ID   MTLD_BACLD              Reviewed;         379 AA.
AC   Q65NA1; Q62YQ5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-NOV-2008, entry version 45.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17;
GN   Name=mtlD; OrderedLocusNames=BLi00507, BL02815;
OS   Bacillus licheniformis (strain DSM 13 / ATCC 14580).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H.,
RA   Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R.,
RA   Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an
RT   organism with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G.,
RA   Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L.,
RA   Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N.,
RA   Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).
CC   -!- CATALYTIC ACTIVITY: D-mannitol 1-phosphate + NAD(+) = D-fructose
CC       6-phosphate + NADH.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
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DR   EMBL; CP000002; AAU22103.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU39463.1; -; Genomic_DNA.
DR   RefSeq; YP_077741.1; -.
DR   RefSeq; YP_090156.1; -.
DR   GeneID; 3030175; -.
DR   GeneID; 3098227; -.
DR   GenomeReviews; CP000002_GR; BL02815.
DR   GenomeReviews; AE017333_GR; BLi00507.
DR   KEGG; bld:BLi00507; -.
DR   KEGG; bli:BL02815; -.
DR   NMPDR; fig|279010.5.peg.593; -.
DR   HOGENOM; Q65NA1; -.
DR   BioCyc; BLIC279010:BL02815-MON; -.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00196; -; 1.
DR   InterPro; IPR013328; DHase_multihelical.
DR   InterPro; IPR013118; Mannitol_DHase_C.
DR   InterPro; IPR000669; Mannitol_DHase_core.
DR   InterPro; IPR013131; Mannitol_DHase_N.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00084; MTLDHDRGNASE.
DR   PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    379       Mannitol-1-phosphate 5-dehydrogenase.
FT                                /FTId=PRO_1000011795.
FT   NP_BIND       3     14       NAD (By similarity).
SQ   SEQUENCE   379 AA;  41676 MW;  9B356236E0A70F1E CRC64;
     MIALHFGAGN IGRGFIGALL CKSGYDVVFA DVNDAVINEL NDKGRYTVEM ADAGRKQETI
     GPVRAINSAT QLDELYDLIA KADLVTTAVG PAVLKLIAEP IAEGLKRRMK INKQPLNIIA
     CENMIGGSAH LREEIFARLT ETERAAISDS VGFPNSAVDR IVPIQHHDDP LKVTVEPFFE
     WAVDQTEFAG KVPDIEGVTY VADLAPFIER KLFTVNTGHA MAAYAGYKKG LKTIKDAIHH
     PEVRQTVAGA LEETGRYLVQ TYDFTQEEHR AYMTKIIGRF ENECLSDDVT RVARSPLRKL
     GRDDRLVGPA RKLCDLGFEP VRLAEGIALA LQFDCADDPE AVQLQSMIAE KGYAGVLRDV
     CGLEEDHSLF KLVISHLKA
//