ID   MTLD_ASPNC              Reviewed;         388 AA.
AC   A2QD49;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            Short=M1PDH;
DE            Short=MPD;
DE            Short=MPDH;
DE            EC=1.1.1.17;
GN   Name=mpdA; ORFNames=An02g05830;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose
CC       6-phosphate and D-mannitol 1-phosphate in the metabolism of mannitol.
CC       Has a strong preference for NADH over NADPH (By similarity).
CC       {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; AM270011; CAK47711.1; -; Genomic_DNA.
DR   RefSeq; XP_001399719.1; XM_001399682.2.
DR   AlphaFoldDB; A2QD49; -.
DR   SMR; A2QD49; -.
DR   PaxDb; A2QD49; -.
DR   EnsemblFungi; CAK47711; CAK47711; An02g05830.
DR   GeneID; 4979072; -.
DR   KEGG; ang:ANI_1_802024; -.
DR   VEuPathDB; FungiDB:An02g05830; -.
DR   HOGENOM; CLU_036089_0_1_1; -.
DR   Proteomes; UP000006706; Chromosome 4R.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034605; P:cellular response to heat; IMP:AspGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:AspGD.
DR   GO; GO:0019593; P:mannitol biosynthetic process; IMP:AspGD.
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..388
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000371521"
FT   ACT_SITE        213
FT                   /evidence="ECO:0000250"
FT   BINDING         5..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  43231 MW;  310A8C21416DD6D0 CRC64;
     MGKKAIQFGG GNIGRGFVAE FLHKAGYEVV FVDVMDKMVE ALQQNKSYKV TEVSEEGEHT
     TTITNYRAIN SKTHESDVIQ EIATADVVTC AVGPNILKFI APVIAKGIDA RTESKPVAVI
     ACENAIGATD TLHGFIKQHT SQDRVESLYD RAQFANSAID RIVPQQAPNS GLDVRIEKFY
     EWAVEKTPFG SVGHPDIPAI HWVDNLEPYI ERKLFTVNTS HATTAYFGHF RGKKMIADAL
     EDKEIRGLVH KVLEETASLI VAKHDISEEE QKEYVEKIVS RISNPYLEDN VDRVGRAPLR
     KLSRKERFIG PASQLAERGM KYDSLMDAVE MALRFQNVPG DDESAELANI LQEQPAEDAT
     TNLTGLEKEH PLYPAVLDRV RKVQQGTK