ID   MTLD_YERPA              Reviewed;         387 AA.
AC   Q1C3J5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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}; OrderedLocusNames=YPA_3015;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG14977.1; -; Genomic_DNA.
DR   RefSeq; WP_002209620.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1C3J5; -.
DR   SMR; Q1C3J5; -.
DR   EnsemblBacteria; ABG14977; ABG14977; YPA_3015.
DR   GeneID; 57974648; -.
DR   KEGG; ypa:YPA_3015; -.
DR   OMA; GKKAVHF; -.
DR   Proteomes; UP000001971; 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_1000011821"
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;  42018 MW;  595EB0BC2FD4BDA9 CRC64;
     MKALHFGAGN IGRGFIGKLL ADAGAQLTFA DVNQPLLDEL NKRKRYQVNV 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