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Database: UniProt
Entry: A0A0J1CIB8_9BURK
LinkDB: A0A0J1CIB8_9BURK
Original site: A0A0J1CIB8_9BURK 
ID   A0A0J1CIB8_9BURK        Unreviewed;       345 AA.
AC   A0A0J1CIB8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Inositol 2-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
DE            EC=1.1.1.18 {ECO:0000256|HAMAP-Rule:MF_01671};
DE   AltName: Full=Myo-inositol 2-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
DE            Short=MI 2-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01671};
GN   Name=iolG {ECO:0000256|HAMAP-Rule:MF_01671};
GN   ORFNames=EOS_41765 {ECO:0000313|EMBL:KLU20417.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU20417.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU20417.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT   Ability.";
RL   Genome Announc. 3:e00798-15(2015).
CC   -!- FUNCTION: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-
CC       inositol (2KMI or 2-inosose). {ECO:0000256|HAMAP-Rule:MF_01671}.
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:0000256|HAMAP-Rule:MF_01671};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01671}.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01671}.
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:KLU20417.1}.
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DR   EMBL; AEJF01000258; KLU20417.1; -; Genomic_DNA.
DR   RefSeq; WP_047898140.1; NZ_AEJF01000258.1.
DR   AlphaFoldDB; A0A0J1CIB8; -.
DR   PATRIC; fig|908627.4.peg.9388; -.
DR   OrthoDB; 8565814at2; -.
DR   Proteomes; UP000035963; Unassembled WGS sequence.
DR   GO; GO:0050112; F:inositol 2-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01671; IolG; 1.
DR   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR023794; MI/DCI_dehydrogenase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43593; -; 1.
DR   PANTHER; PTHR43593:SF1; INOSITOL 2-DEHYDROGENASE; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_C; 2.
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   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01671};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01671}.
FT   DOMAIN          5..125
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          138..238
FT                   /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02894"
FT   DOMAIN          270..327
FT                   /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02894"
SQ   SEQUENCE   345 AA;  37631 MW;  C0F1C53B8E523F13 CRC64;
     MRNELRVAVV GAGLMGSDHV ERLANRIAGA SVVAVVDVDA ERAQRVASKA PGAIAATELG
     SLLTGDRIDA VVIATPGFLH EKTLLQAIEQ GKPILCEKPL TPDAASSWRI IEEEQKIGRK
     LIQVGFMRRF DREYRQLRRL IESREMGDTL MLHFSHRNAV SPSSFTSQML INDSVVHEFD
     GVRYLTGEEI TTVQVRLGRP TRHAHHGQHD PQQVLMETES GILVDVEIFV NAQFGYQVAA
     QAVFEDGIVD IGNDIGPYIR SSGRWGGAVP PSFVERFNDA FNLELQTWVD AAREGTVNGP
     SAWDGYATAA CCEAGVAAQK TGQKVKVALN EKPALYSDEK VATAA
//
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