ID E1LMB7_STRMT Unreviewed; 541 AA.
AC E1LMB7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Malolactic enzyme {ECO:0000313|EMBL:EFN98583.1};
GN ORFNames=SMSK564_1089 {ECO:0000313|EMBL:EFN98583.1};
OS Streptococcus mitis SK564.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=585203 {ECO:0000313|EMBL:EFN98583.1, ECO:0000313|Proteomes:UP000004966};
RN [1] {ECO:0000313|EMBL:EFN98583.1, ECO:0000313|Proteomes:UP000004966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK564 {ECO:0000313|EMBL:EFN98583.1,
RC ECO:0000313|Proteomes:UP000004966};
RA Daugherty S.C., Tallon L.J., Jones K.M., Liu X., Kilian M., Tettelin H.;
RL Submitted (SEP-2010) 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:EFN98583.1}.
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DR EMBL; AEDU01000015; EFN98583.1; -; Genomic_DNA.
DR RefSeq; WP_000123925.1; NZ_AEDU01000015.1.
DR AlphaFoldDB; E1LMB7; -.
DR eggNOG; COG0281; Bacteria.
DR Proteomes; UP000004966; 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 67..249
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 259..515
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-1"
FT BINDING 234
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 258
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-3"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000106-2"
SQ SEQUENCE 541 AA; 59794 MW; 8F59F2E0DE6A2B7D CRC64;
MTAHDILNNP FLNKGTAFTL EERKELGLIG LLPPYVQTIE EQAAQTYAQM QTKANDLEKR
LFLMEIFNTN RTLFYYLFSQ HLEEFNPIVY DPTIADTIEG YSDLFVDPQY AGYLDINHPE
NIEATLKNAA GGREIRLIVV TDAEGILGIG DWGTNGVDIS VGKLMVYTAA AGIDPSMVLP
LVIDAGTNRE ELRNNPNYLG NRHERVRGDR YYDFIDQFVQ TAERLFPKLY LHWEDFGRLN
AANILEKYRK QIPTFNDDIQ GTGIVTLGGI FGSLDISGEK LTDQVYLCYG GGTAGAGIAS
RVLREMVSEG LSEEEAYKRF FMVDKQGLLF DDMDDLTPEQ KPFAKKRADF SNADKLTDLL
EVVKTVKPTI LVGTSTQPNT FTKEIVEAMC ENTERPMIFP LSNPTKLAEA SAKDLIEWSD
GKAFVATGIP ADTVSYKGVD YVIGQANNAL IYPGLGLGML ASEASLLTDE MIGAAAHSLS
GIVNPGQPGA PVLPPFKYVA DVSIKVAEAV AKKAQEQGLA RAKETDMAKA VRDLKWYPEY
K
//
