M2DH_ASPFU
ID M2DH_ASPFU Reviewed; 502 AA.
AC Q4WQY4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Mannitol 2-dehydrogenase;
DE Short=M2DH;
DE Short=MDH;
DE EC=1.1.1.67 {ECO:0000269|PubMed:18983992};
GN ORFNames=AFUA_4G14450;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=18983992; DOI=10.1016/j.cbi.2008.10.001;
RA Krahulec S., Armao G.C., Bubner P., Klimacek M., Nidetzky B.;
RT "Polyol-specific long-chain dehydrogenases/reductases of mannitol
RT metabolism in Aspergillus fumigatus: biochemical characterization and pH
RT studies of mannitol 2-dehydrogenase and mannitol-1-phosphate 5-
RT dehydrogenase.";
RL Chem. Biol. Interact. 178:274-282(2009).
CC -!- FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose
CC and D-mannitol in the mannitol metabolic pathway. Has a preference for
CC NADH over NADPH. {ECO:0000269|PubMed:18983992}.
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 Evidence={ECO:0000269|PubMed:18983992};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 mM for D-mannitol (in the presence of NAD(+))
CC {ECO:0000269|PubMed:18983992};
CC KM=82 mM for D-mannitol (in the presence of NADP(+))
CC {ECO:0000269|PubMed:18983992};
CC KM=60 mM for D-fructose (in the presence of NADH)
CC {ECO:0000269|PubMed:18983992};
CC KM=159 mM for D-fructose (in the presence of NADPH)
CC {ECO:0000269|PubMed:18983992};
CC KM=0.019 mM for NADH {ECO:0000269|PubMed:18983992};
CC KM=0.15 mM for NAD(+) {ECO:0000269|PubMed:18983992};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18983992}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000005; EAL89350.1; -; Genomic_DNA.
DR RefSeq; XP_751388.1; XM_746295.1.
DR AlphaFoldDB; Q4WQY4; -.
DR SMR; Q4WQY4; -.
DR STRING; 746128.CADAFUBP00006987; -.
DR EnsemblFungi; EAL89350; EAL89350; AFUA_4G14450.
DR GeneID; 3509495; -.
DR KEGG; afm:AFUA_4G14450; -.
DR VEuPathDB; FungiDB:Afu4g14450; -.
DR eggNOG; ENOG502QT30; Eukaryota.
DR HOGENOM; CLU_027324_0_1_1; -.
DR InParanoid; Q4WQY4; -.
DR OMA; YKPYDNL; -.
DR OrthoDB; 1095102at2759; -.
DR BRENDA; 1.1.1.67; 508.
DR SABIO-RK; Q4WQY4; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0046029; F:mannitol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0019594; P:mannitol metabolic process; IC:UniProtKB.
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 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..502
FT /note="Mannitol 2-dehydrogenase"
FT /id="PRO_0000371540"
FT BINDING 37..48
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 502 AA; 56475 MW; 230384292D807EB1 CRC64;
MAPLKLNSRN LSQIAAAGGA LVKIPTYQRG RAVKEGIVHI GVGGFHRAHL AVYIDQLMQK
HGVNDYAICG VGLQPFDSAM RDALASQDHL YTLIERSAKG SFAHVIGSIN SYLFAPDNRE
AVIAKMAHPD TKIVSLTITE SGYYYNENTH ELQSEHPDIQ FDLDPANEKA PRTTFGFLYA
GLTRRYQQGL KPFTVMSCDN MQKNGSITRH MLESFARLRN PEVAEWIAEE GAFPNAMVDR
ITPQTSETDK TALAEKFGIV DSWPVVTEPF TQWVIEDQFS DGRPPFEKVG VQVVKDVHAV
EQFEKHKLRL LNGSHSALGY PGQLAGFQYV HEVMANPLFR KFVWQMMQEE VKPLLPEIPG
VDIDEYCNTL IERFTNPTIM DQLPRICLNA SGKIPQFIMP SIAEAIWETG PFRRLCFVAA
AWFHYIKGVD DRGKPFEVVD PMREELQAKA RAGGNDPSEL LSIKSLFGDD LRNDERFLRE
ITTAMNDIAR DGIMKTLPKY IN
