MTLD_ASPNG
ID MTLD_ASPNG Reviewed; 388 AA.
AC Q8NJJ1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 77.
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:7030216};
GN Name=mpdA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=12912888; DOI=10.1128/ec.2.4.690-698.2003;
RA Ruijter G.J.G., Bax M., Patel H., Flitter S.J., van de Vondervoort P.J.I.,
RA de Vries R.P., vanKuyk P.A., Visser J.;
RT "Mannitol is required for stress tolerance in Aspergillus niger
RT conidiospores.";
RL Eukaryot. Cell 2:690-698(2003).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=7030216; DOI=10.1016/0003-9861(81)90496-3;
RA Kiser R.C., Niehaus W.G. Jr.;
RT "Purification and kinetic characterization of mannitol-1-phosphate
RT dehydrogenase from Aspergillus niger.";
RL Arch. Biochem. Biophys. 211:613-621(1981).
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. Required for
CC protection of conidiospores against exogenous stresses such as high
CC temperatures and an oxidative environment.
CC {ECO:0000269|PubMed:12912888, ECO:0000269|PubMed:7030216}.
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:7030216};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.038 mM for D-mannitol 1-phosphate {ECO:0000269|PubMed:7030216};
CC KM=0.54 mM for D-fructose 6-phosphate {ECO:0000269|PubMed:7030216};
CC KM=0.005 mM for NADH {ECO:0000269|PubMed:7030216};
CC KM=0.083 mM for NAD(+) {ECO:0000269|PubMed:7030216};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INDUCTION: Strongly induced at the onset of sporulation.
CC {ECO:0000269|PubMed:12912888}.
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; AY081178; AAL89587.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NJJ1; -.
DR SMR; Q8NJJ1; -.
DR STRING; 5061.CADANGAP00002039; -.
DR PRIDE; Q8NJJ1; -.
DR VEuPathDB; FungiDB:An02g05830; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1144666; -.
DR VEuPathDB; FungiDB:ATCC64974_57930; -.
DR VEuPathDB; FungiDB:M747DRAFT_292171; -.
DR eggNOG; ENOG502QVPN; Eukaryota.
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:0019594; P:mannitol metabolic process; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP: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.
FT CHAIN 1..388
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000371522"
FT ACT_SITE 213
FT /evidence="ECO:0000250"
FT BINDING 5..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 43363 MW; 6CA75A87F52E2AD3 CRC64;
MGKKAIQFGG GNIGRGFVAE FLHKAGYEVV FVDVMDKMVE ALQQNKSYKV TEVSEEGEHT
TTITNYRAIN SKTHESDVIQ EIATADVVTC AVGPHILKFI APVIAKGIDA RTESKPVAVI
ACENAIGATD TLHGFIKQHT SQDRVESLYD RAQFANSAID RIVPQQAPNS GLDVRIEKFY
EWAVEKTPFG SVGHPDIPAI HWVDNLEPYI ERKLFTVNTS HATTAYFGHF RGKKMIADAL
EDEEIRGLVH KVLEETASLI VAKHDISEEE QKEYVKKIVS RISNPYLEDK VERVGRAPLR
KLSRKERFIG PASQLAERGM KYDSLMDAVE MALRFQNVPG DDESAELANI LNEQRAEDAT
IHLTGLDEEH PLYPAVLERV RKVQQGTK
