ID Q2KAX2_RHIEC Unreviewed; 299 AA. AC Q2KAX2; DT 07-MAR-2006, integrated into UniProtKB/TrEMBL. DT 07-MAR-2006, sequence version 1. DT 08-OCT-2025, entry version 107. DE SubName: Full=Probable myo-inositol 2-dehydrogenase protein {ECO:0000313|EMBL:ABC90014.1}; DE EC=1.1.1.18 {ECO:0000313|EMBL:ABC90014.1}; GN OrderedLocusNames=RHE_CH01209 {ECO:0000313|EMBL:ABC90014.1}; OS Rhizobium etli (strain ATCC 51251 / DSM 11541 / JCM 21823 / NBRC 15573 / OS CFN 42). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC90014.1, ECO:0000313|Proteomes:UP000001936}; RN [1] {ECO:0000313|EMBL:ABC90014.1, ECO:0000313|Proteomes:UP000001936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51251 / DSM 11541 / JCM 21823 / NBRC 15573 / CFN 42 RC {ECO:0000313|Proteomes:UP000001936}; RX PubMed=16505379; DOI=10.1073/pnas.0508502103; RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., RA Jimenez-Jacinto V., Collado-Vides J., Davila G.; RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in RT seven interacting replicons."; RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006). CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. CC {ECO:0000256|ARBA:ARBA00010928}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000133; ABC90014.1; -; Genomic_DNA. DR AlphaFoldDB; Q2KAX2; -. DR KEGG; ret:RHE_CH01209; -. DR eggNOG; COG0673; Bacteria. DR HOGENOM; CLU_023194_0_1_5; -. DR Proteomes; UP000001936; Chromosome. DR GO; GO:0050112; F:inositol 2-dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N. DR InterPro; IPR055170; GFO_IDH_MocA-like_dom. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR42840:SF3; BINDING ROSSMANN FOLD OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G10240)-RELATED; 1. DR PANTHER; PTHR42840; NAD(P)-BINDING ROSSMANN-FOLD SUPERFAMILY PROTEIN-RELATED; 1. DR Pfam; PF01408; GFO_IDH_MocA; 1. DR Pfam; PF22725; GFO_IDH_MocA_C3; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:ABC90014.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001936}. FT DOMAIN 3..84 FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal" FT /evidence="ECO:0000259|Pfam:PF01408" FT DOMAIN 97..209 FT /note="GFO/IDH/MocA-like oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF22725" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 299 AA; 33160 MW; 11FA5CC82AEB3C27 CRC64; MDADRARKVA DAYSAHEVDS DPDRVASRPD VDAVIIASPD FTHAPLSLSC IRAGKQALCE KPLSQSSNEC LEIMQAEEAA GSKFIMLGFM RRFDQSYVEM KQALERGAIG RALMMHNFHR NVATPASDFT GAMAITNSAP HEFDVVRHVL DTEYVSVSAF QPKRSDALVA PVYMVLETAD DQLVNIEINN NAAYGYDVRA ELVGEKATIA MNAVNYTRVD RELGQSTSYE ADWRGRYAEA YRRQNRAFVR FVETGVFPHI ASSSWDGYCA ARVAEAGVRA LNDGRKIPVE MIAKPEFYA //