LDHD_STRA3
ID LDHD_STRA3 Reviewed; 330 AA.
AC Q8E6A9;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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; OrderedLocusNames=gbs0668;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(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}.
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DR EMBL; AL766846; CAD46312.1; -; Genomic_DNA.
DR RefSeq; WP_000770077.1; NC_004368.1.
DR AlphaFoldDB; Q8E6A9; -.
DR SMR; Q8E6A9; -.
DR STRING; 211110.gbs0668; -.
DR EnsemblBacteria; CAD46312; CAD46312; CAD46312.
DR KEGG; san:gbs0668; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_9; -.
DR OMA; IAFYTNT; -.
DR Proteomes; UP000000823; 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.
FT CHAIN 1..330
FT /note="D-lactate dehydrogenase"
FT /id="PRO_0000075968"
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; 36501 MW; 1E639C912B4A46B5 CRC64;
MKLKVFNVRE EEATLAQDWA NRNHVELSMS EGPLTLETVN EVEGFDGIAN AQIGPLDDAI
YPLLKEMGIK QIAQRSAGVD MYNLELAKQH GIIISNVPSY SPESIAEFTV TIALNLIRKV
ELIRANVREQ NFSWTLPIRG RVLGNMTVAI IGTGRIGLAT AKIFKGFGCR VIGYDIYHNP
MADGILEYVN SVEEAVEKAD LVSLHMPPTA ENTHLFNLDM FKQFKKGAIL MNMARGALVE
TKDLLEALDQ GLLEGAGIDT YEFEGPYIPK NCQGQDISDK DFLRLINHPK VIYTPHAAYY
TDEAVKNLVE GALNACVEVV ETGTTTTRVN
