ID   M2DH_PHANO              Reviewed;         568 AA.
AC   Q0UEB6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Mannitol 2-dehydrogenase;
DE            Short=M2DH;
DE            Short=MDH;
DE            EC=1.1.1.67;
GN   ORFNames=SNOG_09898;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445339; EAT83163.1; -; Genomic_DNA.
DR   RefSeq; XP_001800184.1; XM_001800132.1.
DR   AlphaFoldDB; Q0UEB6; -.
DR   SMR; Q0UEB6; -.
DR   STRING; 321614.Q0UEB6; -.
DR   EnsemblFungi; SNOT_09898; SNOT_09898; SNOG_09898.
DR   GeneID; 5977089; -.
DR   KEGG; pno:SNOG_09898; -.
DR   VEuPathDB; FungiDB:JI435_098980; -.
DR   eggNOG; ENOG502QT30; Eukaryota.
DR   HOGENOM; CLU_027324_0_1_1; -.
DR   InParanoid; Q0UEB6; -.
DR   OMA; IVASWAR; -.
DR   OrthoDB; 211204at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046029; F:mannitol dehydrogenase activity; IBA:GO_Central.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   PANTHER; PTHR43362:SF1; MANNITOL DEHYDROGENASE 2-RELATED; 1.
DR   PANTHER; PTHR43362; MANNITOL DEHYDROGENASE DSF1-RELATED; 1.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00084; MTLDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..568
FT                   /note="Mannitol 2-dehydrogenase"
FT                   /id="PRO_0000371547"
FT   BINDING         109..120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   568 AA;  63495 MW;  BF3CECA2C4156C92 CRC64;
     MFSYLPRYPL RAASARALVR ATRPSYRSAL LRYQSSEAVG RTQEIVPGAY QIPPRDFSRQ
     HEEKLAPKNA ARAPRRIEPA TLKLNSKNLS QLQNVTVPTY QREGVKQGIV HVGVGGFHRA
     HLAAYVDTLL EQFNSQDWSI CGVDLQPFAA PMRDALGSQD NLYTMIECDT EGTSARVIGS
     ITDYLFAPDN CEAVIAKMAH PDTHIVSMTV TESGYYMNEN THELQIDHPD IAADLAGQQP
     PRTVFAYLYA ALARRHAAGL RPFTVMSCDN MQKNGDISRN MLLAFARQQN PEVADWIAEN
     GAFPNSMVDR ITPRTSDENK AQLAQEFGVE DSWPVVTEVF HQWVLEDKFA DGRPPFEKAG
     VQVVPNVHKV EEYELIKLRL LNASHSAMGY AGYLGGFTYI HEVIADPTFR KYIRNMMQEE
     VQPLLPRIPG VSVDDYCNTL LGRFSNPTLK DELPRICLGG SGKIPQFIMP SIAEQIQAGG
     PLRRLTLCAA AWFRYLRGIN EQGQAFKLDD PMAEELQAKA LESPFSVLEV KSLFGDDLRD
     DKRFVAELKN ALESLERDGA RATIAQYA
//