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Database: UniProt
Entry: Q6GDS2
LinkDB: Q6GDS2
Original site: Q6GDS2 
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   16-JAN-2019, entry version 88.
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=SAR2605;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
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:
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;
CC         EC=1.1.1.28;
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; BX571856; CAG41584.1; -; Genomic_DNA.
DR   RefSeq; WP_000161541.1; NC_002952.2.
DR   ProteinModelPortal; Q6GDS2; -.
DR   SMR; Q6GDS2; -.
DR   EnsemblBacteria; CAG41584; CAG41584; SAR2605.
DR   KEGG; sar:SAR2605; -.
DR   HOGENOM; HOG000136695; -.
DR   KO; K03778; -.
DR   OMA; IAFYTNT; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; SAUR282458:G1G3O-2831-MONOMER; -.
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       D-lactate dehydrogenase.
FT                                /FTId=PRO_0000075962.
FT   NP_BIND     156    157       NAD. {ECO:0000250|UniProtKB:P30901}.
FT   NP_BIND     206    207       NAD. {ECO:0000250|UniProtKB:P30901}.
FT   NP_BIND     233    235       NAD. {ECO:0000250|UniProtKB:P30901}.
FT   ACT_SITE    235    235       {ECO:0000250|UniProtKB:P26297}.
FT   ACT_SITE    264    264       {ECO:0000250|UniProtKB:P26297}.
FT   ACT_SITE    296    296       Proton donor.
FT                                {ECO:0000250|UniProtKB:P26297}.
FT   BINDING     176    176       NAD. {ECO:0000250|UniProtKB:P26297}.
FT   BINDING     259    259       NAD. {ECO:0000250|UniProtKB:P30901}.
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
//
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