ID   LDHD_STRA5              Reviewed;         330 AA.
AC   Q8E0N5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=D-lactate dehydrogenase;
DE            Short=D-LDH;
DE            EC=1.1.1.28;
DE   AltName: Full=D-specific D-2-hydroxyacid dehydrogenase;
GN   Name=ldhD; Synonyms=ldhA; OrderedLocusNames=SAG0695;
OS   Streptococcus agalactiae serotype V.
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=216466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R / Serotype V;
RX   MEDLINE=22222988; PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R.,
RA   Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S.,
RA   Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M.,
RA   Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D.,
RA   Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an
RT   emerging human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC   -!- CATALYTIC ACTIVITY: (R)-lactate + NAD(+) = pyruvate + NADH.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family.
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DR   EMBL; AE009948; AAM99582.1; -; Genomic_DNA.
DR   RefSeq; NP_687710.1; -.
DR   HSSP; P17584; 1DXY.
DR   GeneID; 1013499; -.
DR   GenomeReviews; AE009948_GR; SAG0695.
DR   KEGG; sag:SAG0695; -.
DR   TIGR; SAG0695; -.
DR   HOGENOM; Q8E0N5; -.
DR   OMA; Q8E0N5; KWGERAS.
DR   GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH.
DR   InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG.
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_0000075969.
FT   ACT_SITE    235    235       By similarity.
FT   ACT_SITE    264    264       By similarity.
FT   ACT_SITE    296    296       Proton donor (By similarity).
SQ   SEQUENCE   330 AA;  36560 MW;  1F1589D42E3C9BF5 CRC64;
     MKLKVFNVRE EEATLAQDWA NRNHVELSMS EGPLTLETVN EVEGFDGIAN AQIEPLDDAI
     YPLLKEMGIK QIAQRSAGVD MYNLELAKQH GIIISNVPSY SPESIAEFTV TIALNLIRKV
     ELIRANVREQ NFSWTLPIRG RVLGNMTVAI IGTGRIGLAT AKIFKGFGCR VIGYDIYHNP
     MADGILEYVN SVEEAVEEAD LVSLHMPPTA ENTHLFNLDM FKQFKKGAIL MNMARGALVE
     TKDLLEALDQ GLLEGAGIDT YEFEGPYIPK NCQGQDISDK DFLRLINHPK VIYTPHAAYY
     TDEAVKNLVE GALNACVEVI ETGTTTTKVN
//