M2DH_EMENI
ID M2DH_EMENI Reviewed; 502 AA.
AC Q5B9G5; C8VJH9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Mannitol 2-dehydrogenase;
DE Short=M2DH;
DE Short=MDH;
DE EC=1.1.1.67;
GN ORFNames=AN2815;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA62921.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000050; EAA62921.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF83955.1; -; Genomic_DNA.
DR RefSeq; XP_660419.1; XM_655327.1.
DR AlphaFoldDB; Q5B9G5; -.
DR SMR; Q5B9G5; -.
DR STRING; 162425.CADANIAP00010285; -.
DR EnsemblFungi; CBF83955; CBF83955; ANIA_02815.
DR EnsemblFungi; EAA62921; EAA62921; AN2815.2.
DR GeneID; 2874179; -.
DR KEGG; ani:AN2815.2; -.
DR VEuPathDB; FungiDB:AN2815; -.
DR eggNOG; ENOG502QT30; Eukaryota.
DR HOGENOM; CLU_027324_0_1_1; -.
DR InParanoid; Q5B9G5; -.
DR OMA; YKPYDNL; -.
DR OrthoDB; 1095102at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046029; F:mannitol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..502
FT /note="Mannitol 2-dehydrogenase"
FT /id="PRO_0000371544"
FT BINDING 37..48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 502 AA; 56583 MW; 8350C8EF792FCDEF CRC64;
MPPLKLNSKN LAAILNAGKG QIKVPTYPRN GAVKEGIVHI GVGGFHRAHL AVYIDRLMQN
HGVTDYAIAG VGLTPFDKKM RDILRSQDHL YTVIERSAKG SFANVVGSIN SFLFAPDDRE
AVVAKMAHPD THIVSLTITE SGYYYNENTH ELVSEHPDIQ FDLDPANEKT PRTTFGFLYA
ALARRFKQGL NPFTVMSCDN MQKNGAITRH MLESFARLRN PEIAEWISKK GHFPNAMVDR
ITPQTAPADI TALANDFGIQ DDWPVVTEPF MDWVIEDHFC DGRPPFEKVG VKVVKDLRAV
EEYEKHKLRL LNGSHSAIGY AGQLAGFQYV HEVLQNDTYK KFLWQMMQEE VKPLLPEIPG
VDIDEYCRTL IERFSNPTIK DQLPRICLNA SGKIPQFIMP SIAEAIWVTG PFRRLCFVAA
AWFRYLHGVD DAGNKFDIED PMLEELQAKA KAGGLEPHEI LSIKSLFGDD LRGDKRFLQE
ITTAMQLIDR DGVLKTMPKY VD
