ID   MTLD_STAAR              Reviewed;         368 AA.
AC   Q6GER8;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 24.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17;
GN   Name=mtlD; OrderedLocusNames=SAR2247;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- CATALYTIC ACTIVITY: D-mannitol 1-phosphate + NAD(+) = D-fructose
CC       6-phosphate + NADH.
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; BX571856; CAG41228.1; -; Genomic_DNA.
DR   RefSeq; YP_041605.1; -.
DR   GeneID; 2861316; -.
DR   GenomeReviews; BX571856_GR; SAR2247.
DR   KEGG; sar:SAR2247; -.
DR   HOGENOM; Q6GER8; -.
DR   BioCyc; SAUR282458:SAR2247-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    368       Mannitol-1-phosphate 5-dehydrogenase.
FT                                /FTId=PRO_0000170722.
FT   NP_BIND       3     14       NAD (By similarity).
SQ   SEQUENCE   368 AA;  40826 MW;  32C0CB655983A84B CRC64;
     MKAVHFGAGN IGRGFIGYIL ADNNVKVTFA DVNEEIINAL ATGHQYDVIL ADESKTTTRV
     NNVAAINSMQ PSEELKQAIL EADIITTAVG VNILPIIAKS FAPFLKEKTN HVNIVACENA
     IMATDTLKKA VLDITGPLGN NIHFANSAVD RIVPLQKNEN ILDVMVEPFY EWVVEKDAWY
     GPELNHIKYV DDLTPYIERK LLTVNTGHAY LAYAGKFAGK ATVLDAVKDS SIEAGLRRVL
     AETSQYITNE FDFTEAEQAG YVEKIIDRFN NSYLSDEVTR VGRGTLRKIG PKDRIIKPLA
     YLYNKDLERT GLLNTAALLL KYDDTADQET VEKNNYIKEH GLKAFLSEYA KVDDGLADEI
     IEAYNSLS
//