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 25-NOV-2008, entry version 32. DE RecName: Full=D-lactate dehydrogenase; DE Short=D-LDH; DE EC=1.1.1.28; DE AltName: Full=D-specific D-2-hydroxyacid dehydrogenase; GN Name=ldhD; Synonyms=ddh; OrderedLocusNames=SACOL2535; OS Staphylococcus aureus (strain COL). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=93062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC -!- CATALYTIC ACTIVITY: (R)-lactate + NAD(+) = pyruvate + NADH. CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000046; AAW37312.1; -; Genomic_DNA. DR RefSeq; YP_187328.1; -. DR GeneID; 3238242; -. DR GenomeReviews; CP000046_GR; SACOL2535. DR KEGG; sac:SACOL2535; -. DR TIGR; SACOL2535; -. DR HOGENOM; Q5HD29; -. DR BioCyc; SAUR93062:SACOL2535-MON; -. DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR006139; D-isomer_2_OHA_DHase. DR InterPro; IPR006140; D-isomer_2_OHA_DHase_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 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 Complete proteome; NAD; Oxidoreductase. FT CHAIN 1 330 D-lactate dehydrogenase. FT /FTId=PRO_0000075959. FT ACT_SITE 235 235 By similarity. FT ACT_SITE 264 264 By similarity. FT ACT_SITE 296 296 Proton donor (By similarity). 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 //