MTLD_ASPFU
ID MTLD_ASPFU Reviewed; 388 AA.
AC Q4X1A4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE Short=M1PDH;
DE Short=MPD;
DE Short=MPDH;
DE EC=1.1.1.17 {ECO:0000269|PubMed:18452897, ECO:0000269|PubMed:18983992};
GN Name=mpdA; ORFNames=AFUA_2G10660;
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, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=18452897; DOI=10.1016/j.carres.2008.04.011;
RA Krahulec S., Armao G.C., Weber H., Klimacek M., Nidetzky B.;
RT "Characterization of recombinant Aspergillus fumigatus mannitol-1-phosphate
RT 5-dehydrogenase and its application for the stereoselective synthesis of
RT protio and deuterio forms of D-mannitol 1-phosphate.";
RL Carbohydr. Res. 343:1414-1423(2008).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-213, FUNCTION, AND
RP 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 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic
CC pathway. Has a strong preference for NADH over NADPH.
CC {ECO:0000269|PubMed:18452897, ECO:0000269|PubMed:18983992}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61381; EC=1.1.1.17;
CC Evidence={ECO:0000269|PubMed:18452897, ECO:0000269|PubMed:18983992};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 mM for D-mannitol 1-phosphate {ECO:0000269|PubMed:18452897,
CC ECO:0000269|PubMed:18983992};
CC KM=2.1 mM for D-fructose 6-phosphate {ECO:0000269|PubMed:18452897,
CC ECO:0000269|PubMed:18983992};
CC KM=0.016 mM for NADH {ECO:0000269|PubMed:18452897,
CC ECO:0000269|PubMed:18983992};
CC KM=0.75 mM for NAD(+) {ECO:0000269|PubMed:18452897,
CC ECO:0000269|PubMed:18983992};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18452897}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000001; EAL93361.1; -; Genomic_DNA.
DR RefSeq; XP_755399.1; XM_750306.1.
DR AlphaFoldDB; Q4X1A4; -.
DR SMR; Q4X1A4; -.
DR STRING; 746128.CADAFUBP00002584; -.
DR SwissPalm; Q4X1A4; -.
DR PRIDE; Q4X1A4; -.
DR EnsemblFungi; EAL93361; EAL93361; AFUA_2G10660.
DR GeneID; 3513687; -.
DR KEGG; afm:AFUA_2G10660; -.
DR VEuPathDB; FungiDB:Afu2g10660; -.
DR eggNOG; ENOG502QVPN; Eukaryota.
DR HOGENOM; CLU_036089_0_1_1; -.
DR InParanoid; Q4X1A4; -.
DR OMA; GKKAVHF; -.
DR OrthoDB; 1133390at2759; -.
DR BRENDA; 1.1.1.17; 508.
DR SABIO-RK; Q4X1A4; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0019592; P:mannitol catabolic process; IBA:GO_Central.
DR GO; GO:0019594; P:mannitol metabolic process; IC:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR023028; Mannitol_1_phos_5_DH.
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; Oxidoreductase; Reference proteome.
FT CHAIN 1..388
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000371520"
FT ACT_SITE 213
FT BINDING 5..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MUTAGEN 213
FT /note="K->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:18983992"
SQ SEQUENCE 388 AA; 43004 MW; EE8F7B90FAFC3B3F CRC64;
MGKKAIQFGG GNIGRGFVAE FLHEAGYEVV FIDVVDKIID ALKSTPSYEV TEVSEEGEKT
KTITNYRAIN SKTNEEDVVK EIGTADVVTC AVGPNVLKFI APVIAKGIDA RTASKPVAVI
ACENAIGATD TLRGFIEQNT DKDRLSSMSE RARFANSAID RIVPNQPPNA GLNVRIEKFY
EWTVEQTPFG EFGHPDIPAI HWVDDLKPYI ERKLFTVNTG HATTAYYGHM RGKKMIADAL
ADAEIRQIVH KVLEQTAKLI TTKHEITEQE QNEYVDTIVK RMSNPFLEDN VERVGRAPLR
KLSRNERFIG PASQLAEKGL PFDALLGSIE MALRFQNVPG DEESAELAKI LKEMSAEEAT
GKLTGLEKHH PLYEPVQNVI AKVQKDSK
