ID   LDHD_PEDAC              Reviewed;         331 AA.
AC   Q59642;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=D-lactate/D-glycerate dehydrogenase {ECO:0000305};
DE            Short=D-LDH/GDH {ECO:0000305};
DE            EC=1.1.1.28 {ECO:0000269|PubMed:7539419};
DE            EC=1.1.1.29 {ECO:0000269|PubMed:7539419};
DE   AltName: Full=D-specific 2-hydroxyacid dehydrogenase {ECO:0000305};
GN   Name=ldhD {ECO:0000303|PubMed:7539419};
OS   Pediococcus acidilactici.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus; Pediococcus acidilactici group.
OX   NCBI_TaxID=1254;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DG302;
RX   PubMed=7539419; DOI=10.1128/jb.177.12.3427-3437.1995;
RA   Garmyn D., Ferain T., Bernard N., Hols P., Delplace B., Delcour J.;
RT   "Pediococcus acidilactici ldhD gene: cloning, nucleotide sequence, and
RT   transcriptional analysis.";
RL   J. Bacteriol. 177:3427-3437(1995).
CC   -!- FUNCTION: Has both D-lactate and D-glycerate dehydrogenase activities.
CC       Equally active on pyruvate and hydroxypyruvate.
CC       {ECO:0000269|PubMed:7539419}.
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         Evidence={ECO:0000269|PubMed:7539419};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC         Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.29;
CC         Evidence={ECO:0000269|PubMed:7539419};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26297}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X70925; CAA50275.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59642; -.
DR   SMR; Q59642; -.
DR   STRING; 1254.A4V11_01320; -.
DR   PRIDE; Q59642; -.
DR   GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008465; F:glycerate 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..331
FT                   /note="D-lactate/D-glycerate dehydrogenase"
FT                   /id="PRO_0000075958"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        295
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         154..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         174
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         205..206
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         211
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         232..234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         258
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
SQ   SEQUENCE   331 AA;  37210 MW;  C2E6653EC661AEB8 CRC64;
     MKIIAYGIRD DEKPYLDEWV TKNHIEVKAV PDLLDSSNID LAKDYDGVVA YQQKPYTADL
     FDKMHEFGIH AFSLRNVGLD NVPADALKKN DIKISNVPAY SPRAIAELSV TQLLALLRKI
     PEFEYKMAHG DYRWEPDIGL ELNQMTVGVI GTGRIGRAAI DIFKPFGAKV IAYDVFRNPA
     LEKEGMYVDT LEELYQQANV ITLHVPALKD NYHMLDEKAF GQMQDGTFIL NFARGTLVDT
     PALLKALDSG KVAGAALDTY ENEVGIFDVD HGDQPIDDPV FNDLMSRRNV MITPHAAFYT
     RPAVKNMVQI ALDNNRDLIE KNSSKNEVKF E