ID   M2DH_MAGO7              Reviewed;         502 AA.
AC   A4QQN1; G4NJS3; Q2KEC3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Mannitol 2-dehydrogenase;
DE            Short=M2DH;
DE            Short=MDH;
DE            EC=1.1.1.67;
GN   ORFNames=MGCH7_ch7g1113, MGG_10334;
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;
RA   Thon M.R., Pan H., Diener A., Papalas J., Taro A., Mitchell T.K.,
RA   Dean R.A.;
RT   "The sequence of Magnaporthe grisea chromosome 7.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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       and D-mannitol in the mannitol metabolic pathway. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol + NAD(+) = D-fructose + H(+) + NADH;
CC         Xref=Rhea:RHEA:12084, ChEBI:CHEBI:15378, ChEBI:CHEBI:16899,
CC         ChEBI:CHEBI:37721, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.67;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CM000230; EAQ71706.1; -; Genomic_DNA.
DR   EMBL; CM001237; EHA45740.1; -; Genomic_DNA.
DR   RefSeq; XP_003720483.1; XM_003720435.1.
DR   AlphaFoldDB; A4QQN1; -.
DR   SMR; A4QQN1; -.
DR   STRING; 318829.MGG_10334T0; -.
DR   PRIDE; A4QQN1; -.
DR   EnsemblFungi; MGG_10334T0; MGG_10334T0; MGG_10334.
DR   GeneID; 2681909; -.
DR   KEGG; mgr:MGG_10334; -.
DR   VEuPathDB; FungiDB:MGG_10334; -.
DR   eggNOG; ENOG502QT30; Eukaryota.
DR   HOGENOM; CLU_027324_0_1_1; -.
DR   InParanoid; A4QQN1; -.
DR   OMA; YKPYDNL; -.
DR   OrthoDB; 1095102at2759; -.
DR   Proteomes; UP000009058; Chromosome 7.
DR   GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
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..502
FT                   /note="Mannitol 2-dehydrogenase"
FT                   /id="PRO_0000371545"
FT   BINDING         35..46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  56499 MW;  F1D96C12DBDB7858 CRC64;
     MAFKLSTKHL ADIGAQTEKS IRIPSYDRND VKEGIVHVGV GGFHRAHLAV YVDKLMQSHG
     VRDYAICGVG LQPADASMRD VLASQDHMYT VIERSAAGST AHVVGSIRNF LFAPDDREAV
     IAKMAHPDTH IVSLTITESG YYYNENTHEL QSEHPDIQHD LDPANAAKPK TTFGFLYAAM
     VRRREQGLKP FTVLSCDNML KNGSITRNML QSFAKLKDPS MADWIAQYGG FPNAMVDRIT
     PRTSDPDIKE LADKFKIDDA WPVVTEPFMQ WVVEDKFADG RPPFDLVGVQ VVKDVKDVEQ
     FEKHKLRLLN ASHSAMGYPG QLAGFKYVHE VMEHPLYRKF IWQMMQEEVK PLLPEIPGVD
     IDAYCNTLME RFSNPTIMDQ LPRIALNSSG KMPQFVMPSI AEAIWVTGPF RRLVFVAACW
     FRYVLGVDDK GNKFEVDDPM REELQSKAQA GGTKPHEILS IKSLFGDDLR GDERFLKEVT
     QAMEDIARDG VMATMPKFVN DA