ID   MTLD_CLOAB              Reviewed;         384 AA.
AC   O65992;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17;
GN   Name=mtlD; OrderedLocusNames=CA_C0157;
OS   Clostridium acetobutylicum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   MEDLINE=21097245; PubMed=11160802;
RA   Behrens S., Mitchell W.J., Bahl H.;
RT   "Molecular analysis of the mannitol operon of Clostridium
RT   acetobutylicum encoding a phosphotransferase system and a putative
RT   PTS-modulated regulator.";
RL   Microbiology 147:75-86(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   MEDLINE=21359325; PubMed=11466286;
RX   DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q.,
RA   Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I.,
RA   Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P.,
RA   Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; U53868; AAC12851.1; -; Genomic_DNA.
DR   EMBL; AE001437; AAK78141.1; -; Genomic_DNA.
DR   PIR; B96919; B96919.
DR   RefSeq; NP_346801.1; -.
DR   GeneID; 1116340; -.
DR   GenomeReviews; AE001437_GR; CA_C0157.
DR   KEGG; cac:CAC0157; -.
DR   NMPDR; fig|272562.1.peg.330; -.
DR   HOGENOM; O65992; -.
DR   OMA; O65992; VDRIVPN.
DR   BioCyc; CACE272562:CAC0157-MON; -.
DR   BRENDA; 1.1.1.17; 2866.
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; DH_multihelical.
DR   InterPro; IPR013118; Mannitol_DH_C.
DR   InterPro; IPR000669; Mannitol_DH_core.
DR   InterPro; IPR013131; Mannitol_DH_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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_0000170702.
FT   NP_BIND       3     14       NAD (By similarity).
SQ   SEQUENCE   384 AA;  43922 MW;  0F73B98AFD9B8F6C CRC64;
     MKALHFGAGN IGRGFIGYLL YKSNYETTFV DIFDKVVDDI NKYKRYTVIT LSTSKNKEKV
     ENVRAVNLKD SVALEKEVLE ADLITTSLGL NNLKSTGELL RGFLKKRSEI NDKPLDIIAC
     ENALFASDVL KKAILDGADE ELKKYLEKSV GFPNCTVDRI VPNVDIEKEL PIDVAVEDFY
     EWDIEKNKVK INNKIIGAEY VEKLDPYLER KLFLLNGAHA TIAYLGYLKG YKYIHEAIKD
     KEINKIIVGF HSEAVQALSE KHKIDIQILK EYSNKLLKRF ENEYLKDDVS RVGRDPMRKL
     SSNDRLITPL KLCCDLKIDF TNILFGVASG YLFNYKEDEK AQGIQNIITK EGIKKAISNV
     SQIKEGDYLN NMIAYKYEEL KKQN
//