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Database: UniProt
Entry: A1TC45_MYCVP
LinkDB: A1TC45_MYCVP
Original site: A1TC45_MYCVP 
ID   A1TC45_MYCVP            Unreviewed;       342 AA.
AC   A1TC45;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Inositol 2-dehydrogenase {ECO:0000313|EMBL:ABM14745.1};
DE            EC=1.1.1.18 {ECO:0000313|EMBL:ABM14745.1};
GN   OrderedLocusNames=Mvan_3968 {ECO:0000313|EMBL:ABM14745.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM14745.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM14745.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC       {ECO:0000256|ARBA:ARBA00010928}.
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DR   EMBL; CP000511; ABM14745.1; -; Genomic_DNA.
DR   RefSeq; WP_011781125.1; NZ_JACKSD010000018.1.
DR   AlphaFoldDB; A1TC45; -.
DR   STRING; 350058.Mvan_3968; -.
DR   KEGG; mva:Mvan_3968; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_0_2_11; -.
DR   Proteomes; UP000009159; Chromosome.
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; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABM14745.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159}.
FT   DOMAIN          4..119
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          131..333
FT                   /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02894"
SQ   SEQUENCE   342 AA;  36033 MW;  AB3D9F3AA7CCB939 CRC64;
     MTTLGLIGLG RIGAFHAETL TNLPEVSGLV VTDERPEVVS QLATKYGATP ANSVQELLAS
     GVDGVIVAAA TPAHAELTLA AVERGLPTFC EKPIAATAAE SARVGEVITR SGVPVQVGYQ
     RRFDAAFAAV KHAVDDGSLG ALHTVRSTTM DPAPPPMDYI KGSGGIFRDC AVHDFDVIRW
     VTGQNVVDVY ATGSVQGDPR FAEYGDVDTA AVVVRFDGGA LGVVSAARYN GRGYDCRLEV
     HGFDDTVVAG WDQGAPVRNA DPDFSSPGAF PAGPPHHFFM DRFTEAFRAE LRAFVDVVEG
     GPIRGATVAD AVEVAWIAEA ATESLRRGVP VTIESVRKET QQ
//
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