ID LDHD_STAAR Reviewed; 330 AA. AC Q6GDS2; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 04-NOV-2008, entry version 33. 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=SAR2605; OS Staphylococcus aureus (strain MRSA252). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=282458; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15213324; DOI=10.1073/pnas.0402521101; RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., RA Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., RA Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., RA James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., RA Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., RA Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., RA Spratt B.G., Parkhill J.; RT "Complete genomes of two clinical Staphylococcus aureus strains: RT evidence for the rapid evolution of virulence and drug resistance."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004). 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; BX571856; CAG41584.1; -; Genomic_DNA. DR RefSeq; YP_041951.1; -. DR GeneID; 2859266; -. DR GenomeReviews; BX571856_GR; SAR2605. DR KEGG; sar:SAR2605; -. DR HOGENOM; Q6GDS2; -. DR BioCyc; SAUR282458:SAR2605-MON; -. DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:EC. 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_0000075962. 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; 36756 MW; 4B36154D1B8EAE27 CRC64; MTKIMFFGTR DYEKEMALNW GKKNNVEVTT SKELLSSATV DQLKDYDGVT TMQFGKLEND VYPKLESYGI KQIAQRTAGF DMYDLDLAKK HNIVISNVPS YSPETIAEYS VSIALQLVRR FPDIERRVQA HDFTWQAEIM SKPVKNMTVA IIGTGRIGAA TAKIYAGFGA TITAYDAYPN KDLDFLTYKD SVKEAIKDAD IISLHVPANK ESYHLFDKTM FDHVKKGAIL VNAARGAVIN TPDLIDAVND GTLLGAAIDT YENEAAYFTN DWTNKDIDDK TLLELIEHER ILVTPHIAFF SDEAVQNLVE GGLNAALSVI NTGTCETRLN //