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 16-JUN-2009, entry version 57. 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 (Sinorhizobium meliloti). OG Plasmid pSymB (megaplasmid 2). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=382; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION AS RP MI-DEHYDROGENASE. RC STRAIN=1021; RX MEDLINE=99018841; PubMed=9802033; 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 RT rhizopine utilization by Sinorhizobium meliloti."; RL Microbiology 144:2915-2924(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX MEDLINE=21396508; PubMed=11481431; DOI=10.1073/pnas.161294698; RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., RA Vorhoelter F.J., Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., RA Golding B., Puehler A.; RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2- RT fixing endosymbiont Sinorhizobium meliloti."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001). CC -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) to 2- CC keto-myo-inositol (2KMI or 2-inosose). CC -!- CATALYTIC ACTIVITY: Myo-inositol + NAD(+) = 2,4,6/3,5- CC pentahydroxycyclohexanone + NADH. CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl- CC CoA; acetyl-CoA from myo-inositol: step 1/7. CC -!- INDUCTION: By myo-inositol. CC -!- SIMILARITY: Belongs to the gfo/idh/mocA family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF059313; AAC70005.1; -; Genomic_DNA. DR EMBL; AL591985; CAC49594.1; -; Genomic_DNA. DR PIR; B95991; B95991. DR RefSeq; NP_437734.1; -. DR GeneID; 1237525; -. DR GenomeReviews; AL591985_GR; RB1194. DR KEGG; sme:SM_b20899; -. DR NMPDR; fig|266834.1.peg.5829; -. DR HOGENOM; O68965; -. DR OMA; O68965; LERYMQS. DR BioCyc; SMEL266834:SMB20899-MON; -. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000683; Oxidoreductase_N. DR InterPro; IPR004104; OxRdtase_C. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR Pfam; PF02894; GFO_IDH_MocA_C; 1. PE 1: Evidence at protein level; KW Complete proteome; NAD; Oxidoreductase; Plasmid. FT CHAIN 1 330 Inositol 2-dehydrogenase. FT /FTId=PRO_0000091775. FT CONFLICT 226 226 S -> A (in Ref. 1; AAC70005). 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 //