GenomeNet

Database: UniProt
Entry: P99116
LinkDB: P99116
Original site: P99116 
ID   LDHD_STAAN              Reviewed;         330 AA.
AC   P99116; Q99RB1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   05-DEC-2018, entry version 87.
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=SA2312;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA   Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=N315;
RX   PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA   Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA   Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D.,
RA   Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F.,
RA   Schrenzel J.;
RT   "Correlation of proteomic and transcriptomic profiles of
RT   Staphylococcus aureus during the post-exponential phase of growth.";
RL   J. Microbiol. Methods 60:247-257(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of
RT   S. aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB43615.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BA000018; BAB43615.1; ALT_INIT; Genomic_DNA.
DR   PIR; E90056; E90056.
DR   RefSeq; WP_000161545.1; NC_002745.2.
DR   ProteinModelPortal; P99116; -.
DR   SMR; P99116; -.
DR   SWISS-2DPAGE; P99116; -.
DR   EnsemblBacteria; BAB43615; BAB43615; BAB43615.
DR   KEGG; sau:SA2312; -.
DR   HOGENOM; HOG000136695; -.
DR   KO; K03778; -.
DR   BioCyc; SAUR158879:G1G21-2692-MONOMER; -.
DR   Proteomes; UP000000751; 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   1: Evidence at protein level;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    330       D-lactate dehydrogenase.
FT                                /FTId=PRO_0000075961.
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;  36712 MW;  AE23FA56A784B320 CRC64;
     MTKIMFFGTR DYEKEMALNW GKKNNVEVTT SKELLSSATV DQLKDYDGVT TMQFGKLEND
     VYPKLESYGI KQIAQRTAGF DMYDLDLAKK HNIVISNVPS YSPETIAEYS VSIALQLVRR
     FPDIERRVQT HDFTWQAEIM SKPVKNMTVA IIGTGRIGAA TAKIYAGFGA TITAYDAYPN
     KDLDFLTYKD SVKEAIKDAD IISLHVPANK ESYHLFDKAM FDHVKKGAIL VNAARGAVIN
     TPDLIAAVND GTLLGAAIDT YENEAAYFTN DWTNKDIDDK TLLELIEHER ILVTPHIAFF
     SDEAVQNLVE GGLNAALSVI NTGTCETRLN
//
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