ID D3LB62_OENOE Unreviewed; 541 AA.
AC D3LB62;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Malolactic enzyme {ECO:0008006|Google:ProtNLM};
GN ORFNames=AWRIB429_1592 {ECO:0000313|EMBL:EFD87766.1};
OS Oenococcus oeni AWRIB429.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=655225 {ECO:0000313|EMBL:EFD87766.1, ECO:0000313|Proteomes:UP000003075};
RN [1] {ECO:0000313|EMBL:EFD87766.1, ECO:0000313|Proteomes:UP000003075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRIB429 {ECO:0000313|EMBL:EFD87766.1,
RC ECO:0000313|Proteomes:UP000003075};
RX PubMed=20111862; DOI=10.1007/s00253-009-2425-6;
RA Borneman A.R., Bartowsky E.J., McCarthy J., Chambers P.J.;
RT "Genotypic diversity in Oenococcus oeni by high-density microarray
RT comparative genome hybridization and whole genome sequencing.";
RL Appl. Microbiol. Biotechnol. 86:681-691(2010).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFD87766.1}.
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DR EMBL; ACSE01000029; EFD87766.1; -; Genomic_DNA.
DR RefSeq; WP_002819378.1; NZ_ACSE01000029.1.
DR AlphaFoldDB; D3LB62; -.
DR GeneID; 75066475; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000003075; Unassembled WGS sequence.
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; 59118 MW; F82D8F9FA91E45E4 CRC64;
MTDPVSILND PFINKGTAFT EAEREELGLN GLLPAKVQAL QEQVDQTYAQ FQSKVSNLEK
RLFLMEIFNT NHVLFYKLFS QHVVEFMPIV YDPTIADTIE NYSELFVEPQ GAAFLDINHP
ENIQSTLKNA ANGRDIKLLV VSDGEGILGI 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
//
