ID   MTLD_PASMU              Reviewed;         385 AA.
AC   Q9CLY7;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=PM1062;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03146.1; -; Genomic_DNA.
DR   RefSeq; WP_010906996.1; NC_002663.1.
DR   AlphaFoldDB; Q9CLY7; -.
DR   SMR; Q9CLY7; -.
DR   STRING; 747.DR93_903; -.
DR   EnsemblBacteria; AAK03146; AAK03146; PM1062.
DR   KEGG; pmu:PM1062; -.
DR   PATRIC; fig|272843.6.peg.1076; -.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OMA; GKKAVHF; -.
DR   Proteomes; UP000000809; 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; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170715"
FT   BINDING         3..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   385 AA;  42595 MW;  ABEB7345ABB52DE2 CRC64;
     MKALHFGAGN IGRGFIGKLL ADSGIQVIFA DVNDHVIEQL KTQRAYPVKI VGDRLNVIET
     VSNVTGVNSK NEADIIACFT EVDLVTTAVG PNVLKIISST IAKGLSARFR AGNTRPLNII
     ACENMVRGTS FLKDNVFSYL TPEEQQQAEA QIGFVDSAVD RIVPPVQFDP ANPLLVTVEE
     FSEWIVDKTQ FKGTIPAITG MEQTDNLMAF VERKLFTLNT GHATTAYLGK LKGHQFVKDS
     IDDPDIREAV KATMQESGAV LIKRYGFDPH AHAAYIEKIL KRFANPYLQD DVDRVGREPL
     RKLSYNDRLI KPLRGTLEYG LPNQHLIQTI ASALAYRNES DPQAVELAQL LQQDTLESAV
     KKITELTESN IVQQIVTAYN ALQKN