MTLD_CLOAB
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 03-AUG-2022, entry version 118.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE EC=1.1.1.17;
GN Name=mtlD; OrderedLocusNames=CA_C0157;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11160802; DOI=10.1099/00221287-147-1-75;
RA Behrens S., Mitchell W.J., Bahl H.;
RT "Molecular analysis of the mannitol operon of Clostridium acetobutylicum
RT encoding a phosphotransferase system and a putative PTS-modulated
RT 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 PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA 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:
CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61381; EC=1.1.1.17;
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000305}.
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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; NC_003030.1.
DR RefSeq; WP_010963483.1; NC_003030.1.
DR AlphaFoldDB; O65992; -.
DR SMR; O65992; -.
DR STRING; 272562.CA_C0157; -.
DR EnsemblBacteria; AAK78141; AAK78141; CA_C0157.
DR GeneID; 44996649; -.
DR KEGG; cac:CA_C0157; -.
DR PATRIC; fig|272562.8.peg.341; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_9; -.
DR OMA; GMNLADN; -.
DR OrthoDB; 1442117at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR023028; Mannitol_1_phos_5_DH.
DR InterPro; IPR000669; Mannitol_DH.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR023027; Mannitol_DH_CS.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..384
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_0000170702"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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