ID   MTLD_PARBR              Reviewed;         388 AA.
AC   Q874B3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            Short=M1PDH;
DE            Short=MPD;
DE            Short=MPDH;
DE            EC=1.1.1.17;
OS   Paracoccidioides brasiliensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=121759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Castro N.S., Parente J.A., Jesuino R.S.A., Pereira M., Felipe M.S.S.,
RA   Soares C.M.A.;
RT   "The mannitol-1-phosphate dehydrogenase of Paracoccidioides brasiliensis.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AY204753; AAO47089.1; -; mRNA.
DR   AlphaFoldDB; Q874B3; -.
DR   SMR; Q874B3; -.
DR   VEuPathDB; FungiDB:PABG_02864; -.
DR   VEuPathDB; FungiDB:PADG_01372; -.
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   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..388
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000371531"
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;  43032 MW;  B783BA0D44AF4FBC CRC64;
     MGKKAVHFGG GNIGRGFVGE FLHESGYEVV FVDVMDSVID ALQKASSYTV TEISGEGEHK
     KVIENYRAIN SKHNLDDVIK EISTADVVTC AVGPNILKFI APPIAKGIDI RTQPKPLAVI
     ACENAIGATD TLHGFIKDNT DESRRDSLPS RAQFANSAID RIVPTQDPNS GLDVKIEKFY
     EWVVEKTPFG DVGHPDIKAI HWVDNLEPYI ERKLFTVNTG HATAAYFGYN AGKPTIHDAL
     KDERIRSQVN AVLAETSALI VEKHHIPAEE QHDYVQKIIT RISNPYLEDV VQRVGRAPLR
     KLSRKERFIG PAAQLAERGQ QVDALMGAVE EALKFQNVPD DEESFELHKI LKELSAADAT
     TKLTDLEPDH PLYPRVLEKV TKVQSETK