ID Q5S3L3_OENOE Unreviewed; 541 AA.
AC Q5S3L3; K6Q630;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Malolactic enzyme {ECO:0000313|EMBL:AAV65766.1};
DE SubName: Full=NAD-dependent malic enzyme {ECO:0000313|EMBL:USO99232.1};
GN Name=mleA {ECO:0000313|EMBL:AAV65766.1};
GN ORFNames=LOD97_08500 {ECO:0000313|EMBL:USO99232.1};
OS Oenococcus oeni (Leuconostoc oenos).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=1247 {ECO:0000313|EMBL:AAV65766.1};
RN [1] {ECO:0000313|EMBL:AAV65766.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SD-2a {ECO:0000313|EMBL:AAV65766.1};
RA Liu Y., Jiang S., Li H., He X., Zhang B.;
RT "Sequence and analysis of malolactic enzyme gene from Oenococcus oeni.";
RL Wei Sheng Wu Xue Za Zhi 24:29-30(2004).
RN [2] {ECO:0000313|EMBL:ACX48921.1}
RP NUCLEOTIDE SEQUENCE.
RA Schuemann C., Michlmayr H., Barreira Braz da Silva N.M., del Hierro A.M.,
RA Kulbe K.D.;
RT "Overexpression of MLE from Oenococcus oeni in Escherichia coli.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ACX48921.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22452826; DOI=10.1186/2191-0855-2-19;
RA Schumann C., Michlmayr H., Eder R., Del Hierro A.M., Kulbe K.D.,
RA Mathiesen G., Nguyen T.H.;
RT "Heterologous expression of Oenococcus oeni malolactic enzyme in
RT Lactobacillus plantarum for improved malolactic fermentation.";
RL AMB Express 2:19-19(2012).
RN [4] {ECO:0000313|EMBL:USO99232.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SD-2a {ECO:0000313|EMBL:USO99232.1};
RX PubMed=35716166;
RA Liu L., Peng S., Song W., Zhao H., Li H., Wang H.;
RT "Genomic Analysis of an Excellent Wine-Making Strain Oenococcus oeni SD-
RT 2a.";
RL Pol. J. Microbiol. 71:279-292(2022).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC Note=Divalent metal cations. Prefers magnesium or manganese.
CC {ECO:0000256|PIRSR:PIRSR000106-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785, ECO:0000256|RuleBase:RU003427}.
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; AY786176; AAV65766.1; -; Genomic_DNA.
DR EMBL; GQ911572; ACX48921.1; -; Genomic_DNA.
DR EMBL; CP087569; USO99232.1; -; Genomic_DNA.
DR RefSeq; WP_002821690.1; NZ_SNSU01000001.1.
DR SMR; Q5S3L3; -.
DR BRENDA; 4.1.1.101; 3009.
DR Proteomes; UP001055671; Chromosome.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0043883; F:malolactic enzyme activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0043464; P:malolactic fermentation; IEA:InterPro.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_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; IPR048182; Malolactic_enz.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF041582; malolactic; 1.
DR PANTHER; PTHR23406; MALIC ENZYME-RELATED; 1.
DR PANTHER; PTHR23406:SF32; NAD-DEPENDENT MALIC ENZYME, MITOCHONDRIAL; 1.
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; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000106-3}.
FT DOMAIN 68..250
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 260..516
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 236
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 259
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 541 AA; 59132 MW; 7D6AAEE393273AFE CRC64;
MTDPVSILND PFINKGTAFT EAEREELGLN GLLPAKVQAL QEQVDQTYAQ FQSKVSNLEK
RLFLMEIFNT NHVLFYKLFS QHVVEFMPIV YDPTIADTIE NYSELFVEPQ GAAFLDINHP
ENIQSTLKNA ANGRDIKLLV VSDAEGILGI GDWGVQGVDI AVGKLMVYTV AAGIDPSTVL
AVVIDAGTNN EKLLKDPMYL GNKFNRVRGD KYYDFIDKFV NHAESLFPNL YLHWEDFGRS
NASNILNSYK DKIATFNDDI QGTGIVVLAG VLGALKISGQ KLTDQTYMSF GAGTAGMGIV
KQLHEEMVEQ GLSDEEAKKH FFLVDKQGLL FDDDPDLTPE QKPFAAKRSD FKNANQLTNL
QAAVEAVHPT ILVGTSTHPN SFTEEIVKDM SGYTERPIIF PISNPTKLAE AKAEDVLKWS
NGKALIGTGV PVDDIEYEGN AYQIGQANNA LIYPGLGFGA IAAQSKLLTP EMISAAAHSL
GGIVDTTKVG AAVLPPVSKL ADFSRTVAVA VAKKAVEQGL NRQPIDDVEK AVDDLKWEPK
Y
//
