IOLG_THEMA
ID IOLG_THEMA Reviewed; 334 AA.
AC Q9WYP5; G4FHX3;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Myo-inositol 2-dehydrogenase {ECO:0000305|PubMed:23441918};
DE EC=1.1.1.18 {ECO:0000269|PubMed:23441918};
GN Name=iolG {ECO:0000303|PubMed:23441918};
GN OrderedLocusNames=TM_0414 {ECO:0000312|EMBL:AAD35499.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RX PubMed=23441918; DOI=10.1111/1462-2920.12096;
RA Rodionova I.A., Leyn S.A., Burkart M.D., Boucher N., Noll K.M.,
RA Osterman A.L., Rodionov D.A.;
RT "Novel inositol catabolic pathway in Thermotoga maritima.";
RL Environ. Microbiol. 15:2254-2266(2013).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH (4S)- AND
RP (4R)-2-METHYLPENTANE-2,4-DIOL.
RA Ramagopal U.A., Toro R., Freeman J., Chang S., Maletic M., Gheyi T.,
RA Burley S.K., Almo S.C.;
RT "Crystal structure of probable dehydrogenase TM_0414 from Thermotoga
RT maritima.";
RL Submitted (OCT-2008) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of myo-inositol (MI)
CC to 2-keto-myo-inositol (scyllo-inosose), and thus probably functions in
CC a myo-inositol degradation pathway together with IolM, IolN and IolO.
CC Has no activity with scyllo-inositol and much reduced activity (78-fold
CC lower catalytic efficiency) with 1D-chiro-inositol.
CC {ECO:0000269|PubMed:23441918}.
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:0000269|PubMed:23441918};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.10 mM for myo-inositol {ECO:0000269|PubMed:23441918};
CC KM=2.9 mM for 1D-chiro-inositol {ECO:0000269|PubMed:23441918};
CC Note=kcat is 2.7 sec(-1) with myo-inositol as substrate. kcat is 1
CC sec(-1) with 1D-chiro-inositol as substrate.
CC {ECO:0000269|PubMed:23441918};
CC -!- PATHWAY: Polyol metabolism; myo-inositol metabolism.
CC {ECO:0000305|PubMed:23441918}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35499.1; -; Genomic_DNA.
DR PIR; D72381; D72381.
DR RefSeq; NP_228224.1; NC_000853.1.
DR RefSeq; WP_004083264.1; NZ_CP011107.1.
DR PDB; 3EZY; X-ray; 2.04 A; A/B/C/D=2-334.
DR PDBsum; 3EZY; -.
DR AlphaFoldDB; Q9WYP5; -.
DR SMR; Q9WYP5; -.
DR STRING; 243274.THEMA_02655; -.
DR DNASU; 897415; -.
DR EnsemblBacteria; AAD35499; AAD35499; TM_0414.
DR KEGG; tma:TM0414; -.
DR PATRIC; fig|243274.17.peg.412; -.
DR eggNOG; COG0673; Bacteria.
DR InParanoid; Q9WYP5; -.
DR OMA; QVHAVNI; -.
DR OrthoDB; 1465613at2; -.
DR BioCyc; MetaCyc:MON-17948; -.
DR BRENDA; 1.1.1.369; 6331.
DR UniPathway; UPA00914; -.
DR EvolutionaryTrace; Q9WYP5; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006020; P:inositol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006740; P:NADPH regeneration; IBA:GO_Central.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR030827; Myo_inos_IolG.
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.
DR TIGRFAMs; TIGR04380; myo_inos_iolG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Myo-inositol 2-dehydrogenase"
FT /id="PRO_0000440854"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:3EZY"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:3EZY"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:3EZY"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 275..296
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 304..323
FT /evidence="ECO:0007829|PDB:3EZY"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:3EZY"
SQ SEQUENCE 334 AA; 37485 MW; 97A3569F165A64A7 CRC64;
MRIGVIGLGR IGTIHAENLK MIDDAILYAI SDVREDRLRE MKEKLGVEKA YKDPHELIED
PNVDAVLVCS STNTHSELVI ACAKAKKHVF CEKPLSLNLA DVDRMIEETK KADVILFTGF
NRRFDRNFKK LKEAVENGTI GKPHVLRITS RDPAPPPLDY IRVSGGIFLD MTIHDFDMAR
YIMGEEVEEV FADGSVLVDE EIGKAGDVDT AVVVLRFKSG ALGVIDNSRR AVYGYDQRIE
VFGSKGRIFA DNVRETTVVL TDEQGDRGSR YLYFFLERYR DSYLEELKTF IKNVKSGEPP
AVSGEDGKMA LLLGYAAKKS LEEKRSVKLE EVIG
