ID   MTLD_YERP3              Reviewed;         387 AA.
AC   A7FP92;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00196};
DE            EC=1.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00196};
GN   Name=mtlD {ECO:0000255|HAMAP-Rule:MF_00196};
GN   OrderedLocusNames=YpsIP31758_4127;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT   causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00196};
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00196}.
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DR   EMBL; CP000720; ABS46756.1; -; Genomic_DNA.
DR   RefSeq; WP_012105967.1; NC_009708.1.
DR   AlphaFoldDB; A7FP92; -.
DR   SMR; A7FP92; -.
DR   EnsemblBacteria; ABS46756; ABS46756; YpsIP31758_4127.
DR   KEGG; ypi:YpsIP31758_4127; -.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OMA; GKKAVHF; -.
DR   Proteomes; UP000002412; Chromosome.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-UniRule.
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; IPR023027; Mannitol_DH_CS.
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.
DR   PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..387
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_1000058534"
FT   BINDING         3..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   387 AA;  41891 MW;  C220054A61E909F8 CRC64;
     MKALHFGAGN IGRGFIGKLL ADAGAQLTFA DVNQPLLDAL NKRKSYQVNV VGEQARVEEV
     KNVSAVNSGS PEVVALIAEA DIVTTAVGPQ ILARIAATVA QGLITRHQQG NTRPLNIIAC
     ENMVRGTSQL KQHVFAALSE DEQIWVEQHV GFVDSAVDRI VPPSEAGSTD ILAVTVETFS
     EWIVDGTQFK GQPPEIVGME LTDNLMAFVE RKLFTLNTGH AITAYLGQLA GHQTIRDAIL
     DPAVRQTVKG AMEESGAVLI KRYAFDPQKH AAYINKILSR FENPYLHDDV ERVGRQPLRK
     LSAGDRLIKP LLGTLEYQLP HDSLVTGIAA AMSYRSEQDP QAQELVTLLA QLGPKAALAQ
     ISGLPADSEV VEQAVSVYNA MQQKLAH