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 27-MAR-2024, entry version 111. 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 Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / OS Af293) (Neosartorya fumigata). 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 / CBS 101355 / FGSC A1100 / Af293; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHF01000005; EAL89350.1; -; Genomic_DNA. DR RefSeq; XP_751388.1; XM_746295.1. DR PDB; 7RK4; X-ray; 1.80 A; A/B=1-502. DR PDB; 7RK5; X-ray; 2.10 A; A/B=1-502. DR PDBsum; 7RK4; -. DR PDBsum; 7RK5; -. DR AlphaFoldDB; Q4WQY4; -. DR SMR; Q4WQY4; -. DR STRING; 330879.Q4WQY4; -. 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; IVASWAR; -. DR OrthoDB; 211204at2759; -. 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:0019594; P:mannitol metabolic process; IC:UniProtKB. 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 1: Evidence at protein level; KW 3D-structure; 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" FT TURN 8..10 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 11..17 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 44..48 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 50..61 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 68..72 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 78..85 FT /evidence="ECO:0007829|PDB:7RK4" FT TURN 86..89 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 91..97 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 100..106 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 119..127 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 140..143 FT /evidence="ECO:0007829|PDB:7RK4" FT TURN 147..150 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 157..163 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 174..187 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 194..197 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 204..217 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 221..230 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 236..239 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 247..257 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 272..277 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 286..289 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 297..310 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 312..325 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 330..335 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 337..349 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 352..354 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 363..375 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:7RK5" FT HELIX 383..387 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 394..397 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 399..407 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 413..425 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 443..452 FT /evidence="ECO:0007829|PDB:7RK4" FT STRAND 453..455 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 458..461 FT /evidence="ECO:0007829|PDB:7RK4" FT TURN 464..466 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 469..472 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 475..491 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 493..496 FT /evidence="ECO:0007829|PDB:7RK4" FT HELIX 497..500 FT /evidence="ECO:0007829|PDB:7RK4" 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 //