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LDHD_LACPL
ID   LDHD_LACPL              Reviewed;         332 AA.
AC   Q88VJ2; F9UQ12;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=D-lactate dehydrogenase;
DE            Short=D-LDH;
DE            EC=1.1.1.28;
GN   Name=ldhD; OrderedLocusNames=lp_2057;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC         Xref=Rhea:RHEA:16369, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16004, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.28;
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AL935263; CCC79301.1; -; Genomic_DNA.
DR   RefSeq; WP_003640741.1; NC_004567.2.
DR   RefSeq; YP_004889815.1; NC_004567.2.
DR   AlphaFoldDB; Q88VJ2; -.
DR   SMR; Q88VJ2; -.
DR   STRING; 220668.lp_2057; -.
DR   EnsemblBacteria; CCC79301; CCC79301; lp_2057.
DR   GeneID; 57025607; -.
DR   GeneID; 66449834; -.
DR   KEGG; lpl:lp_2057; -.
DR   PATRIC; fig|220668.9.peg.1742; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_1_9; -.
DR   OMA; VIVTAHQ; -.
DR   PhylomeDB; Q88VJ2; -.
DR   BioCyc; LPLA220668:G1GW0-1762-MON; -.
DR   BioCyc; MetaCyc:MON-8683; -.
DR   SABIO-RK; Q88VJ2; -.
DR   Proteomes; UP000000432; Chromosome.
DR   GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
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   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..332
FT                   /note="D-lactate dehydrogenase"
FT                   /id="PRO_0000075955"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        296
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         155..156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         206..207
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         212
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         233..235
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         259
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
SQ   SEQUENCE   332 AA;  37181 MW;  BA65655CCF083F04 CRC64;
     MKIIAYAVRD DERPFFDTWM KENPDVEVKL VPELLTEDNV DLAKGFDGAD VYQQKDYTAE
     VLNKLADEGV KNISLRNVGV DNLDVPTVKA RGLNISNVPA YSPNAIAELS VTQLMQLLRQ
     TPLFNKKLAK QDFRWAPDIA KELNTMTVGV IGTGRIGRAA IDIFKGFGAK VIGYDVYRNA
     ELEKEGMYVD TLDELYAQAD VITLHVPALK DNYHMLNADA FSKMKDGAYI LNFARGTLID
     SEDLIKALDS GKVAGAALDT YEYETKIFNK DLEGQTIDDK VFMNLFNRDN VLITPHTAFY
     TETAVHNMVH VSMNSNKQFI ETGKADTQVK FD
 
 
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