ID   M2DH_PYRTR              Reviewed;         566 AA.
AC   B2W2N2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Mannitol 2-dehydrogenase;
DE            Short=M2DH;
DE            Short=MDH;
DE            EC=1.1.1.67;
GN   ORFNames=PTRG_03680;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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; DS231617; EDU46518.1; -; Genomic_DNA.
DR   RefSeq; XP_001934013.1; XM_001933978.1.
DR   AlphaFoldDB; B2W2N2; -.
DR   SMR; B2W2N2; -.
DR   STRING; 45151.EDU46518; -.
DR   EnsemblFungi; EDU46518; EDU46518; PTRG_03680.
DR   GeneID; 6341912; -.
DR   eggNOG; ENOG502QT30; Eukaryota.
DR   HOGENOM; CLU_027324_0_1_1; -.
DR   InParanoid; B2W2N2; -.
DR   OMA; YKPYDNL; -.
DR   OrthoDB; 1095102at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
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..566
FT                   /note="Mannitol 2-dehydrogenase"
FT                   /id="PRO_0000371548"
FT   BINDING         106..117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   566 AA;  62728 MW;  66AE6016BDE2FFA3 CRC64;
     MPPQVARNLL RAARARAVFQ STRPAHRRPA AISCRFQSTE AVRQTPSDVY QAPPRGFVPR
     KEEKFVPTQS RKAAPAATLK LNSKNLSSLQ NVSVPTYKRH GVKQGIVHVG VGGFHRAHLA
     AYVDTLLEQF NVQDWSICGV DLQPFAAPMR DALKPQDNLY TMIERAADGT SARVIGSITD
     YLFAPDSAEA VIAKMAHPDT HIVSMTVTES GYYMNENTHE LQIDHPDVAA DLAGEQPART
     VFGYLYAAMA RRHAAGLRPF TVLSCDNMQK NGDISRNMLV SFARHAGNNE VADWIASNGA
     FPNSMVDRIT PRTNDEDKVS LAKNFGVEDA WPVVTEPFHQ WVLEDKFVDG RPPFEKAGVQ
     IVPDVHQVEE YEMIKLRLLN GSHSAMGYAG QLAGFTYIHE VISHPVYRQF VINMMQQEVK
     PLLPQIPGVS VDDYCNTLLG RFSNPTLKDE LPRICLGGSG KIPQFIMPSI AEQIIAGGPL
     RRLTLVAAAW FRYNKGIDDA GNAFKVDDPM VEELQAKAAE GPIAQLQIKN LFGDDLRQDK
     RFVQELKTAL EGLEREGALA MIEKYA