ID W9EI83_9LACO Unreviewed; 547 AA.
AC W9EI83;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Malolactic enzyme {ECO:0000313|EMBL:ETO40720.1};
GN ORFNames=B808_382 {ECO:0000313|EMBL:ETO40720.1};
OS Fructilactobacillus florum 8D.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1221538 {ECO:0000313|EMBL:ETO40720.1, ECO:0000313|Proteomes:UP000019474};
RN [1] {ECO:0000313|EMBL:ETO40720.1, ECO:0000313|Proteomes:UP000019474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8D {ECO:0000313|EMBL:ETO40720.1,
RC ECO:0000313|Proteomes:UP000019474};
RA Kim E.B., Marco M.L.;
RT "Genome sequencing of Lactobacillus florum 8D.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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:ETO40720.1}.
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DR EMBL; ALXG01000015; ETO40720.1; -; Genomic_DNA.
DR RefSeq; WP_035421567.1; NZ_ALXG01000015.1.
DR AlphaFoldDB; W9EI83; -.
DR PATRIC; fig|1221538.3.peg.388; -.
DR OrthoDB; 3314528at2; -.
DR Proteomes; UP000019474; 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 CDD; cd05312; NAD_bind_1_malic_enz; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019474}.
FT DOMAIN 68..252
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 262..518
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 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 237
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 238
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 547 AA; 59637 MW; 9C534747D353CEF5 CRC64;
MTRSQEIVNN PFLNKGTAFS ATERKDLHLE GMLPPRIQTL DQQTDRVYAQ YQEMSTDLEK
RMYLMSVFNE NRVLFYATFA KHVSEFMPIV YDPTIADSIE NYSRLYVNPQ NAAYLSINDH
SRATIRESLI NAAEGRNVKL LVVTDGEGIL GIGDWGTQGI DIPVGKLMVY TAAAGIDPSE
ILPVVLDAGT TRASLKNDPL YVGLDQDRDY SENYYEFVDN FVQEAESLFP NLYLHFEDFG
RANAAKILEK YQDQFLVFND DIQGTGIIVL AGVLGALNIS GESMTDQKYL CFGAGTAGVG
IAQRVAEEMV QAGLSEAEAK KHFYMVDKQG LLFDDMPDLT PGQQEFARSR SEFDNADELT
DLLSVVQAVH PTIMVGTSTV HGAFTQEVVT EMAAHTNRPI ILPISNPTKL AEATAADLIK
WTNGRALVAT GVPSAPVEHD GVTYEIGQAN NALVYPGIGL GAIAATATTL NDEMISAAAH
SLGGIVDSSK PGAAILPPVE QLTEFSQTVA NAVAQSAVDQ GVTREQISDV KAAVEAEKWY
PVYRELN
//
