ID   M2DH_ASPOR              Reviewed;         502 AA.
AC   Q2U100;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Mannitol 2-dehydrogenase;
DE            Short=M2DH;
DE            Short=MDH;
DE            EC=1.1.1.67;
GN   ORFNames=AO090011000230;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007171; BAE64765.1; -; Genomic_DNA.
DR   RefSeq; XP_001825898.1; XM_001825846.2.
DR   AlphaFoldDB; Q2U100; -.
DR   SMR; Q2U100; -.
DR   STRING; 510516.Q2U100; -.
DR   EnsemblFungi; BAE64765; BAE64765; AO090011000230.
DR   GeneID; 5998001; -.
DR   KEGG; aor:AO090011000230; -.
DR   VEuPathDB; FungiDB:AO090011000230; -.
DR   HOGENOM; CLU_027324_0_1_1; -.
DR   OMA; IVASWAR; -.
DR   OrthoDB; 211204at2759; -.
DR   Proteomes; UP000006564; Chromosome 7.
DR   GO; GO:0005576; C:extracellular region; IDA:AspGD.
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_0000371542"
FT   BINDING         37..48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  56251 MW;  B34B1957B39B630E CRC64;
     MAPLKLNNKN LSQIAAAGET QVKVPTYKRG GDVKEGIVHV GVGGFHRAHL AVYVDQLMQK
     HGVTDYAICG VGLQPFDAAM RDALGSQDHL YTVIERSAKG SFAHVVGSIN SYLFAPDNRE
     AVIAKMAHPD THIVSLTITE SGYYYNENTH ELQSEHPDIQ FDLQPANEKS PRTTFGFLYA
     ALARRYQQGL KPFTVMSCDN MQKNGSITRH MLESFARLRN PEIAKWIAEQ GAFPNAMVDR
     ITPQTSATDK TALADNFAIE DSWPVVTEPF MQWVIEDQFS DGRPPFEKVG AQVVKNVHDV
     EEFEKHKLRL LNGSHSAIGY PGQLAGFKYV HEVMENPLFS KFVWQMMQDE VKPLLPEIPG
     VNIDEYCKTL IERFSNPTIM DQLPRICLNA SGKIPQFIMP SIAEAIWVTG PFRRLCFVAA
     AWFHYINGVD DSGKKFEVDD PMREELQAKA RAGGTSPAEL LSIKSLFGDD LRGDKRFLQE
     ITKAMEDIAR DGILKTLPKY ID
//