ID   MTLD_STRMU              Reviewed;         382 AA.
AC   Q02418;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17;
GN   Name=mtlD; OrderedLocusNames=SMU_1182;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700611 / UA130 / Serotype c;
RX   PubMed=1322373; DOI=10.1128/iai.60.8.3369-3375.1992;
RA   Honeyman A.L., Curtiss R. III;
RT   "Isolation, characterization, and nucleotide sequence of the Streptococcus
RT   mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific
RT   factor III gene of the phosphoenolpyruvate phosphotransferase system.";
RL   Infect. Immun. 60:3369-3375(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF210133; AAA26942.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN58872.1; -; Genomic_DNA.
DR   PIR; C44798; C44798.
DR   RefSeq; NP_721566.1; NC_004350.2.
DR   RefSeq; WP_002262168.1; NC_004350.2.
DR   AlphaFoldDB; Q02418; -.
DR   SMR; Q02418; -.
DR   STRING; 210007.SMU_1182; -.
DR   PRIDE; Q02418; -.
DR   EnsemblBacteria; AAN58872; AAN58872; SMU_1182.
DR   GeneID; 66817428; -.
DR   KEGG; smu:SMU_1182; -.
DR   PATRIC; fig|210007.7.peg.1060; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_9; -.
DR   OMA; GKKAVHF; -.
DR   PhylomeDB; Q02418; -.
DR   BioCyc; MetaCyc:MON-13098; -.
DR   Proteomes; UP000002512; 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..382
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170725"
FT   BINDING         4..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        170
FT                   /note="E -> K (in Ref. 1; AAA26942)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   382 AA;  42972 MW;  B2C1F81856A1CA9D CRC64;
     MKKAVHFGAG NIGRGFIGQI LFENGFAIDF VDVNDKIINA LNERHSYDIE IAEDGKRHIT
     VSNVAGINNK ENPQAVIDAV AETELITTAI GPNILPFIAQ LIAKGIEKRR ESQNQTPLDI
     IACENMIGGS AFLWQEVQKY LSADGLAFAK DYIGFPNAAV DRIVPAQVHE DPLFVVVEPF
     SEWVVETAAM KNPDLKLSSV HYEENLEPFI ERKLFSVNSG HATTAYTGAY FGAKTVLEAL
     KDQQVKEQVK AVLGEIRQLL MAKWQFKEND LKVYHDIIIS RFENPYIVDD VTRVARTPIR
     KLGYDERFIR PIRELKDRGL SYEYLLQTVA YVFHYKDSND EQSVQLKLLL QEKSLKAVVK
     EVTGLTDAAL IEEIVTSVES LD