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Database: UniProt
Entry: B1MX03_LEUCK
LinkDB: B1MX03_LEUCK
Original site: B1MX03_LEUCK 
ID   B1MX03_LEUCK            Unreviewed;       330 AA.
AC   B1MX03;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:ACA82055.1};
GN   OrderedLocusNames=LCK_00222 {ECO:0000313|EMBL:ACA82055.1};
OS   Leuconostoc citreum (strain KM20).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA82055.1, ECO:0000313|Proteomes:UP000002166};
RN   [1] {ECO:0000313|EMBL:ACA82055.1, ECO:0000313|Proteomes:UP000002166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM20 {ECO:0000313|EMBL:ACA82055.1,
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 D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; DQ489736; ACA82055.1; -; Genomic_DNA.
DR   RefSeq; WP_004903761.1; NC_010471.1.
DR   AlphaFoldDB; B1MX03; -.
DR   STRING; 349519.LCK_00222; -.
DR   KEGG; lci:LCK_00222; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_1_9; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000002166; Chromosome.
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   CDD; cd12186; LDH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR   PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          10..328
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          114..299
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   330 AA;  36346 MW;  912CDBB7EAE9BF36 CRC64;
     MTKILMTSVR SDEEPSIKTY AKAHNLQIDM VREEFHPGQH DNLSEYNGLI VQQTANIGGD
     EAFYQSLVHQ GLKQITTRTA GVDMIPVTLA KRAGLKITNV PKYSPRSVAE LALTQIFQLL
     RRTWAFEQRM NQNDFRWAGL QAREIHTITV GIIGAGRIGG TLAKLLHLLG AKVIAYDVKP
     QECLKKYLTY VSKATLLAQS DVISVHVDLN DSTVGLLQAV DFNQMKIGSL FLNMSRGDVV
     NTEALIAALL SGKIQAAALD TVTGESLVFN RDLRQQGIDN SQIRQLMAMP NVLLTPHIAF
     FTNIAVDNMV NTALDDVLAI ISGHQAVNEI
//
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