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Database: UniProt
Entry: Q59642
LinkDB: Q59642
Original site: Q59642 
ID   LDHD_PEDAC              Reviewed;         331 AA.
AC   Q59642;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   05-DEC-2018, entry version 85.
DE   RecName: Full=D-lactate/D-glycerate dehydrogenase {ECO:0000305};
DE            Short=D-LDH/GDH {ECO:0000305};
DE            EC=1.1.1.28 {ECO:0000269|PubMed:7539419};
DE            EC=1.1.1.29 {ECO:0000269|PubMed:7539419};
DE   AltName: Full=D-specific 2-hydroxyacid dehydrogenase {ECO:0000305};
GN   Name=ldhD {ECO:0000303|PubMed:7539419};
OS   Pediococcus acidilactici.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus; Pediococcus acidilactici group.
OX   NCBI_TaxID=1254;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DG302;
RX   PubMed=7539419; DOI=10.1128/jb.177.12.3427-3437.1995;
RA   Garmyn D., Ferain T., Bernard N., Hols P., Delplace B., Delcour J.;
RT   "Pediococcus acidilactici ldhD gene: cloning, nucleotide sequence, and
RT   transcriptional analysis.";
RL   J. Bacteriol. 177:3427-3437(1995).
CC   -!- FUNCTION: Has both D-lactate and D-glycerate dehydrogenase
CC       activities. Equally active on pyruvate and hydroxypyruvate.
CC       {ECO:0000269|PubMed:7539419}.
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; Evidence={ECO:0000269|PubMed:7539419};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC         Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.29; Evidence={ECO:0000269|PubMed:7539419};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26297}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; X70925; CAA50275.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q59642; -.
DR   SMR; Q59642; -.
DR   PRIDE; Q59642; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008465; F:glycerate 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    331       D-lactate/D-glycerate dehydrogenase.
FT                                /FTId=PRO_0000075958.
FT   NP_BIND     154    155       NAD. {ECO:0000250|UniProtKB:P30901}.
FT   NP_BIND     205    206       NAD. {ECO:0000250|UniProtKB:P30901}.
FT   NP_BIND     232    234       NAD. {ECO:0000250|UniProtKB:P30901}.
FT   ACT_SITE    234    234       {ECO:0000250|UniProtKB:P26297}.
FT   ACT_SITE    263    263       {ECO:0000250|UniProtKB:P26297}.
FT   ACT_SITE    295    295       Proton donor.
FT                                {ECO:0000250|UniProtKB:P26297}.
FT   BINDING     174    174       NAD. {ECO:0000250|UniProtKB:P26297}.
FT   BINDING     211    211       NAD. {ECO:0000250|UniProtKB:P30901}.
FT   BINDING     258    258       NAD. {ECO:0000250|UniProtKB:P30901}.
SQ   SEQUENCE   331 AA;  37210 MW;  C2E6653EC661AEB8 CRC64;
     MKIIAYGIRD DEKPYLDEWV TKNHIEVKAV PDLLDSSNID LAKDYDGVVA YQQKPYTADL
     FDKMHEFGIH AFSLRNVGLD NVPADALKKN DIKISNVPAY SPRAIAELSV TQLLALLRKI
     PEFEYKMAHG DYRWEPDIGL ELNQMTVGVI GTGRIGRAAI DIFKPFGAKV IAYDVFRNPA
     LEKEGMYVDT LEELYQQANV ITLHVPALKD NYHMLDEKAF GQMQDGTFIL NFARGTLVDT
     PALLKALDSG KVAGAALDTY ENEVGIFDVD HGDQPIDDPV FNDLMSRRNV MITPHAAFYT
     RPAVKNMVQI ALDNNRDLIE KNSSKNEVKF E
//
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