ID   MTLD_MYCPU              Reviewed;         360 AA.
AC   Q98PH2;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=MYPU_7500;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(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; AL445565; CAC13923.1; -; Genomic_DNA.
DR   PIR; F90605; F90605.
DR   RefSeq; WP_010925551.1; NC_002771.1.
DR   AlphaFoldDB; Q98PH2; -.
DR   SMR; Q98PH2; -.
DR   STRING; 272635.MYPU_7500; -.
DR   PRIDE; Q98PH2; -.
DR   EnsemblBacteria; CAC13923; CAC13923; CAC13923.
DR   KEGG; mpu:MYPU_7500; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_14; -.
DR   OMA; GKKAVHF; -.
DR   OrthoDB; 1442117at2; -.
DR   BioCyc; MPUL272635:G1GT6-761-MON; -.
DR   Proteomes; UP000000528; 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; 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.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..360
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170713"
FT   BINDING         6..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   360 AA;  42410 MW;  E60949DC40914B1D CRC64;
     MKKYKALHFG AGNIGRGLIS DIYMKNNMDF ALVDIDKDLI EKLNKQKSYS IIDFQTNKVF
     QISNFKAFSI DQEDEIKKWI EQADFISTSI GWSNLASLKK FFENVKLKEK AQIICFENGY
     KISSFFQSIL NIDSNHFVNA SVDKIIPNFK SDSLDVYVES YYEIILEQKN ESQKKLNFVN
     YSTDLEAYIN KKLFLVNAIH STIGYLGYLK KYTYINEALN DQQILFKIKR LAKIINEILS
     KEYLLFKVDY LNDYLEKNLK RFSIKENQDL ISRVARNPIQ KLSKNERYFL IYNLVKKHNL
     EIDILLEIYK SIFYYDNKMD KESSKIQSTI ENKSLAYALK KFSNLDQEDQ EKILKSLAKK