LDHD_STAAC
ID LDHD_STAAC Reviewed; 330 AA.
AC Q5HD29;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=SACOL2535;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW37312.1; -; Genomic_DNA.
DR RefSeq; WP_000161536.1; NC_002951.2.
DR AlphaFoldDB; Q5HD29; -.
DR SMR; Q5HD29; -.
DR EnsemblBacteria; AAW37312; AAW37312; SACOL2535.
DR KEGG; sac:SACOL2535; -.
DR HOGENOM; CLU_019796_1_1_9; -.
DR OMA; IAFYTNT; -.
DR Proteomes; UP000000530; 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_0000075959"
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; 36682 MW; A483404D1D240230 CRC64;
MTKIMFFGTR DYEKEMALNW GKKNNVEVTT SKELLSSATV DQLKDYDGVT TMQFGKLEND
VYPKLESYGI KQIAQRTAGF DMYDLDLAKK HNIVISNVPS YSPETIAEYS VSIALQLVRR
FPDIERRVQA HDFTWQAEIM SKPVKNMTVA IIGTGRIGAA TAKIYAGFGA TITAYDAYPN
KDLDFLTYKD SVKEAIKDAD IISLHVPANK ESYHLFDKAM FDHVKKGAIL VNAARGAVIN
TPDLIAAVND GTLLGAAIDT YENEAAYFTN DWTNKDIDDK TLLELIEHER ILVTPHIAFF
SDEAVQNLVE GGLNAALSVI NTGTCETRLN