ID   MTLD_ECO24              Reviewed;         382 AA.
AC   A7ZTE9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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};
GN   OrderedLocusNames=EcE24377A_4099;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(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; CP000800; ABV20147.1; -; Genomic_DNA.
DR   RefSeq; WP_000645424.1; NC_009801.1.
DR   AlphaFoldDB; A7ZTE9; -.
DR   SMR; A7ZTE9; -.
DR   EnsemblBacteria; ABV20147; ABV20147; EcE24377A_4099.
DR   GeneID; 66672505; -.
DR   KEGG; ecw:EcE24377A_4099; -.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   OMA; GKKAVHF; -.
DR   Proteomes; UP000001122; 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   Acetylation; NAD; Oxidoreductase.
FT   CHAIN           1..382
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_1000058531"
FT   BINDING         3..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
FT   MOD_RES         269
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ   SEQUENCE   382 AA;  41139 MW;  0EE8392D33C58CDE CRC64;
     MKALHFGAGN IGRGFIGKLL ADAGIQLTFA DVNQVVLDAL NARHSYQVHV VGETEQVDTV
     SGVNAVSSIG DDVVDLIAQV DLVTTAVGPV VLERIAPAIA KGLVKRKEQG NESPLNIIAC
     ENMVRGTTQL KGHVMNALPE DAKAWVEEHV GFVDSAVDRI VPPSASATND PLEVTVETFS
     EWIVDKTQFK GALPNIPGME LTDNLMAFVE RKLFTLNTGH AITAYLGKLA GHQTIRDAIL
     DEKIRAVVKG AMEESGAVLI KRYGFDADKH AAYIQKILGR FENPYLKDDV ERVGRQPLRK
     LSAGDRLIKP LLGTLEYSLP HKNLIQGIAG AMHFRSEDDP QAQELAALIA DKGPQAALAQ
     ISGLDANSEV VSEAVTAYKA MQ