MLES_LACPL
ID MLES_LACPL Reviewed; 547 AA.
AC F9UMS6;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Malolactic enzyme {ECO:0000303|PubMed:6833282};
DE Short=MLE {ECO:0000303|PubMed:6833282};
DE EC=4.1.1.101 {ECO:0000269|PubMed:6833282};
GN Name=mleS {ECO:0000303|PubMed:6833282}; OrderedLocusNames=lp_1118;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RX PubMed=6833282; DOI=10.1016/s0021-9258(18)32513-4;
RA Caspritz G., Radler F.;
RT "Malolactic enzyme of Lactobacillus plantarum. Purification, properties,
RT and distribution among bacteria.";
RL J. Biol. Chem. 258:4907-4910(1983).
CC -!- FUNCTION: Involved in the malolactic fermentation (MLF) of wine, which
CC results in a natural decrease in acidity and favorable changes in wine
CC flavors. Catalyzes the decarboxylation of L-malate to L-lactate.
CC {ECO:0000269|PubMed:6833282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + H(+) = (S)-lactate + CO2; Xref=Rhea:RHEA:46276,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16651; EC=4.1.1.101;
CC Evidence={ECO:0000269|PubMed:6833282};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:6833282};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:6833282};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.012 mM for manganese {ECO:0000269|PubMed:6833282};
CC KM=0.059 mM for NAD {ECO:0000269|PubMed:6833282};
CC KM=9.5 mM for (S)-malate {ECO:0000269|PubMed:6833282};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6833282}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; AL935263; CCC78515.1; -; Genomic_DNA.
DR RefSeq; WP_011101261.1; NC_004567.2.
DR RefSeq; YP_004889029.1; NC_004567.2.
DR AlphaFoldDB; F9UMS6; -.
DR SMR; F9UMS6; -.
DR STRING; 220668.lp_1118; -.
DR EnsemblBacteria; CCC78515; CCC78515; lp_1118.
DR KEGG; lpl:lp_1118; -.
DR PATRIC; fig|220668.9.peg.945; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_9; -.
DR OMA; QMWDPVY; -.
DR PhylomeDB; F9UMS6; -.
DR BioCyc; LPLA220668:G1GW0-958-MON; -.
DR Proteomes; UP000000432; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0043464; P:malolactic fermentation; IDA:UniProtKB.
DR Gene3D; 3.40.50.10380; -; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PIRSF; PIRSF000106; ME; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Lyase; Manganese; Metal-binding; NAD; Reference proteome.
FT CHAIN 1..547
FT /note="Malolactic enzyme"
FT /id="PRO_0000435671"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 236
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 260
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 293..296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 405
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 450
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40927"
SQ SEQUENCE 547 AA; 59465 MW; 1BE828D5F4DF292E CRC64;
MTKTASEILN NPFLNKGTAF TKEERQALGL TGTLPSKVQT IDEQATQAYA QFKSKPSRLE
QRIFLMNLFN ENRTLFFHLM DEHVVEFMPI VYDPVVADSI EQYNELFLDP QNAAFVSVDA
PEDIEATLKN AADGRDIRLV VVTDAEGILG MGDWGVNGVD IAIGKLMVYT AAAGIDPSQV
LPVSIDAGTN NQKLLDDPLY LGNRHKCVSG EQYYDVIDKF VAAEQQLFPD SLLHFEDFGR
DNAQVILDKY KDQIATFNDD IQGTGMVVLA GILGALNISK ESIKDQKILS FGAGTAGMGI
ANQILDELMQ AGLTEEEAKQ HFYAVDKQGL LFDDTEGLTP AQKAFTRKRS EFSNADELTN
LEAVVKAVHP TVMIGTSTQP GTFTESIIKE MAAHTERPII FPLSNPTKLA EAKAEDLIKW
TDGRALVATG IPADDVEYKG VTYQIGQGNN ALMYPGLGFG LIASTAKVLN AETLSAACHA
LGGIVDTSKP GAAVLPPVAK ITEFSQKLAE VVAQSVIDQK LNKEPIADAK QAVADMKWVP
EYRAISK
