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Database: UniProt
Entry: B1MWB3_LEUCK
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Original site: B1MWB3_LEUCK 
ID   B1MWB3_LEUCK            Unreviewed;       304 AA.
AC   B1MWB3;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   SubName: Full=Malate/lactate dehydrogenase {ECO:0000313|EMBL:ACA83478.1};
GN   OrderedLocusNames=LCK_01655 {ECO:0000313|EMBL:ACA83478.1};
OS   Leuconostoc citreum (strain KM20).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA83478.1, ECO:0000313|Proteomes:UP000002166};
RN   [1] {ECO:0000313|EMBL:ACA83478.1, ECO:0000313|Proteomes:UP000002166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM20 {ECO:0000313|EMBL:ACA83478.1,
RC   ECO:0000313|Proteomes:UP000002166};
RX   PubMed=18281406; DOI=10.1128/JB.01862-07;
RA   Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA   Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT   "Complete genome sequence of Leuconostoc citreum KM20.";
RL   J. Bacteriol. 190:3093-3094(2008).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
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DR   EMBL; DQ489736; ACA83478.1; -; Genomic_DNA.
DR   RefSeq; WP_004908858.1; NC_010471.1.
DR   AlphaFoldDB; B1MWB3; -.
DR   STRING; 349519.LCK_01655; -.
DR   GeneID; 61103160; -.
DR   KEGG; lci:LCK_01655; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_1_2_9; -.
DR   OMA; IVSHYDD; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000002166; Chromosome.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF31; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369}.
FT   DOMAIN          3..143
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          146..296
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         119..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   304 AA;  32411 MW;  410A611F9BCED321 CRC64;
     MRKIGIVGIG HVGSTVAHLI ISQGLADELI LVDKNTAKRD SEVLDFRDAA SLLPHHVHIA
     SGTPADLADA DVVISALGHI DLIEPGGDRF TELRANTPEV QQVGQALHRA RFNGVLIVIS
     NPVDVITGIY QQVTGLPANQ VFGTGTYLDT ARLKRSLGDA LNVDPRSIQG YMLGEHGDSQ
     FAAWSTVRVL GQKADELVTN YHLDLDAVAN DARVGGFTVF SGKKYTNFAI AHAAVSLAQL
     VLSDAHNEAI VSHYDARFAG YISTPAIIGR SGVVANFELT LTADEQRALQ QSANAIAEKT
     AAYL
//
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