MTLD_SALEP
ID MTLD_SALEP Reviewed; 382 AA.
AC B5R5B9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00196};
DE EC=1.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00196};
GN Name=mtlD {ECO:0000255|HAMAP-Rule:MF_00196}; OrderedLocusNames=SEN3508;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00196};
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00196}.
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DR EMBL; AM933172; CAR35087.1; -; Genomic_DNA.
DR RefSeq; WP_000645377.1; NC_011294.1.
DR AlphaFoldDB; B5R5B9; -.
DR SMR; B5R5B9; -.
DR KEGG; set:SEN3508; -.
DR HOGENOM; CLU_036089_2_0_6; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000000613; 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.
FT CHAIN 1..382
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000099197"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 382 AA; 40895 MW; F18374D7C1B7D829 CRC64;
MKALHFGAGN IGRGFIGKLL ADAGIQLTFA DVNQVVLDAL NARHSYQVHV VGENEQVDTV
SGVNAVSSIG DDVVDLIAHV DLITTAVGPV VLERIAPAIA KGLAKRKAQG VDAPLNIIAC
ENMVRGTTQL KGHVMNALAD GDKAWVEQHV GFVDSAVDRI VPPSASATHD PLEVTVETFS
EWIVDKTQFK GALPNIPGME LTDNLMAFVE RKLFTLNTGH AITAYLGKLA GHQTIRDAIL
DESIRAVVKG AMEESGAVLI KRYGFDADKH AAYIQKILGR FENPYLKDDV ERVGRQPLRK
LSAGDRLIKP LLGTLEYGLP HVNLVKGIAA AMHFRSDEDP QAQELAALIT EKGPQAALAQ
ISGLDANSDV VAEAVNAYNA TK
