LDHD_LEUMC
ID LDHD_LEUMC Reviewed; 331 AA.
AC P51011;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Leuconostoc mesenteroides subsp. cremoris.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=33965;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=195;
RX PubMed=7569323; DOI=10.1016/0923-2508(96)81052-7;
RA Dartois V., Phalip V., Schmitt P., Divies C.;
RT "Purification, properties and DNA sequence of the D-lactate dehydrogenase
RT from Leuconostoc mesenteroides subsp. cremoris.";
RL Res. Microbiol. 146:291-302(1995).
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 -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; L29327; AAA99506.1; -; Genomic_DNA.
DR AlphaFoldDB; P51011; -.
DR SMR; P51011; -.
DR BioCyc; MetaCyc:MON-13061; -.
DR BRENDA; 1.1.1.28; 839.
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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..331
FT /note="D-lactate dehydrogenase"
FT /id="PRO_0000075957"
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 331 AA; 36316 MW; 0A63C462303672D8 CRC64;
MKIFAYGIRD DEKPSLEEWK AANPEIEVDY TQELLTPETA KLAEGSDSAV VYQQLDYTRE
TLTALANVGV TNLSLRNVGT DNIDFDAARE FNFNISNVPV YSPNAIAEHS MLQLSRLLRR
TKALDAKIAK RDLRWAPTTG REMRMQTVGV IGTGHIGRVA INILKGFGAK VIAYDKYPNA
ELQAEGLYVD TLDELYAQAD AISLYVPGVP ENHHLINADA IAKMKDGVVI MNAARGNLMD
IDAIIDGLNS GKISDFGMDV YENEVACSMK IGLVKNSPDA KIADLIAREN VMITPHTAFY
TTKAVLEMVH QSFDAAVAFA KGEKPAIAVE Y
