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   03-AUG-2022, entry version 108.
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=ldhA; OrderedLocusNames=SAG0695;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   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., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; EC=1.1.1.28;
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009948; AAM99582.1; -; Genomic_DNA.
DR   RefSeq; NP_687710.1; NC_004116.1.
DR   RefSeq; WP_000770070.1; NC_004116.1.
DR   AlphaFoldDB; Q8E0N5; -.
DR   SMR; Q8E0N5; -.
DR   STRING; 208435.SAG0695; -.
DR   EnsemblBacteria; AAM99582; AAM99582; SAG0695.
DR   GeneID; 66885598; -.
DR   KEGG; sag:SAG0695; -.
DR   PATRIC; fig|208435.3.peg.701; -.
DR   HOGENOM; CLU_019796_1_1_9; -.
DR   OMA; EWGITIT; -.
DR   Proteomes; UP000000821; 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   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..330
FT                   /note="D-lactate dehydrogenase"
FT                   /id="PRO_0000075969"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   ACT_SITE        296
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         155..156
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P26297"
FT   BINDING         206..207
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         212
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         233..235
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
FT   BINDING         259
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P30901"
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