ID   MTLD_CHAGB              Reviewed;         398 AA.
AC   Q2H2D7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=CHGG_04059;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408032; EAQ87440.1; -; Genomic_DNA.
DR   RefSeq; XP_001223273.1; XM_001223272.1.
DR   AlphaFoldDB; Q2H2D7; -.
DR   SMR; Q2H2D7; -.
DR   STRING; 38033.XP_001223273.1; -.
DR   EnsemblFungi; EAQ87440; EAQ87440; CHGG_04059.
DR   GeneID; 4392871; -.
DR   eggNOG; ENOG502QVPN; Eukaryota.
DR   HOGENOM; CLU_036089_0_1_1; -.
DR   InParanoid; Q2H2D7; -.
DR   OMA; GKKAVHF; -.
DR   OrthoDB; 1133390at2759; -.
DR   Proteomes; UP000001056; 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..398
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000371525"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000250"
FT   BINDING         10..21
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  44047 MW;  6C1802D7C566865A CRC64;
     MVQRNAPKKA VHFGAGNIGR GFVACFLHNS GYEVIFAEVN DTTVQKLNSQ KSYKVIEVGA
     DGTSESTITN YRAINSRLNE AELVQEIATA DLVTCSVGPH ILKFLAPVIA KGIDARSTDL
     TPVAVIACEN AIGATDTLAE FIKAPENTNP DRLADYDKRA RFANSAIDRI VPAQDPDAGL
     DVRLEKFYEW VVERTPFADH EPPAVEGIHW VDNLQPFIER KLYTVNTGHA TAAYHGYIRR
     KSTVYDALQD REIQEEVKKA LANTASLITQ KHGIPQDEQQ AYVDKIVRRI SNPHLEDAVE
     RVGRAPLRKL SRKERFIGPA AELAEHGKDC GALLDAAEMA FRFQNVEGDD ESFKLAEIME
     QNGPEDVVKQ VCGLEPKEKL FPAVVDVVKR VQADTQSD