MTLD_ENTFA
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 03-AUG-2022, entry version 128.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE EC=1.1.1.17;
GN Name=mtlD; OrderedLocusNames=EF_0413;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1904856; DOI=10.1128/jb.173.12.3709-3715.1991;
RA Fischer R., von Strandmann R.P., Hengstenberg W.;
RT "Mannitol-specific phosphoenolpyruvate-dependent phosphotransferase system
RT of Enterococcus faecalis: molecular cloning and nucleotide sequences of the
RT enzyme IIIMtl gene and the mannitol-1-phosphate dehydrogenase gene,
RT expression in Escherichia coli, and comparison of the gene products with
RT similar enzymes.";
RL J. Bacteriol. 173:3709-3715(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX 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., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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 -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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; NC_004668.1.
DR RefSeq; WP_002355280.1; NZ_KE136524.1.
DR AlphaFoldDB; P27543; -.
DR SMR; P27543; -.
DR STRING; 226185.EF_0413; -.
DR EnsemblBacteria; AAO80272; AAO80272; EF_0413.
DR GeneID; 60892857; -.
DR KEGG; efa:EF0413; -.
DR PATRIC; fig|226185.45.peg.2919; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_9; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000001415; 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_0000170706"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 23..28
FT /note="NGFHIT -> TGFILP (in Ref. 1; AAA24780)"
FT /evidence="ECO:0000305"
FT CONFLICT 34..37
FT /note="ETII -> GNHH (in Ref. 1; AAA24780)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="K -> NG (in Ref. 1; AAA24780)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..146
FT /note="KYLKNPAYA -> IIFEKPSLS (in Ref. 1; AAA24780)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="E -> K (in Ref. 1; AAA24780)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..202
FT /note="HYVAD -> ITCR (in Ref. 1; AAA24780)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..216
FT /note="NT -> TS (in Ref. 1; AAA24780)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="Q -> N (in Ref. 1; AAA24780)"
FT /evidence="ECO:0000305"
FT CONFLICT 320..323
FT /note="PHLL -> AAFI (in Ref. 1; AAA24780)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..384
FT /note="IAEVTGIEDPETVKNIKQNVERYARPQVA -> DR (in Ref. 1;
FT AAA24780)"
FT /evidence="ECO:0000305"
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
