MTLD_ECOL6
ID MTLD_ECOL6 Reviewed; 382 AA.
AC Q8FCB7;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=c4417;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN82853.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN82853.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000645420.1; NC_004431.1.
DR AlphaFoldDB; Q8FCB7; -.
DR SMR; Q8FCB7; -.
DR STRING; 199310.c4417; -.
DR DNASU; 1037857; -.
DR EnsemblBacteria; AAN82853; AAN82853; c4417.
DR KEGG; ecc:c4417; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_036089_2_0_6; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000001410; 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_0000170704"
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; 41124 MW; 3121F924FE9357B7 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 LLGTLEYGLP HKNLIEGIAA AMHFRSEDDP QAQELAALIA DKGPQAALAQ
ISGLDANSEV VSEAVTAYKA MQ