GenomeNet

Database: UniProt
Entry: P72357
LinkDB: P72357
Original site: P72357 
ID   LDHD_STAAU              Reviewed;         330 AA.
AC   P72357;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   05-DEC-2018, entry version 101.
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;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   FUNCTION.
RC   STRAIN=523k;
RX   PubMed=8787900;
RA   Milewski W.M., Boyle-Vavra S., Moreira B., Ebert C.C., Daum R.S.;
RT   "Overproduction of a 37-kilodalton cytoplasmic protein homologous to
RT   NAD(+)-linked D-lactate dehydrogenase associated with vancomycin
RT   resistance in Staphylococcus aureus.";
RL   Antimicrob. Agents Chemother. 40:166-172(1996).
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; U31175; AAB17663.1; -; Genomic_DNA.
DR   RefSeq; WP_000161536.1; NZ_UHEH01000001.1.
DR   ProteinModelPortal; P72357; -.
DR   SMR; P72357; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
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   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN         1    330       D-lactate dehydrogenase.
FT                                /FTId=PRO_0000075964.
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;  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
//
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