ID   MTLD_ECOLI              Reviewed;         382 AA.
AC   P09424; Q2M7R3;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 3.
DT   04-NOV-2026, entry version 188.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            EC=1.1.1.17 {ECO:0000269|PubMed:6384188};
GN   Name=mtlD; OrderedLocusNames=b3600, JW3574;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3135464; DOI=10.1111/j.1365-2958.1988.tb00045.x;
RA   Davis T., Yamada M., Elgort M., Saier M.H. Jr.;
RT   "Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli.";
RL   Mol. Microbiol. 2:405-412(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC   STRAIN=K12;
RX   PubMed=1964486; DOI=10.1111/j.1365-2958.1990.tb02050.x;
RA   Jaiang W., Wu L.F., Tomich J., Saier M.H. Jr., Nichaus W.G.;
RT   "Corrected sequence of the mannitol (mtl) operon in Escherichia coli.";
RL   Mol. Microbiol. 4:2003-2006(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 369-382.
RC   STRAIN=K12;
RX   PubMed=8300537; DOI=10.1128/jb.176.3.840-847.1994;
RA   Figge R.M., Ramseier T.M., Saier M.H. Jr.;
RT   "The mannitol repressor (MtlR) of Escherichia coli.";
RL   J. Bacteriol. 176:840-847(1994).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-25, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=6384188; DOI=10.1128/jb.159.3.986-990.1984;
RA   Novotny M.J., Reizer J., Esch F., Saier M.H. Jr.;
RT   "Purification and properties of D-mannitol-1-phosphate dehydrogenase and D-
RT   glucitol-6-phosphate dehydrogenase from Escherichia coli.";
RL   J. Bacteriol. 159:986-990(1984).
RN   [8]
RP   PROTEIN SEQUENCE OF 1-15.
RX   PubMed=8899705; DOI=10.1111/j.1365-2958.1996.tb02652.x;
RA   Gonzalez-Gil G., Bringmann P., Kahmann R.;
RT   "FIS is a regulator of metabolism in Escherichia coli.";
RL   Mol. Microbiol. 22:21-29(1996).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-269, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC         + NADH + H(+); 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         Evidence={ECO:0000269|PubMed:6384188};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19662;
CC         Evidence={ECO:0000305|PubMed:6384188};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:6384188}.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X51359; CAA35744.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18577.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76624.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77693.1; -; Genomic_DNA.
DR   EMBL; X06794; CAA29954.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U03845; AAA92661.1; -; Genomic_DNA.
DR   PIR; B65160; B65160.
DR   RefSeq; NP_418057.1; NC_000913.3.
DR   RefSeq; WP_000645439.1; NZ_CP009789.1.
DR   AlphaFoldDB; P09424; -.
DR   SMR; P09424; -.
DR   BioGRID; 4261273; 15.
DR   DIP; DIP-10268N; -.
DR   FunCoup; P09424; 161.
DR   IntAct; P09424; 11.
DR   STRING; 511145.b3600; -.
DR   iPTMnet; P09424; -.
DR   jPOST; P09424; -.
DR   PaxDb; 511145-b3600; -.
DR   EnsemblBacteria; AAC76624; AAC76624; b3600.
DR   GeneID; 948117; -.
DR   KEGG; ecj:JW3574; -.
DR   KEGG; eco:b3600; -.
DR   KEGG; ecoc:C3026_19520; -.
DR   PATRIC; fig|1411691.4.peg.3107; -.
DR   EchoBASE; EB0611; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_036089_2_0_6; -.
DR   InParanoid; P09424; -.
DR   OMA; AAALCYK; -.
DR   OrthoDB; 271711at2; -.
DR   PhylomeDB; P09424; -.
DR   BioCyc; EcoCyc:MANNPDEHYDROG-MONOMER; -.
DR   BioCyc; MetaCyc:MANNPDEHYDROG-MONOMER; -.
DR   BRENDA; 1.1.1.17; 2026.
DR   PRO; PR:P09424; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P09424; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0019592; P:mannitol catabolic process; IMP:EcoCyc.
DR   FunFam; 1.10.1040.10:FF:000009; Mannitol-1-phosphate 5-dehydrogenase; 1.
DR   FunFam; 3.40.50.720:FF:000075; Mannitol-1-phosphate 5-dehydrogenase; 1.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; NF002648; mtlD; 1.
DR   NCBIfam; NF002646; PRK02318.1-2; 1.
DR   NCBIfam; NF002647; PRK02318.1-3; 1.
DR   NCBIfam; NF002650; PRK02318.2-2; 1.
DR   NCBIfam; NF002652; PRK02318.2-5; 1.
DR   PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00084; MTLDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..382
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000170703"
FT   BINDING         3..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         269
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   CONFLICT        5
FT                   /note="H -> V (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14..15
FT                   /note="GF -> SL (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="A -> R (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   382 AA;  41139 MW;  1AC44028C150A7B2 CRC64;
     MKALHFGAGN IGRGFIGKLL ADAGIQLTFA DVNQVVLDAL NARHSYQVHV VGETEQVDTV
     SGVNAVSSIG DDVVDLIAQV DLVTTAVGPV VLERIAPAIA KGQVKRKEQG NESPLNIIAC
     ENMVRGTTQL KGHVMNALPE DAKAWVEEHV GFVDSAVDRI VPPSASATND PLEVTVETFS
     EWIVDKTQFK GALPNIPGME LTDNLMAFVE RKLFTLNTGH AITAYLGKLA GHQTIRDAIL
     DEKIRAVVKG AMEESGAVLI KRYGFDADKH AAYIQKILGR FENPYLKDDV ERVGRQPLRK
     LSAGDRLIKP LLGTLEYGLP HKNLIEGIAA AMHFRSEDDP QAQELAALIA DKGPQAALAQ
     ISGLDANSEV VSEAVTAYKA MQ
//