ID   MTLD_YERPS              Reviewed;         387 AA.
AC   Q663V5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-NOV-2008, entry version 28.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17;
GN   Name=mtlD; OrderedLocusNames=YPTB3919;
OS   Yersinia pseudotuberculosis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Yersinia.
OX   NCBI_TaxID=633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953 / Serotype I;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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; BX936398; CAH23157.1; -; Genomic_DNA.
DR   RefSeq; YP_072395.1; -.
DR   GeneID; 2956090; -.
DR   GenomeReviews; BX936398_GR; YPTB3919.
DR   KEGG; yps:YPTB3919; -.
DR   NMPDR; fig|273123.1.peg.3977; -.
DR   HOGENOM; Q663V5; -.
DR   BioCyc; YPSE273123:YPTB3919-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    387       Mannitol-1-phosphate 5-dehydrogenase.
FT                                /FTId=PRO_1000011824.
FT   NP_BIND       3     14       NAD (By similarity).
SQ   SEQUENCE   387 AA;  41992 MW;  C110364E31E909F3 CRC64;
     MKALHFGAGN IGRGFIGKLL ADAGAQLTFA DVNQPLLDAL NKRKSYQVNV VGEQARVEEV
     KNVSAVNSGS PEVVALIAEA DIVTTAVGPQ ILARIAATVA QGLITRHQQG NTRPLNIIAC
     ENMVRGTSQL KQHVFAALSE DEQRWVEQHV GFVDSAVDRI VPPSEAGSTD ILAVTVETFS
     EWIVDGTQFK GQPPEIVGME LTDNLMAFVE RKLFTLNTGH AITAYLGQLA GHQTIRDAIL
     DPAVRQTVKG AMEESGAVLI KRYAFDPQKH AAYINKILSR FENPYLHDDV ERVGRQPLRK
     LSAGDRLIKP LLGTLEYQLP HDSLVTGIAA AMSYRSEQDP QAQELVTLLA QLGPKAALAQ
     ISDLPADSEV VEQAVSVYNA MQQKLAH
//