MTLD_YERPS
ID MTLD_YERPS Reviewed; 387 AA.
AC Q663V5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=YPTB3919;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH23157.1; -; Genomic_DNA.
DR RefSeq; WP_011193338.1; NZ_CP009712.1.
DR AlphaFoldDB; Q663V5; -.
DR SMR; Q663V5; -.
DR EnsemblBacteria; CAH23157; CAH23157; YPTB3919.
DR GeneID; 66843662; -.
DR KEGG; ypo:BZ17_2662; -.
DR KEGG; yps:YPTB3919; -.
DR PATRIC; fig|273123.14.peg.2790; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000001011; 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..387
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000011824"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 387 AA; 41992 MW; C110364E31E909F3 CRC64;
MKALHFGAGN IGRGFIGKLL ADAGAQLTFA DVNQPLLDAL NKRKSYQVNV VGEQARVEEV
KNVSAVNSGS PEVVALIAEA DIVTTAVGPQ ILARIAATVA QGLITRHQQG NTRPLNIIAC
ENMVRGTSQL KQHVFAALSE DEQRWVEQHV GFVDSAVDRI VPPSEAGSTD ILAVTVETFS
EWIVDGTQFK GQPPEIVGME LTDNLMAFVE RKLFTLNTGH AITAYLGQLA GHQTIRDAIL
DPAVRQTVKG AMEESGAVLI KRYAFDPQKH AAYINKILSR FENPYLHDDV ERVGRQPLRK
LSAGDRLIKP LLGTLEYQLP HDSLVTGIAA AMSYRSEQDP QAQELVTLLA QLGPKAALAQ
ISDLPADSEV VEQAVSVYNA MQQKLAH