LDHD_STAES
ID LDHD_STAES Reviewed; 330 AA.
AC Q8CN22;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=D-lactate dehydrogenase;
DE Short=D-LDH;
DE EC=1.1.1.28;
DE AltName: Full=D-specific 2-hydroxyacid dehydrogenase;
GN Name=ldhD; Synonyms=ddh; OrderedLocusNames=SE_2074;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05716.1; -; Genomic_DNA.
DR RefSeq; NP_765629.1; NC_004461.1.
DR RefSeq; WP_002456690.1; NZ_WBME01000003.1.
DR AlphaFoldDB; Q8CN22; -.
DR SMR; Q8CN22; -.
DR STRING; 176280.SE_2074; -.
DR EnsemblBacteria; AAO05716; AAO05716; SE_2074.
DR GeneID; 50017841; -.
DR KEGG; sep:SE_2074; -.
DR PATRIC; fig|176280.10.peg.2026; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_9; -.
DR OMA; IAFYTNT; -.
DR Proteomes; UP000001411; 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.
FT CHAIN 1..330
FT /note="D-lactate dehydrogenase"
FT /id="PRO_0000075966"
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 156..157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT BINDING 176
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 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 330 AA; 36526 MW; E49590DB57226722 CRC64;
MTKIMFFGTR AYEKDMALRW GKKNNIDVTT STELLSVDTV DQLKDYDGVT TMQFGKLEPE
VYPKLESYGI KQIAQRTAGF DMYDLELAKK HEIIISNIPS YSPETIAEYS VSIALQLVRK
FPTIEKRVQA HNFTWASPIM SRPVKNMTVA IIGTGRIGAA TGKIYAGFGA RVVGYDAYPN
HSLSFLEYKE TVEDAIKDAD IISLHVPANK DSFHLFDNNM FKNVKKGAVL VNAARGAVIN
TPDLIEAVNN GTLSGAAIDT YENEANYFTF DCSNQTIDDP ILLDLIRNEN ILVTPHIAFF
SDEAVQNLVE GGLNAALSVI NTGTCDTRLN
