEVQ AWVDAALHGE IGGPSAWDGY
ATAACCEAGV AAQRSGQRTA VVLAAKPELY R