ID   M2DH_ASPFC              Reviewed;         502 AA.
AC   B0Y581;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Mannitol 2-dehydrogenase;
DE            Short=M2DH;
DE            Short=MDH;
DE            EC=1.1.1.67;
GN   ORFNames=AFUB_071700;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499598; EDP50830.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y581; -.
DR   SMR; B0Y581; -.
DR   EnsemblFungi; EDP50830; EDP50830; AFUB_071700.
DR   VEuPathDB; FungiDB:AFUB_071700; -.
DR   HOGENOM; CLU_027324_0_1_1; -.
DR   PhylomeDB; B0Y581; -.
DR   Proteomes; UP000001699; 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.
FT   CHAIN           1..502
FT                   /note="Mannitol 2-dehydrogenase"
FT                   /id="PRO_0000371539"
FT   BINDING         37..48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  56475 MW;  230384292D807EB1 CRC64;
     MAPLKLNSRN LSQIAAAGGA LVKIPTYQRG RAVKEGIVHI GVGGFHRAHL AVYIDQLMQK
     HGVNDYAICG VGLQPFDSAM RDALASQDHL YTLIERSAKG SFAHVIGSIN SYLFAPDNRE
     AVIAKMAHPD TKIVSLTITE SGYYYNENTH ELQSEHPDIQ FDLDPANEKA PRTTFGFLYA
     GLTRRYQQGL KPFTVMSCDN MQKNGSITRH MLESFARLRN PEVAEWIAEE GAFPNAMVDR
     ITPQTSETDK TALAEKFGIV DSWPVVTEPF TQWVIEDQFS DGRPPFEKVG VQVVKDVHAV
     EQFEKHKLRL LNGSHSALGY PGQLAGFQYV HEVMANPLFR KFVWQMMQEE VKPLLPEIPG
     VDIDEYCNTL IERFTNPTIM DQLPRICLNA SGKIPQFIMP SIAEAIWETG PFRRLCFVAA
     AWFHYIKGVD DRGKPFEVVD PMREELQAKA RAGGNDPSEL LSIKSLFGDD LRNDERFLRE
     ITTAMNDIAR DGIMKTLPKY IN