MLES_LACLA
ID MLES_LACLA Reviewed; 540 AA.
AC Q48662; Q48645;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Malolactic enzyme {ECO:0000303|PubMed:8405453};
DE Short=MLE {ECO:0000303|PubMed:8405453};
DE EC=4.1.1.101 {ECO:0000250|UniProtKB:Q48796};
GN Name=mleS {ECO:0000303|PubMed:8405453}; OrderedLocusNames=LL0900;
GN ORFNames=L121483;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=IL1441;
RX PubMed=8405453; DOI=10.1016/0014-5793(93)80488-g;
RA Ansanay V., Dequin S., Blondin B., Barre P.;
RT "Cloning, sequence and expression of the gene encoding the malolactic
RT enzyme from Lactococcus lactis.";
RL FEBS Lett. 332:74-80(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=IL1441;
RX PubMed=8132158; DOI=10.1111/j.1574-6968.1994.tb06679.x;
RA Denayrolles M., Aigle M., Lonvaud-Funel A.;
RT "Cloning and sequence analysis of the gene encoding Lactococcus lactis
RT malolactic enzyme: relationships with malic enzymes.";
RL FEMS Microbiol. Lett. 116:79-86(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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:8132158, ECO:0000269|PubMed:8405453}.
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:0000250|UniProtKB:Q48796};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q48796};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q48796};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q48796}.
CC -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50716.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X75982; CAA53589.1; -; Genomic_DNA.
DR EMBL; X71897; CAA50716.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE005176; AAK04998.1; -; Genomic_DNA.
DR PIR; D86737; D86737.
DR PIR; S38728; S38728.
DR RefSeq; NP_267056.1; NC_002662.1.
DR RefSeq; WP_010905616.1; NC_002662.1.
DR AlphaFoldDB; Q48662; -.
DR SMR; Q48662; -.
DR STRING; 272623.L121483; -.
DR PaxDb; Q48662; -.
DR PRIDE; Q48662; -.
DR EnsemblBacteria; AAK04998; AAK04998; L121483.
DR KEGG; lla:L121483; -.
DR PATRIC; fig|272623.7.peg.965; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_9; -.
DR OMA; QMWDPVY; -.
DR BRENDA; 4.1.1.101; 2903.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB.
DR GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0043464; P:malolactic fermentation; ISS: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 3: Inferred from homology;
KW Lyase; Manganese; Metal-binding; NAD; Reference proteome.
FT CHAIN 1..540
FT /note="Malolactic enzyme"
FT /id="PRO_0000160249"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 291..294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 403
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 448
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P40927"
FT CONFLICT 44
FT /note="E -> V (in Ref. 1; CAA53589)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="N -> S (in Ref. 1; CAA53589)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="Y -> H (in Ref. 1; CAA53589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 540 AA; 59517 MW; D7ED86C76BA676D8 CRC64;
MRAHEILNNP FLNKGTAFTM KERQELGLIG LLPPTVQTIE EQAEQTYEQY LTKPSDLEKR
HFLMEIFNTN RTLFYYLFNK HIVEFNPVVY DPTIADTIEN YSHLFVDPQY AAYLDINHPE
NITETLKNAA GDREIRLIVV TDAEGILGIG DWGTQGVDIS VGKLMIYTAA AGIDPASVLP
VVIDAGTNRK ELLEDHLYLG NHQERIYGDQ YYSFVDQFVE TAESIFPKLY LHWEDFGRSN
AATILNNYKT KIPTFNDDIQ GTGIVVLGGI FGSLDITGEK LTDQVYLCYG GGSAGAGIAG
RVHAEMVSEG LSEEEAYKHF FMIDQQGLLF DDMEDLTPAQ KPFAKKRADY KDAGDMTDLL
NVVKTVKPTI LVGTSTNPGA FTKEVVEAMC ANTERPVIFP ISNPTKKMET TAEQVIEWSD
GKAFVATGVP SGTISYKGVD YQIGQANNSL IYPGLGLGML ASEAKLLTDE MIGAAAHSLS
GLVDPGKPGA PVLPPFEFVA DVSIKVAEAV AKKAQEQGLT ESKETDMAKA VRDLKWYPEY
