ID   MTLD_ALTAL              Reviewed;         390 AA.
AC   Q6UQ76;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            Short=M1PDH;
DE            Short=MPD;
DE            Short=MPDH;
DE            EC=1.1.1.17;
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17092745; DOI=10.1016/j.fgb.2006.09.008;
RA   Velez H., Glassbrook N.J., Daub M.E.;
RT   "Mannitol metabolism in the phytopathogenic fungus Alternaria alternata.";
RL   Fungal Genet. Biol. 44:258-268(2007).
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. Has a strong preference for NADH over NADPH.
CC       {ECO:0000269|PubMed:17092745}.
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; AY364263; AAQ63948.1; -; Genomic_DNA.
DR   RefSeq; XP_018390108.1; XM_018526447.1.
DR   AlphaFoldDB; Q6UQ76; -.
DR   SMR; Q6UQ76; -.
DR   GeneID; 29112041; -.
DR   KEGG; aalt:CC77DRAFT_1028464; -.
DR   OMA; GKKAVHF; -.
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.
FT   CHAIN           1..390
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000371517"
FT   ACT_SITE        216
FT                   /evidence="ECO:0000250"
FT   BINDING         7..18
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  43550 MW;  A98836F5940BFEC6 CRC64;
     MSYEKKAVHF GGGNIGRGFV AEFLHNSGYE VVFVDVMDSI IESLQKTKTY TVTEIGDDGE
     RKFTIDHYRA INSKHEMDKV VQEIASADVV TCAVGPNILK FVAEPVAKAI EARTLDYPIA
     VIACENAINA TTTWRGFIES KLSEETKKNI DSKARFANSA IDRIVPQQPP NGGLDVVIEK
     FHEWCVEQKP FENGGKKPDV KGIHYVDDLE PYIERKLFTV NTSHATAAYY GHQNKVQYIH
     EVLHDKKLHD TVRDAVKETA HLIVTKHGVE TAEQDAYVEE IIKRISNPVL KDNVERVGRA
     PLRKLSRKER FIGPAAQLAE RGEKVDALLG AVEQAYRFQN VEGDEESVEL AKILKENSAE
     EVVTKVNGIE KGQPLFDRLV AIVKKVQGGS