ID   MTLD_LACLA              Reviewed;         385 AA.
AC   Q9CJH1;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=LL0024;
GN   ORFNames=L33416;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(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; AE005176; AAK04122.1; -; Genomic_DNA.
DR   PIR; H86627; H86627.
DR   RefSeq; NP_266180.1; NC_002662.1.
DR   RefSeq; WP_010905040.1; NC_002662.1.
DR   AlphaFoldDB; Q9CJH1; -.
DR   SMR; Q9CJH1; -.
DR   STRING; 272623.L33416; -.
DR   PaxDb; Q9CJH1; -.
DR   EnsemblBacteria; AAK04122; AAK04122; L33416.
DR   KEGG; lla:L33416; -.
DR   PATRIC; fig|272623.7.peg.28; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_9; -.
DR   OMA; GKKAVHF; -.
DR   Proteomes; UP000002196; 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_0000170708"
FT   BINDING         4..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   385 AA;  43673 MW;  C06C1B98324D6F67 CRC64;
     MKKAVHFGAG NIGRGFIGEI LSKNGFDIHF VDTNKSIIAE LNNRHSYEIG IASSEHEKIS
     VKAVSGINNS ENPEAVIEAI AKADILTTAI GPNVLPYIAE LIAKGLQKRK EEKVQSPLDI
     IACENMIGGS EFLEEKVSDY LSESDKLYLS KFIGFPNAAV DRIVPAQKHK DVLYVEVEPF
     SEWVIDASHL KNKEIKLEGV HYTTDLEPFI ERKLFSVNSG HAAVAYSSAY KGYKTILEGL
     QDEEILNILK AVQKETRALL LAKWAQYFKQ DELIKYHELI ISRFSNPEII DEVSRVARTP
     IRKLGYDERF IRPIRELNDR KLSYQNHLDI VGKIFAYHDE NDAQAIQLQE KLKITELPML
     IEEVTGLSNQ KLILEIEKVI NHYKK