ID F9VDT1_LACGL Unreviewed; 540 AA.
AC F9VDT1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Malolactic enzyme {ECO:0000313|EMBL:BAK60482.1};
GN OrderedLocusNames=LCGL_1022 {ECO:0000313|EMBL:BAK60482.1};
OS Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK60482.1, ECO:0000313|Proteomes:UP000008520};
RN [1] {ECO:0000313|EMBL:BAK60482.1, ECO:0000313|Proteomes:UP000008520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lg2 {ECO:0000313|EMBL:BAK60482.1,
RC ECO:0000313|Proteomes:UP000008520};
RX PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT "Complete genome sequence and comparative analysis of the fish pathogen
RT Lactococcus garvieae.";
RL PLoS ONE 6:E23184-E23184(2011).
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}.
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DR EMBL; AP009333; BAK60482.1; -; Genomic_DNA.
DR RefSeq; WP_014024819.1; NC_017490.1.
DR AlphaFoldDB; F9VDT1; -.
DR STRING; 420890.LCGL_1022; -.
DR KEGG; lgv:LCGL_1022; -.
DR PATRIC; fig|420890.5.peg.1018; -.
DR eggNOG; COG0281; Bacteria.
DR HOGENOM; CLU_011405_5_2_9; -.
DR Proteomes; UP000008520; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008520}.
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 540 AA; 59460 MW; EF2F3EE1EEE3DB4E CRC64;
MRAHEILNNP FLNKGTAFTM EERKELGLIG LLPPYVQTLE EQAEQTYQHY LEKPSDLEKR
HFLMEIFNTN RTLFYYLFNQ HIVEFNPIVY DPVIAETIEN YSRLFVDPQY AAYLDINHPE
NIQETLKNAA GDRNIRLIVV TDAEGILGIG DWGTQGVDIS VGKLMVYTAA AGIDPASVLP
IVIDAGTNRK ELLEDSMYLG NRHTRVYGDQ YYDFVDQFVE TAEAMFPKLY LHWEDFGRSN
AANILNKYKK EIPTFNDDIQ GTGIVVLGGI FGSLDITGEK LTDQVYLCYG GGSAGAGIAD
RVHAEMVSEG LSEEEAYNHF FMMDKQGLLF DDMEDLTPAQ KPFAKKRADF ANAGDMTDLA
NVIKTVKATI LVGTSTDAGA FTKEVVEAMC ANTERPVIFP ISNPTKKLEA TAEQVITWSD
GKAFVATGIP SGTVSYKGVD YQIGQANNAL IYPGLGLGML ASEASLLTDE MIGAAAHSLS
GLVDPGAAGA PVLPPFEYVA DVSIKVAEAV AKKAQEQGLA QAQEKDMVKA VREMKWYPKY
//
