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 11-DEC-2019, entry version 20. 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; Leuconostocaceae; 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; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JRGZ01000002; KGB50834.1; -; Genomic_DNA. 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; 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 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 NP_BIND 293..296 FT /note="NAD" FT /evidence="ECO:0000250|UniProtKB:P40927" 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 METAL 236 FT /note="Manganese" FT /evidence="ECO:0000250|UniProtKB:P40927" FT METAL 237 FT /note="Manganese" FT /evidence="ECO:0000250|UniProtKB:P40927" FT METAL 260 FT /note="Manganese" FT /evidence="ECO:0000250|UniProtKB:P40927" FT BINDING 165 FT /note="Substrate" FT /evidence="ECO:0000250|UniProtKB:P40927" FT BINDING 405 FT /note="NAD" FT /evidence="ECO:0000250|UniProtKB:P40927" FT BINDING 450 FT /note="NAD" FT /evidence="ECO:0000250|UniProtKB:P40927" FT BINDING 450 FT /note="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 //