ID   MTLD_PENRW              Reviewed;         388 AA.
AC   B6HRL5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            Short=M1PDH;
DE            Short=MPD;
DE            Short=MPDH;
DE            EC=1.1.1.17;
GN   ORFNames=Pc22g20800;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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. {ECO:0000250}.
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AM920437; CAP99368.1; -; Genomic_DNA.
DR   RefSeq; XP_002565979.1; XM_002565933.1.
DR   AlphaFoldDB; B6HRL5; -.
DR   SMR; B6HRL5; -.
DR   STRING; 1108849.XP_002565979.1; -.
DR   EnsemblFungi; CAP99368; CAP99368; PCH_Pc22g20800.
DR   GeneID; 8305222; -.
DR   KEGG; pcs:Pc22g20800; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g20800; -.
DR   eggNOG; ENOG502QVPN; Eukaryota.
DR   HOGENOM; CLU_036089_0_1_1; -.
DR   OMA; GKKAVHF; -.
DR   OrthoDB; 1133390at2759; -.
DR   BioCyc; PCHR:PC22G20800-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..388
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000371532"
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;  42445 MW;  DF07664EA8DAFF7B CRC64;
     MEKKAVHFGG GNIGRGFVAE FLHTAGYEVV FVDVMDSIIT ALQNTKSYEV TEVSDEGEAT
     KTITNYRAIN SKTHESDVIN EISTATVVTC AVGPNILKFI APAIAKGIDA RTAATPLAVI
     ACENAIGATD TLHHFIKDNT AQDRLGSMPD RARFANSAID RIVPGQAADS GLNVRIEKFY
     EWAVESTPFG EFGHPDIPAI HWVSDLEPYI ERKLFTVNTG HATAAYYGYN AGKKTIAEAL
     HDSRIRGIVR DVLQETASLI IDKHEISAAE QQEYVETIIT RISNPYLEDT VERVGRAPMR
     KVSRKERFIG PASQLAERGG KFQSLLGSLE MALRFQNVEG DEESVELAKI LKENAPADAA
     VRLTGLDRDH PLFPHVVKVV DGVQSDAK