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Database: UniProt
Entry: Q99ZM2
LinkDB: Q99ZM2
Original site: Q99ZM2 
ID   LDHD_STRP1              Reviewed;         330 AA.
AC   Q99ZM2; Q48YR4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   13-FEB-2019, entry version 117.
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=SPy_1170, M5005_Spy0890;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J.,
RA   Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J.,
RA   Hoe N.P., Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of
RT   serotype M1 group A Streptococcus involved multiple horizontal gene
RT   transfer events.";
RL   J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK34037.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51508.1; -; Genomic_DNA.
DR   RefSeq; NP_269316.1; NC_002737.2.
DR   ProteinModelPortal; Q99ZM2; -.
DR   SMR; Q99ZM2; -.
DR   STRING; 160490.SPy_1170; -.
DR   PaxDb; Q99ZM2; -.
DR   EnsemblBacteria; AAK34037; AAK34037; SPy_1170.
DR   EnsemblBacteria; AAZ51508; AAZ51508; M5005_Spy0890.
DR   GeneID; 901282; -.
DR   KEGG; spy:SPy_1170; -.
DR   KEGG; spz:M5005_Spy0890; -.
DR   PATRIC; fig|160490.10.peg.1021; -.
DR   eggNOG; ENOG4107RBM; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136695; -.
DR   KO; K03778; -.
DR   Proteomes; UP000000750; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    330       D-lactate dehydrogenase.
FT                                /FTId=PRO_0000075970.
FT   NP_BIND     155    156       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     175    175       NAD. {ECO:0000250|UniProtKB:P26297}.
FT   BINDING     212    212       NAD. {ECO:0000250|UniProtKB:P30901}.
FT   BINDING     259    259       NAD. {ECO:0000250|UniProtKB:P30901}.
SQ   SEQUENCE   330 AA;  36126 MW;  34897A432723B092 CRC64;
     MKLKLYNVRG EEAVLAKKWA DDNGIEISLT ESPLTPETVK EAEGFDGIAN AQIGPLDDAI
     YPLLKEMGIK QIAQHSASVD MYNLDLATEN DIIITNVPSY SPESIAEFTV TIVLNLIRHV
     ELIRENVKKQ NFTWGLPIRG RVLGDMTVAI IGTGRIGLAT AKIFKGFGCK VVGYDIYQSD
     AAKAVLDYKE SVEEAIKDAD LVSLHMPPTA ENTHLFNSDL FKSFKKGAIL MNMARGAVIE
     TQDLLDALDA GLLSGAGIDT YEFEGPYIPK NFEGQEITDS LFKALINHPK VIYTPHAAYY
     TDEAVKNLVE GALNATVEII KTGTTTTRVN
//
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