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Database: UniProt
Entry: Q8CN22
LinkDB: Q8CN22
Original site: Q8CN22 
ID   LDHD_STAES              Reviewed;         330 AA.
AC   Q8CN22;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   05-DEC-2018, entry version 99.
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=SE_2074;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05716.1; -; Genomic_DNA.
DR   RefSeq; NP_765629.1; NC_004461.1.
DR   RefSeq; WP_002456690.1; NC_004461.1.
DR   ProteinModelPortal; Q8CN22; -.
DR   SMR; Q8CN22; -.
DR   STRING; 176280.SE2074; -.
DR   EnsemblBacteria; AAO05716; AAO05716; SE_2074.
DR   GeneID; 1057713; -.
DR   KEGG; sep:SE2074; -.
DR   PATRIC; fig|176280.10.peg.2026; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   KO; K03778; -.
DR   OMA; IAFYTNT; -.
DR   BioCyc; SEPI176280:G1G05-2133-MONOMER; -.
DR   Proteomes; UP000001411; 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   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    330       D-lactate dehydrogenase.
FT                                /FTId=PRO_0000075966.
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;  36526 MW;  E49590DB57226722 CRC64;
     MTKIMFFGTR AYEKDMALRW GKKNNIDVTT STELLSVDTV DQLKDYDGVT TMQFGKLEPE
     VYPKLESYGI KQIAQRTAGF DMYDLELAKK HEIIISNIPS YSPETIAEYS VSIALQLVRK
     FPTIEKRVQA HNFTWASPIM SRPVKNMTVA IIGTGRIGAA TGKIYAGFGA RVVGYDAYPN
     HSLSFLEYKE TVEDAIKDAD IISLHVPANK DSFHLFDNNM FKNVKKGAVL VNAARGAVIN
     TPDLIEAVNN GTLSGAAIDT YENEANYFTF DCSNQTIDDP ILLDLIRNEN ILVTPHIAFF
     SDEAVQNLVE GGLNAALSVI NTGTCDTRLN
//
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