ID   M2DH_ASPTN              Reviewed;         502 AA.
AC   Q0CYP4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Mannitol 2-dehydrogenase;
DE            Short=M2DH;
DE            Short=MDH;
DE            EC=1.1.1.67;
GN   ORFNames=ATEG_01190;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476595; EAU37947.1; -; Genomic_DNA.
DR   RefSeq; XP_001208555.1; XM_001208555.1.
DR   AlphaFoldDB; Q0CYP4; -.
DR   SMR; Q0CYP4; -.
DR   STRING; 341663.Q0CYP4; -.
DR   EnsemblFungi; EAU37947; EAU37947; ATEG_01190.
DR   GeneID; 4316123; -.
DR   VEuPathDB; FungiDB:ATEG_01190; -.
DR   eggNOG; ENOG502QT30; Eukaryota.
DR   HOGENOM; CLU_027324_0_1_1; -.
DR   OMA; IVASWAR; -.
DR   OrthoDB; 211204at2759; -.
DR   Proteomes; UP000007963; 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_0000371543"
FT   BINDING         37..48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  56515 MW;  CF961F095B9A5226 CRC64;
     MAPLKLNSRN LAQIFAAGKD RVKVPTYQRG SAVKEGIVHV GVGGFHRAHL AVYVDQLMQN
     HGVNDYAICG VGLQPFDAAM RDALRSQDHL YTVIERSAKG SFAHVVGSIN SYLFAPDNRE
     AVIAKMAHPD THIVSLTITE SGYYYNENTH ELQAEHPDIQ FDLDPANEKT PRTTFGFLYA
     ALARRHQQGL RPFTVLSCDN MQKNGSITRH MLESFARLRN PELAKWIAEQ GAFPNAMVDR
     ITPQTSPTDK KALAETIGIE DSWPVVTEPF MQWVLEDQFS DGRPPFEKAG AQVVKNVHDV
     EQFEKHKLRL LNGSHSAIGY AGQMAGFEYV HEVMEHPLYN RFVWQMMQEE VKPLLPEIPG
     VDIDEYCKTL MERFSNPTIM DQLPRICLNA SGKIPQFIMP SIAEAIWVTG PFRRLCFVAA
     AWFRYLNGID DSGKTFNVDD PMREELQAKA RAGGTNPAEL LNVKSLFGDD LRSDKRFLQE
     ITTAMEAIAR DGIMKTMPKY VD
//