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Database: UniProt
Entry: F5XJE0_MICPN
LinkDB: F5XJE0_MICPN
Original site: F5XJE0_MICPN 
ID   F5XJE0_MICPN            Unreviewed;       338 AA.
AC   F5XJE0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
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=idh {ECO:0000313|EMBL:BAK35840.1};
GN   Synonyms=iolG {ECO:0000256|HAMAP-Rule:MF_01671,
GN   ECO:0000313|EMBL:BAK35840.1};
GN   OrderedLocusNames=MLP_28260 {ECO:0000313|EMBL:BAK35840.1};
OS   Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS   101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Microlunatus.
OX   NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK35840.1, ECO:0000313|Proteomes:UP000007947};
RN   [1] {ECO:0000313|EMBL:BAK35840.1, ECO:0000313|Proteomes:UP000007947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC   / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA   Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA   Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00010928, ECO:0000256|HAMAP-Rule:MF_01671}.
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DR   EMBL; AP012204; BAK35840.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5XJE0; -.
DR   STRING; 1032480.MLP_28260; -.
DR   KEGG; mph:MLP_28260; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_1_11; -.
DR   OMA; RKPVMCE; -.
DR   Proteomes; UP000007947; Chromosome.
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; 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; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000007947}.
FT   DOMAIN          6..125
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          138..327
FT                   /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02894"
SQ   SEQUENCE   338 AA;  36160 MW;  DE46CEFEA461A0B9 CRC64;
     MKLTDLRVAV LGLGLMGSFH TELLTSRIRG VQVTVVNDFV QAKAEEVAAR IGARVVADPI
     EAIKDPEVDA VLLATPGNTH AEQVNACLDA GKPVLCEKPL TTDVDSAYAI VAKEAALGKQ
     LIQVGFMRRF DAEYAALREL IVDGGLGNPL MVHCTHRNPA VPPHFNSEFM IRDSVVHEVD
     VARFLLGEEI ASVQVIKGVA TSTAPEGTND PMLVIFEMTS GRIVTDEIYV RTGVAYEVRT
     EVVGESGSAL IGLDQNLQVK STDGRWGGRI TPGFVERFGQ AYAVELQRWV DAAGQGTIDG
     PGAWDGYAAV AVCEAGVQAL TVDGKVEVQL QTRPEAAR
//
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