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 02-NOV-2016, entry version 13. 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 RT pulque, a traditional Mexican alcoholic fermented beverage."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RP AND ENZYME 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, CC which results in a natural decrease in acidity and favorable CC changes in wine flavors. Catalyzes the decarboxylation of L-malate CC to L-lactate. {ECO:0000269|PubMed:16345941}. CC -!- CATALYTIC ACTIVITY: (S)-malate = (S)-lactate + CO(2). CC {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 -!- ENZYME 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 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:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0043464; P:malolactic fermentation; IDA:UniProtKB. DR Gene3D; 3.40.50.10380; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR015884; Malic_enzyme_CS. DR InterPro; IPR012301; Malic_N_dom. DR InterPro; IPR012302; Malic_NAD-bd. DR InterPro; IPR001891; Malic_OxRdtase. DR InterPro; IPR016040; NAD(P)-bd_dom. 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 Malolactic enzyme. FT /FTId=PRO_0000435672. FT NP_BIND 293 296 NAD. {ECO:0000250|UniProtKB:P40927}. FT ACT_SITE 92 92 Proton donor. FT {ECO:0000250|UniProtKB:P40927}. FT ACT_SITE 165 165 Proton acceptor. FT {ECO:0000250|UniProtKB:P40927}. FT METAL 236 236 Manganese. FT {ECO:0000250|UniProtKB:P40927}. FT METAL 237 237 Manganese. FT {ECO:0000250|UniProtKB:P40927}. FT METAL 260 260 Manganese. FT {ECO:0000250|UniProtKB:P40927}. FT BINDING 165 165 Substrate. FT {ECO:0000250|UniProtKB:P40927}. FT BINDING 405 405 NAD. {ECO:0000250|UniProtKB:P40927}. FT BINDING 450 450 NAD. {ECO:0000250|UniProtKB:P40927}. FT BINDING 450 450 Substrate. FT {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 //