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-MAY-2023, entry version 95.
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; Bacillota; 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}.
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DR EMBL; X70925; CAA50275.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59642; -.
DR SMR; Q59642; -.
DR STRING; 1254.A4V11_01320; -.
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 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; 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
//
