ID   M2DH_ASPNC              Reviewed;         488 AA.
AC   A2QGA1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   13-SEP-2023, entry version 81.
DE   RecName: Full=Mannitol 2-dehydrogenase;
DE            Short=M2DH;
DE            Short=MDH;
DE            EC=1.1.1.67;
GN   ORFNames=An03g02430;
OS   Aspergillus niger (strain ATCC MYA-4892 / 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=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
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       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; AM270048; CAK38211.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QGA1; -.
DR   SMR; A2QGA1; -.
DR   EnsemblFungi; CAK38211; CAK38211; An03g02430.
DR   VEuPathDB; FungiDB:An03g02430; -.
DR   HOGENOM; CLU_027324_0_1_1; -.
DR   Proteomes; UP000006706; Chromosome 6R.
DR   GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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..488
FT                   /note="Mannitol 2-dehydrogenase"
FT                   /id="PRO_0000371541"
FT   BINDING         37..48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   488 AA;  54803 MW;  47DE72CE48497048 CRC64;
     MGPLKLNTAN LSQIVAAGAG RVKVPTYRRG PALKEGIVHV GVGGFHRAHL AVYVDQLMQN
     HGVTDYAICG VGLQPFDSAM RDALSSQDNL YTVIERSAKG SFANVIGSIN SYLFAPDDRE
     AVIAKMAHPD TRIVSLTITE SGYYYNENTH ELQSEHPDIQ FDLDPANEKT PRTTFGFLYA
     ALARRHQQEE WFHHPSHARV FRPSPHPEVA QWITDKGAFP NAMVDRITPQ TSPADKESLA
     NTMGIEDSWP VVTEPFMQWV IEDQFSDGRP PFEKVGVQVV KDVHAVEEFE KHKLRLLNGS
     HSAIGYPGQM AGFNYVHEVL ENPDFNKFVW QMMQEEVKPS LPEIPGVDID QYCKTLMERF
     SNPTIMDQLP RICLNASGKI PQFIMPSIAE AIWVKGPLRR LCFVAAAWFR YINGVDDQGN
     TFTVDDPMRE ELQAKARAGG TKPSELLSIT SLFGDDLRND KRFMQEITNA MEDIARDGIL
     KTLPKYID
//