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Database: UniProt
Entry: B2HR73_MYCMM
LinkDB: B2HR73_MYCMM
Original site: B2HR73_MYCMM 
ID   B2HR73_MYCMM            Unreviewed;       408 AA.
AC   B2HR73;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=inositol-3-phosphate synthase {ECO:0000256|ARBA:ARBA00012125};
DE            EC=5.5.1.4 {ECO:0000256|ARBA:ARBA00012125};
GN   OrderedLocusNames=MMAR_2508 {ECO:0000313|EMBL:ACC40959.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC40959.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC40959.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 1/2. {ECO:0000256|ARBA:ARBA00005117}.
CC   -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC       {ECO:0000256|ARBA:ARBA00010813}.
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DR   EMBL; CP000854; ACC40959.1; -; Genomic_DNA.
DR   RefSeq; WP_012394248.1; NC_010612.1.
DR   AlphaFoldDB; B2HR73; -.
DR   STRING; 216594.MMAR_2508; -.
DR   KEGG; mmi:MMAR_2508; -.
DR   eggNOG; COG1260; Bacteria.
DR   HOGENOM; CLU_021486_0_0_11; -.
DR   OrthoDB; 729130at2; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0006021; P:inositol biosynthetic process; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR   InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11510:SF5; INOSITOL-3-PHOSPHATE SYNTHASE 1; 1.
DR   PANTHER; PTHR11510; MYO-INOSITOL-1 PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF01658; Inos-1-P_synth; 1.
DR   Pfam; PF07994; NAD_binding_5; 1.
DR   PIRSF; PIRSF015578; Myoinos-ppht_syn; 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   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT   DOMAIN          238..342
FT                   /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT                   /evidence="ECO:0000259|Pfam:PF01658"
SQ   SEQUENCE   408 AA;  42552 MW;  A030ED29BDC51F86 CRC64;
     MNRDRARSEA TAGQRCGLWL SGARGSVATT SIVGLYALSA GLVSETGCVT SNADFADVPL
     PNYSDFVVGG RDLSTTSLVK RAETLVEAGL LPHQVVATLS DRLAATDDEI VGPSCVATPD
     PCSAGASTQA ELIDRLCDAM ASFVSRHGLD GLVVIDVAST QPPVADLPEY RDPQLLRLAL
     GEKNRALLPA SALTALAAIR TGAAYACFTP SPSLGIPALR QLAAEADISY AGQDAKTGQT
     LLRTVLAPMF ASRAMNVHSW AGSNLLGGGD GATLADPVAV QSKLASKQRG IQQMLGGHVT
     APLHIDYVPD LGETKVAWDF IHATGFLGGQ ITLQTTWSAP DSALAAPLVL DVARLLSMAR
     MRGAQGVVGE LGFFFKEPWG SSTHSLAAQY EALHQWANSF STPDSAEL
//
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