MLES_LEUME
ID MLES_LEUME Reviewed; 542 AA.
AC A0A095AMW7;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Malolactic enzyme {ECO:0000303|PubMed:16345941};
DE Short=MLE {ECO:0000303|PubMed:16345941};
DE EC=4.1.1.101 {ECO:0000269|PubMed:16345941};
GN Name=mleS; ORFNames=LH61_04880;
OS Leuconostoc mesenteroides.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=1245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P45;
RA Riveros-Mckay F., Campos I., Giles-Gomez M., Bolivar F., Escalante A.;
RT "Genome sequence of Leuconostoc mesenteroides P45 isolated from pulque, a
RT traditional Mexican alcoholic fermented beverage.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP ACTIVITY REGULATION.
RX PubMed=16345941; DOI=10.1128/aem.43.2.357-361.1982;
RA Lonvaud-Funel A., de Saad A.M.;
RT "Purification and Properties of a Malolactic Enzyme from a Strain of
RT Leuconostoc mesenteroides Isolated from Grapes.";
RL Appl. Environ. Microbiol. 43:357-361(1982).
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:16345941}.
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:16345941};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16345941};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:16345941};
CC -!- ACTIVITY REGULATION: Oxamate, fructose-1,6-diphosphate and L-lactate
CC act as non-competitive inhibitors, whereas succinate, citrate and
CC tartrate isomers produce a competitive inhibition.
CC {ECO:0000269|PubMed:16345941}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.043 mM for NAD {ECO:0000269|PubMed:16345941};
CC KM=16.7 mM for (S)-malate {ECO:0000269|PubMed:16345941};
CC pH dependence:
CC Optimum pH is 4.35. {ECO:0000269|PubMed:16345941};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q48796}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR EMBL; JRGZ01000002; KGB50834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095AMW7; -.
DR SMR; A0A095AMW7; -.
DR EnsemblBacteria; KGB50834; KGB50834; LH61_04880.
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.
FT CHAIN 1..542
FT /note="Malolactic enzyme"
FT /id="PRO_0000435672"
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 542 AA; 59205 MW; F2B6A27F7E2AA86E CRC64;
MNTTGYDILR NPFLNKGTAF SEAERQQLGL TGTLPSQIQT IEEQAEQAYK QFQAKSPLLE
KRIFLMNLFN ENVTLFYHLM DQHVSEFMPI VYDPVVAESI EQYNEIYTNP QNAAFLSVDR
PEDVENALKN AAAGRDIKLV VVTDAEGILG MGDWGVNGVD IAVGKLMVYT AAAGIDPATV
LPVSIDAGTN NKELLHNPLY LGNKHERIAG EQYLEFIDKF VTAEQNLFPE SLLHWEDFGR
SNAQVILDKY KESIATFNDD IQGTGMIVLA GIFGALNISK QKLVDQKFVT FGAGTAGMGI
VNQIFSELKQ AGLSDDEARN HFYLVDKQGL LFDDTEGLTA AQKPFTRSRK EFVNPEQLIN
LETIVKELHP TVLIGTSTQP GTFTETIVKS MAENTERPII FPLSNPTKLA EATAEDLIKW
TGGKALVATG IPAADVDYKG VTYKIGQGNN ALIYPGLGFG LVASTAKLLT QETISAAIHA
LGGLVDTDEP GAAVLPPVSN LTDFSQKIAE ITAQSVVNQG LNREKIVDPK QAVQDAKWSA
EY
