MTLD_YERPY
ID MTLD_YERPY Reviewed; 387 AA.
AC B1JH11;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=YPK_0027;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA66341.1; -; Genomic_DNA.
DR RefSeq; WP_012303323.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JH11; -.
DR SMR; B1JH11; -.
DR EnsemblBacteria; ACA66341; ACA66341; YPK_0027.
DR KEGG; ypy:YPK_0027; -.
DR PATRIC; fig|502800.11.peg.628; -.
DR OMA; GKKAVHF; -.
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_1000099211"
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; 41960 MW; 2DC451E490470238 CRC64;
MKALHFGAGN IGRGFIGKLL ADAGAQLTFA DVNQPLLDAL NKRKRYQVNV VGEQARVEEV
KNVSAVNSGS PEVVALIAEA DIVTTAVGPQ ILARIAATVA QGLITRHQQG NTRPLNIIAC
ENMVRGTSQL KQHVFAALSE DEQIWVEQHV GFVDSAVDRI VPPSEAGSTD ILAVTVETFS
EWIVDGTQFK GQPPEIVGME LTDNLMAFVE RKLFTLNTGH AITAYLGQLA GHQTIRDAIL
DPAVRQTVKG AMEESGAVLI KRYAFDPQKH AAYINKILSR FENPYLHDDV ERVGRQPLRK
LSAGDRLIKP LLGTLEYQLP HDSLVTGIAA AMSYRSEQDP QAQELVTLLA QLGPKAALAQ
ISGLPADSEV VEQAVSVYNA MQQKLAH