ID   MTLD_MYCMS              Reviewed;         328 AA.
AC   P55800;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   04-NOV-2026, entry version 124.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17;
GN   Name=mtlD; OrderedLocusNames=MSC_0017;
OS   Mycoplasma mycoides subsp. mycoides SC (strain CCUG 32753 / NCTC 10114 /
OS   PG1).
OC   Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Mycoplasmataceae;
OC   Mycoplasma.
OX   NCBI_TaxID=272632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 32753 / NCTC 10114 / PG1;
RX   PubMed=14762060; DOI=10.1101/gr.1673304;
RA   Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA   Johansson K.-E., Pettersson B., Uhlen M.;
RT   "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT   PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL   Genome Res. 14:221-227(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-328.
RC   STRAIN=L2;
RX   PubMed=9004514; DOI=10.1099/13500872-142-12-3515;
RA   Cheng X., Nicolet J., Miserez R., Kuhnert P., Krampe M., Pilloud T.,
RA   Abdo E.-M., Griot C., Frey J.;
RT   "Characterization of the gene for an immunodominant 72 kDa lipoprotein of
RT   Mycoplasma mycoides subsp. mycoides small colony type.";
RL   Microbiology 142:3515-3524(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC         + NADH + H(+); 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   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BX293980; CAE76670.1; -; Genomic_DNA.
DR   EMBL; U61140; AAC44573.1; -; Genomic_DNA.
DR   RefSeq; WP_011166228.1; NC_005364.2.
DR   AlphaFoldDB; P55800; -.
DR   SMR; P55800; -.
DR   STRING; 272632.MSC_0017; -.
DR   KEGG; mmy:MSC_0017; -.
DR   PATRIC; fig|272632.4.peg.17; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_14; -.
DR   OMA; AAALCYK; -.
DR   Proteomes; UP000001016; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019592; P:mannitol catabolic process; IEA:TreeGrafter.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
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   PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..328
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170711"
FT   BINDING         3..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        176
FT                   /note="S -> R (in Ref. 2; AAC44573)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="F -> L (in Ref. 2; AAC44573)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   328 AA;  38565 MW;  9995F74B7577876C CRC64;
     MNLIHFGAGN IGCGFIAPIL SSIVDHIYFV DNNIDIVNKI NTQKLIKIHT SDSKKISITN
     ISAWLLTDFI NYKKTWNEVS LLTISIGIKN LKHIIYYVNQ LIDYKIKNNQ KLIIMCCENG
     IRVSSLFKSY FSNLNNNIYF VDVLVDRIVS NKNILNDYLE CEDYYLWIVD KTQLPSDFKQ
     VPNLTYTTSF DIQITKKIYM LNALHCSLAW FVFKNFSFNK YLYVYQALKN DKVVEFVNNY
     LNEVILVLNH KYNINLDELN NYKNQIIKRL NSNFIKDDLK RLARNTELKL SKNERILTIL
     DYAKDNNLKH DILLLSYQNG LEYLKNNK
//