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Database: UniProt
Entry: P26298
LinkDB: P26298
Original site: P26298 
ID   LDHD_LACPE              Reviewed;         332 AA.
AC   P26298;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   05-DEC-2018, entry version 88.
DE   RecName: Full=D-lactate dehydrogenase;
DE            Short=D-LDH;
DE            EC=1.1.1.28;
DE   AltName: Full=D-specific 2-hydroxyacid dehydrogenase;
OS   Lactobacillus pentosus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8041 / DSM 20314 / JCM 1558 / NCDO 363 / NCIMB 8026;
RX   PubMed=1840590;
RA   Ohta T., Taguchi H.;
RT   "D-lactate dehydrogenase is a member of the D-isomer-specific 2-
RT   hydroxyacid dehydrogenase family. Cloning, sequencing, and expression
RT   in Escherichia coli of the D-lactate dehydrogenase gene of
RT   Lactobacillus plantarum.";
RL   J. Biol. Chem. 266:12588-12594(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=8740366; DOI=10.1016/S0969-2126(96)00049-4;
RA   Stoll V.S., Kimber M.S., Pai E.F.;
RT   "Insights into substrate binding by D-2-ketoacid dehydrogenases from
RT   the structure of Lactobacillus pentosus D-lactate dehydrogenase.";
RL   Structure 4:437-447(1996).
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   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: Also active on D-glycerate.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from L.plantarum.
CC       {ECO:0000305|PubMed:1840590}.
DR   EMBL; D90339; BAA14352.1; -; Genomic_DNA.
DR   PIR; A40885; A40885.
DR   ProteinModelPortal; P26298; -.
DR   SMR; P26298; -.
DR   PRIDE; P26298; -.
DR   SABIO-RK; P26298; -.
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   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    332       D-lactate dehydrogenase.
FT                                /FTId=PRO_0000075956.
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}.
SQ   SEQUENCE   332 AA;  37183 MW;  FA63723C63B53EBE CRC64;
     MKIIAYAVRD DERPFFDTWM KENPDVEVKL VPELLTEDNV DLAKGFDGAD VYQQKDYTAE
     VLNKLADEGV KNISLRNVGV DNLDVPTVKA RGLNISNVPA YSPNAIAELS VTQLMQLLRQ
     TPMFNKKLAK QDFRWAPDIA KELNTMTVGV IGTGRIGRAA IDIFKGFGAK VIGYDVYRNA
     ELEKEGMYVD TLDELYAQAD VITLHVPALK DNYHMLNADA FSKMKDGAYI LNFARGTLID
     SEDLIKALDS GKVAGAALVT YEYETKIFNK DLEGQTIDDK VFMNLFNRDN VLITPHTAFY
     TETAVHNMVH VSMNSNKQFI ETGKADTQVK FD
//
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