MI2D_RHIME
ID MI2D_RHIME Reviewed; 330 AA.
AC O68965;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Inositol 2-dehydrogenase;
DE EC=1.1.1.18;
DE AltName: Full=Myo-inositol 2-dehydrogenase;
DE Short=MI-dehydrogenase;
GN Name=idhA; Synonyms=iolG; OrderedLocusNames=RB1194; ORFNames=SMb20899;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION AS
RP MI-DEHYDROGENASE.
RC STRAIN=1021;
RX PubMed=9802033; DOI=10.1099/00221287-144-10-2915;
RA Galbraith M.P., Feng S.F., Borneman J., Triplett E.W., de Bruijn F.J.,
RA Rossbach S.;
RT "A functional myo-inositol catabolism pathway is essential for rhizopine
RT utilization by Sinorhizobium meliloti.";
RL Microbiology 144:2915-2924(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-
CC inositol (2KMI or 2-inosose). {ECO:0000269|PubMed:9802033}.
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 -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 1/7.
CC -!- INDUCTION: By myo-inositol. {ECO:0000269|PubMed:9802033}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AF059313; AAC70005.1; -; Genomic_DNA.
DR EMBL; AL591985; CAC49594.1; -; Genomic_DNA.
DR PIR; B95991; B95991.
DR RefSeq; NP_437734.1; NC_003078.1.
DR RefSeq; WP_010976021.1; NC_003078.1.
DR PDB; 4HKT; X-ray; 2.00 A; A/B/C/D=1-330.
DR PDBsum; 4HKT; -.
DR AlphaFoldDB; O68965; -.
DR SMR; O68965; -.
DR STRING; 266834.SM_b20899; -.
DR PRIDE; O68965; -.
DR EnsemblBacteria; CAC49594; CAC49594; SM_b20899.
DR GeneID; 61601140; -.
DR KEGG; sme:SM_b20899; -.
DR PATRIC; fig|266834.11.peg.6121; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_023194_0_3_5; -.
DR OMA; QVHAVNI; -.
DR BRENDA; 1.1.1.18; 5347.
DR UniPathway; UPA00076; UER00143.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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; Plasmid; Reference proteome.
FT CHAIN 1..330
FT /note="Inositol 2-dehydrogenase"
FT /id="PRO_0000091775"
FT CONFLICT 226
FT /note="S -> A (in Ref. 1; AAC70005)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:4HKT"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:4HKT"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4HKT"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 280..295
FT /evidence="ECO:0007829|PDB:4HKT"
FT HELIX 304..323
FT /evidence="ECO:0007829|PDB:4HKT"
SQ SEQUENCE 330 AA; 35147 MW; 06F5FBBAC7484A58 CRC64;
MTVRFGLLGA GRIGKVHAKA VSGNADARLV AVADAFPAAA EAIAGAYGCE VRTIDAIEAA
ADIDAVVICT PTDTHADLIE RFARAGKAIF CEKPIDLDAE RVRACLKVVS DTKAKLMVGF
NRRFDPHFMA VRKAIDDGRI GEVEMVTITS RDPSAPPVDY IKRSGGIFRD MTIHDFDMAR
FLLGEEPVSV TATAAVLIDK AIGDAGDYDS VSVILQTASG KQAIISNSRR ATYGYDQRIE
VHGSKGAVAA ENQRPVSIEI ATGDGYTRPP LHDFFMTRYT EAYANEIESF IAAIEKGAEI
APSGNDGLAA LALADAAVRS VAEKRQISIA
