ID   M2DH_NEOFI              Reviewed;         502 AA.
AC   A1CVQ6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Mannitol 2-dehydrogenase;
DE            Short=M2DH;
DE            Short=MDH;
DE            EC=1.1.1.67;
GN   ORFNames=NFIA_101920;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
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; DS027685; EAW24708.1; -; Genomic_DNA.
DR   RefSeq; XP_001266605.1; XM_001266604.1.
DR   AlphaFoldDB; A1CVQ6; -.
DR   SMR; A1CVQ6; -.
DR   STRING; 331117.A1CVQ6; -.
DR   EnsemblFungi; EAW24708; EAW24708; NFIA_101920.
DR   GeneID; 4593956; -.
DR   KEGG; nfi:NFIA_101920; -.
DR   VEuPathDB; FungiDB:NFIA_101920; -.
DR   eggNOG; ENOG502QT30; Eukaryota.
DR   HOGENOM; CLU_027324_0_1_1; -.
DR   OMA; IVASWAR; -.
DR   OrthoDB; 211204at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
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..502
FT                   /note="Mannitol 2-dehydrogenase"
FT                   /id="PRO_0000371546"
FT   BINDING         37..48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  56355 MW;  DD51019DF6C1F7D1 CRC64;
     MAPLKLNSKN LSQIAAAGGA LVKIPTYQRG RAVKEGIVHI GVGGFHRAHL AVYIDQLMQK
     HGVTDYAICG VGLQPFDSAM RDALASQDHL YTLIERSAKG SFAHVIGSIN SYLFAPDNRE
     AVIAKMAHPD TKIVSLTITE SGYYYNENTH ELQSEHPDIQ FDLDPANEKA PRTTFGFLYA
     GLTRRYQQGL KPFTVMSCDN MQKNGSITRH MLESFARLRN PEVAEWIAEE GAFPNAMVDR
     ITPQTSENDK TALADTFGIV DSWPVVTEPF TQWVIEDQFS NGRPPFEKVG VQVVKDVHAV
     EQFEKHKLRL LNGSHSALGY PGQLAGFKYV HEVMENPLFR KFVWQMMQEE VKPLLPEIPG
     VNIDEYCNTL IERFTNPTIM DQLPRICLNA SGKIPQFIMP SIAEAIWVTG PFRRLCFVAA
     AWFHYVKGVD DSGKPFEVVD PMREELQAKA RAGGNDPFEL LSIKSLFGDD LRSDERFLKE
     ITTAMNDIAR DGIMKTLPKY ID
//