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 16-JUN-2009, entry version 84. DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase; DE EC=1.1.1.17; GN Name=mtlD; OrderedLocusNames=b3600, JW3574; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX MEDLINE=88288055; PubMed=3135464; RX 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 RT coli."; RL Mol. Microbiol. 2:405-412(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. RC STRAIN=K12; RX MEDLINE=91186837; PubMed=1964486; RX 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 RT coli."; RL Mol. Microbiol. 4:2003-2006(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=94316500; 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 RT region 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 MEDLINE=97426617; 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., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 369-382. RC STRAIN=K12; RX MEDLINE=94131964; PubMed=8300537; 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. RX MEDLINE=85006766; PubMed=6384188; RA Novotny M.J., Reizer J., Esch F., Saier M.H. Jr.; RT "Purification and properties of D-mannitol-1-phosphate dehydrogenase RT and D-glucitol-6-phosphate dehydrogenase from Escherichia coli."; RL J. Bacteriol. 159:986-990(1984). RN [8] RP PROTEIN SEQUENCE OF 1-15. RX MEDLINE=97055418; PubMed=8899705; RX 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 MASS SPECTROMETRY. 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: D-mannitol 1-phosphate + NAD(+) = D-fructose CC 6-phosphate + NADH. CC -!- SUBUNIT: Monomer. CC -!- INTERACTION: CC P0A821:selA; NbExp=1; IntAct=EBI-554652, EBI-1118693; CC P77561:ydeP; NbExp=1; IntAct=EBI-554652, EBI-545210; CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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; AP_004192.1; -. DR RefSeq; NP_418057.1; -. DR DIP; DIP:10268N; -. DR IntAct; P09424; 11. DR GeneID; 948117; -. DR GenomeReviews; AP009048_GR; JW3574. DR GenomeReviews; U00096_GR; b3600. DR KEGG; ecj:JW3574; -. DR KEGG; eco:b3600; -. DR EchoBASE; EB0611; -. DR EcoGene; EG10616; mtlD. DR HOGENOM; P09424; -. DR OMA; P09424; VDRIVPN. DR BioCyc; EcoCyc:MANNPDEHYDROG-MON; -. DR BioCyc; MetaCyc:MANNPDEHYDROG-MON; -. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:HAMAP. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00196; -; 1. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR013118; Mannitol_DH_C. DR InterPro; IPR000669; Mannitol_DH_core. DR InterPro; IPR013131; Mannitol_DH_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR Pfam; PF01232; Mannitol_dh; 1. DR Pfam; PF08125; Mannitol_dh_C; 1. DR PRINTS; PR00084; MTLDHDRGNASE. DR PROSITE; PS00974; MANNITOL_DHGENASE; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Direct protein sequencing; NAD; KW Oxidoreductase. FT CHAIN 1 382 Mannitol-1-phosphate 5-dehydrogenase. FT /FTId=PRO_0000170703. FT NP_BIND 3 14 NAD (By similarity). FT MOD_RES 269 269 N6-acetyllysine. FT CONFLICT 5 5 H -> V (in Ref. 8; AA sequence). FT CONFLICT 14 15 GF -> SL (in Ref. 8; AA sequence). FT CONFLICT 86 86 A -> R (in Ref. 1 and 2). 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 //