ID   MTLD_ENTFA              Reviewed;         384 AA.
AC   P27543;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   25-NOV-2008, entry version 59.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17;
GN   Name=mtlD; OrderedLocusNames=EF_0413;
OS   Enterococcus faecalis (Streptococcus faecalis).
OC   Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus.
OX   NCBI_TaxID=1351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91267934; PubMed=1904856;
RA   Fischer R., von Strandmann R.P., Hengstenberg W.;
RT   "Mannitol-specific phosphoenolpyruvate-dependent phosphotransferase
RT   system of Enterococcus faecalis: molecular cloning and nucleotide
RT   sequences of the enzyme IIIMtl gene and the mannitol-1-phosphate
RT   dehydrogenase gene, expression in Escherichia coli, and comparison of
RT   the gene products with similar enzymes.";
RL   J. Bacteriol. 173:3709-3715(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V583 / ATCC 700802;
RX   MEDLINE=22550857; PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
RA   Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
RA   Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
RA   Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant
RT   Enterococcus faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- CATALYTIC ACTIVITY: D-mannitol 1-phosphate + NAD(+) = D-fructose
CC       6-phosphate + NADH.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M38386; AAA24780.1; -; Genomic_DNA.
DR   EMBL; AE016830; AAO80272.1; -; Genomic_DNA.
DR   PIR; C39435; C39435.
DR   RefSeq; NP_814201.1; -.
DR   GeneID; 1199330; -.
DR   GenomeReviews; AE016830_GR; EF_0413.
DR   KEGG; efa:EF0413; -.
DR   NMPDR; fig|226185.1.peg.387; -.
DR   TIGR; EF_0413; -.
DR   HOGENOM; P27543; -.
DR   BioCyc; EFAE226185:EF_0413-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    384       Mannitol-1-phosphate 5-dehydrogenase.
FT                                /FTId=PRO_0000170706.
FT   NP_BIND       3     14       NAD (By similarity).
FT   CONFLICT     23     28       NGFHIT -> TGFILP (in Ref. 1; AAA24780).
FT   CONFLICT     34     37       ETII -> GNHH (in Ref. 1; AAA24780).
FT   CONFLICT    115    115       K -> NG (in Ref. 1; AAA24780).
FT   CONFLICT    138    146       KYLKNPAYA -> IIFEKPSLS (in Ref. 1;
FT                                AAA24780).
FT   CONFLICT    167    167       E -> K (in Ref. 1; AAA24780).
FT   CONFLICT    198    202       HYVAD -> ITCR (in Ref. 1; AAA24780).
FT   CONFLICT    215    216       NT -> TS (in Ref. 1; AAA24780).
FT   CONFLICT    277    277       Q -> N (in Ref. 1; AAA24780).
FT   CONFLICT    320    323       PHLL -> AAFI (in Ref. 1; AAA24780).
FT   CONFLICT    356    384       IAEVTGIEDPETVKNIKQNVERYARPQVA -> DR (in
FT                                Ref. 1; AAA24780).
SQ   SEQUENCE   384 AA;  43099 MW;  CE51664A668BC7CD CRC64;
     MNAVHFGAGN IGRGFIGEIL AKNGFHITFV DVNETIIQAL KERKSYTIEL ADASHQQINV
     ENVTGLNNMT EPEKVVEAIA EADLVTTAIG PNILPRIAEL IAQGIDARAE ANCQKPLDII
     ACENMIGGST FLAEEVAKYL KNPAYAEQWI GFPDAAVDRI VPLQKHEDPL FVQVEPFCEW
     VIDDTNRKAK EIQLEGVHYV ADLEPYIERK LFSVNTGHAT VAYTGALLGY QTIDEAMQDA
     LVVAQLKSVL QETGKLLVAK WNFDEQEHAA YIEKIIQRFQ NKYISDAITR VARTPIRKLG
     AQERFIRPIR ELQERNLVSP HLLAMIGIVF NYHDPEDEQS RQLQEMLDQE SVDTVIAEVT
     GIEDPETVKN IKQNVERYAR PQVA
//