ID A0A017HNF3_9RHOB Unreviewed; 283 AA.
AC A0A017HNF3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Myo-inositol 2-dehydrogenase {ECO:0000313|EMBL:EYD75901.1};
DE EC=1.1.1.18 {ECO:0000313|EMBL:EYD75901.1};
GN ORFNames=Rumeso_02519 {ECO:0000313|EMBL:EYD75901.1};
OS Rubellimicrobium mesophilum DSM 19309.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD75901.1, ECO:0000313|Proteomes:UP000019666};
RN [1] {ECO:0000313|EMBL:EYD75901.1, ECO:0000313|Proteomes:UP000019666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD75901.1,
RC ECO:0000313|Proteomes:UP000019666};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYD75901.1}.
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DR EMBL; AOSK01000064; EYD75901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A017HNF3; -.
DR STRING; 442562.Rumeso_02519; -.
DR PATRIC; fig|442562.3.peg.2483; -.
DR HOGENOM; CLU_023194_19_1_5; -.
DR Proteomes; UP000019666; Unassembled WGS sequence.
DR GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43708; CONSERVED EXPRESSED OXIDOREDUCTASE (EUROFUNG); 1.
DR PANTHER; PTHR43708:SF5; CONSERVED EXPRESSED OXIDOREDUCTASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF02894; GFO_IDH_MocA_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:EYD75901.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019666}.
FT DOMAIN 2..58
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 72..246
FT /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02894"
FT REGION 250..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 283 AA; 30820 MW; 03B077DDA1C05AAD CRC64;
MDAVTVTTPP ETRRELVLEA IAAGLHVIAD KPFAPSAEGG RELEAAAKAK GVILSVFHNR
RWDSDMRTLR KVVSDGCLGP LWRVHSRMDL DQPSTLEAGP TGGLLRDLGS HLVDQMLWLL
GPVRAVDAQL DFLDLPQGRT DAGFTLTLRH ESGTHSHLSA SKLNRLAMRE LRAYGQAGSY
VASSTDVQAQ SIFAGRRPTQ DLSGWGFEPR TSWGILRTAA GEVEVPAEQG RYHDFYAAFA
HAIHDGAAAP VTAAEDDRCS DRARRSPSER PRRALHRALA GHP
//