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
//
