MTLD_LIGS1
ID MTLD_LIGS1 Reviewed; 382 AA.
AC Q1WRQ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=LSL_1618;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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; CP000233; ABE00420.1; -; Genomic_DNA.
DR RefSeq; WP_011476472.1; NC_007929.1.
DR RefSeq; YP_536503.1; NC_007929.1.
DR AlphaFoldDB; Q1WRQ9; -.
DR SMR; Q1WRQ9; -.
DR STRING; 362948.LSL_1618; -.
DR EnsemblBacteria; ABE00420; ABE00420; LSL_1618.
DR KEGG; lsl:LSL_1618; -.
DR PATRIC; fig|362948.14.peg.1713; -.
DR HOGENOM; CLU_036089_2_0_9; -.
DR OMA; GKKAVHF; -.
DR Proteomes; UP000006559; 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 NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..382
FT /note="Mannitol-1-phosphate 5-dehydrogenase"
FT /id="PRO_1000011805"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00196"
SQ SEQUENCE 382 AA; 42778 MW; 433ECC73F7C9FF0F CRC64;
MRAVHFGAGN IGRGFIGETL AANGFGIDFV DVNDTIISAL NQRGEYDIEL AVPGQKKIHV
ENVDGINNGE HPEKVVEAIK TTDLVTTAIG PKILKFIAPL IADGIKARKD ADNKQTLDVI
ACENMIGGSQ HLKEEVYSHL DDDVKAFADE YIGFPNAAVD RIVPLQKHDD PLLVSVEEFK
EWVVDESQMK NPSLKLETVH YAPDLEPYIE RKLFSVNTGH ATVAYTGKAL GYETIGEAIK
DEKVLTQLKN TLKEIRSLLL AKWDFQEKEL EEYHDKIIGR FENPYISDEI ARVGRTPIRK
LGYDERFIRP IRELKARGLS YTTLMETVGK IYHFDEPKDD ESQKLQKMLK DEDLKDVIVE
TTGLKDDADL VAEIAASVKA AD