ID   LDHD_LACPE              Reviewed;         332 AA.
AC   P26298;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=D-lactate dehydrogenase;
DE            Short=D-LDH;
DE            EC=1.1.1.28;
DE   AltName: Full=D-specific 2-hydroxyacid dehydrogenase;
OS   Lactiplantibacillus pentosus (Lactobacillus pentosus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8041 / DSM 20314 / BCRC 11053 / JCM 1558 / KCTC 3120 / LMG
RC   10755 / NBRC 106467 / NCDO 363 / NCIMB 8026 / 124-2;
RX   PubMed=1840590; DOI=10.1016/s0021-9258(18)98939-8;
RA   Ohta T., Taguchi H.;
RT   "D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid
RT   dehydrogenase family. Cloning, sequencing, and expression in Escherichia
RT   coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum.";
RL   J. Biol. Chem. 266:12588-12594(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=8740366; DOI=10.1016/s0969-2126(96)00049-4;
RA   Stoll V.S., Kimber M.S., Pai E.F.;
RT   "Insights into substrate binding by D-2-ketoacid dehydrogenases from the
RT   structure of Lactobacillus pentosus D-lactate dehydrogenase.";
RL   Structure 4:437-447(1996).
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   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: Also active on D-glycerate.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from L.plantarum.
CC       {ECO:0000305|PubMed:1840590}.
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DR   EMBL; D90339; BAA14352.1; -; Genomic_DNA.
DR   PIR; A40885; A40885.
DR   AlphaFoldDB; P26298; -.
DR   SMR; P26298; -.
DR   STRING; 1589.GCA_001188985_01186; -.
DR   SABIO-RK; P26298; -.
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   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..332
FT                   /note="D-lactate dehydrogenase"
FT                   /id="PRO_0000075956"
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"
SQ   SEQUENCE   332 AA;  37183 MW;  FA63723C63B53EBE CRC64;
     MKIIAYAVRD DERPFFDTWM KENPDVEVKL VPELLTEDNV DLAKGFDGAD VYQQKDYTAE
     VLNKLADEGV KNISLRNVGV DNLDVPTVKA RGLNISNVPA YSPNAIAELS VTQLMQLLRQ
     TPMFNKKLAK QDFRWAPDIA KELNTMTVGV IGTGRIGRAA IDIFKGFGAK VIGYDVYRNA
     ELEKEGMYVD TLDELYAQAD VITLHVPALK DNYHMLNADA FSKMKDGAYI LNFARGTLID
     SEDLIKALDS GKVAGAALVT YEYETKIFNK DLEGQTIDDK VFMNLFNRDN VLITPHTAFY
     TETAVHNMVH VSMNSNKQFI ETGKADTQVK FD