ID   MTLD_AJECN              Reviewed;         388 AA.
AC   A6RGF3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 68.
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=HCAG_08720;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN05065.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CH476666; EDN05065.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001536398.1; XM_001536348.1.
DR   AlphaFoldDB; A6RGF3; -.
DR   SMR; A6RGF3; -.
DR   STRING; 339724.A6RGF3; -.
DR   EnsemblFungi; EDN05065; EDN05065; HCAG_08720.
DR   GeneID; 5442776; -.
DR   KEGG; aje:HCAG_08720; -.
DR   HOGENOM; CLU_036089_0_1_1; -.
DR   OrthoDB; 1133390at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
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_0000371516"
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;  43148 MW;  4EB793D2DFFEDF7C CRC64;
     MGKKAVHFGG GNIGRGFVGE FLHESGYEVV FVDVMDNVID ALNKHSSYTV TEISEEGEQQ
     KVITNYRAIN SKHNLDDVIK EISTADVVTC AVGPNILKFI APPIAKGIDT RTLSKPLAVI
     ACENAIGATD TLHGFIKENT DEARLPSLYS RAQFANSAID RIVPTQDLGS GLNVKIEKFY
     EWVVEKTPFG DVGHPDIKDI HWVDNLEPYI ERKLFTVNTG HATAAYYGYS AGKKTIHDAL
     RDDRIRKEVN AALAETSRLI VEKHGISPEE QARYVSSIIT RISNPHLEDI VQRVGRAPLR
     KLSRKERFIG PASQLAERGH TVTALMDAVE QALKFQNVPD DEESFELFKI LKENSAADAT
     TKLTGLEKEH PLYSRVLEKV DKVQKETK