ID   MTLD_MAGO7              Reviewed;         400 AA.
AC   P0CT14; G4MS33; Q5EMU8;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            Short=M1PDH;
DE            Short=MPD;
DE            Short=MPDH;
DE            EC=1.1.1.17;
GN   ORFNames=MGG_10503;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose
CC       6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic
CC       pathway. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:61381; EC=1.1.1.17;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CM001231; EHA57499.1; -; Genomic_DNA.
DR   RefSeq; XP_003710111.1; XM_003710063.1.
DR   AlphaFoldDB; P0CT14; -.
DR   SMR; P0CT14; -.
DR   STRING; 318829.MGG_10503T0; -.
DR   EnsemblFungi; MGG_10503T0; MGG_10503T0; MGG_10503.
DR   GeneID; 2682115; -.
DR   KEGG; mgr:MGG_10503; -.
DR   VEuPathDB; FungiDB:MGG_10503; -.
DR   eggNOG; ENOG502QVPN; Eukaryota.
DR   HOGENOM; CLU_036089_0_1_1; -.
DR   OMA; GKKAVHF; -.
DR   OrthoDB; 1133390at2759; -.
DR   Proteomes; UP000009058; Chromosome 1.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR023028; Mannitol_1_phos_5_DH.
DR   InterPro; IPR000669; Mannitol_DH.
DR   InterPro; IPR013118; Mannitol_DH_C.
DR   InterPro; IPR013131; Mannitol_DH_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00084; MTLDHDRGNASE.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..400
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000371528"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000250"
FT   BINDING         12..23
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  44518 MW;  AAB005CB5590EADE CRC64;
     MSQTNGTHTK KAVHFGAGNI GRGFVACFLH NSGYEVVFAD VTDRTCDALN NQTSYKVIEV
     GAEGTEEKTI TNYRAINSKT KEDELLQEIA TADVVTCSVG PNILKFIAPV IAKGLDMRSE
     ELKPAAVIAC ENAIGATDTL AEHIKEHLPA TRVEDLSTRA RFANSAIDRI VPAQDPNSGL
     DVKLEKFYEW VVDRTPFADH EVPSIEGIHW VDNLEPYIER KLYTVNTGHA TAAYHGYNRQ
     KRTVYDALQD REIQSEVRRA LENTSKLITA KHGINPEEQQ AYVRKIMTRI GNPHLEDAVE
     RVGRAPLRKL SRKERFVGPA AELAEKGEDC SALLDAAEMA LRFQNVEEDA ESKELAKIMA
     ENSAEQVVSQ VCGLQPSEKL YPKMVEIVHR VQQDSMDDTE