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Database: UniProt
Entry: P52643
LinkDB: P52643
Original site: P52643 
ID   LDHD_ECOLI              Reviewed;         329 AA.
AC   P52643; P78152;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   13-FEB-2019, entry version 143.
DE   RecName: Full=D-lactate dehydrogenase;
DE            Short=D-LDH;
DE            EC=1.1.1.28;
DE   AltName: Full=Fermentative lactate dehydrogenase;
GN   Name=ldhA; Synonyms=hslI, htpH; OrderedLocusNames=b1380, JW1375;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=9025293; DOI=10.1099/00221287-143-1-187;
RA   Bunch P.K., Mat-Jan F., Lee N., Clark D.P.;
RT   "The ldhA gene encoding the fermentative lactate dehydrogenase of
RT   Escherichia coli.";
RL   Microbiology 143:187-195(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   CHARACTERIZATION AS AN HEAT-SHOCK GENE.
RX   PubMed=8349564; DOI=10.1128/jb.175.16.5242-5252.1993;
RA   Chuang S.E., Blattner F.R.;
RT   "Characterization of twenty-six new heat shock genes of Escherichia
RT   coli.";
RL   J. Bacteriol. 175:5242-5252(1993).
RN   [6]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA   Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
CC   -!- FUNCTION: Fermentative lactate dehydrogenase.
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   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; U36928; AAB51772.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74462.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA14990.1; -; Genomic_DNA.
DR   PIR; G64888; G64888.
DR   RefSeq; NP_415898.1; NC_000913.3.
DR   RefSeq; WP_000762236.1; NZ_LN832404.1.
DR   ProteinModelPortal; P52643; -.
DR   SMR; P52643; -.
DR   BioGrid; 4259502; 26.
DR   DIP; DIP-10087N; -.
DR   IntAct; P52643; 4.
DR   STRING; 316385.ECDH10B_1505; -.
DR   EPD; P52643; -.
DR   jPOST; P52643; -.
DR   PaxDb; P52643; -.
DR   PRIDE; P52643; -.
DR   EnsemblBacteria; AAC74462; AAC74462; b1380.
DR   EnsemblBacteria; BAA14990; BAA14990; BAA14990.
DR   GeneID; 946315; -.
DR   KEGG; ecj:JW1375; -.
DR   KEGG; eco:b1380; -.
DR   PATRIC; fig|1411691.4.peg.892; -.
DR   EchoBASE; EB2978; -.
DR   EcoGene; EG13186; ldhA.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136695; -.
DR   InParanoid; P52643; -.
DR   KO; K03778; -.
DR   PhylomeDB; P52643; -.
DR   BioCyc; EcoCyc:DLACTDEHYDROGNAD-MONOMER; -.
DR   BioCyc; ECOL316407:JW1375-MONOMER; -.
DR   BioCyc; MetaCyc:DLACTDEHYDROGNAD-MONOMER; -.
DR   PRO; PR:P52643; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008720; F:D-lactate dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0070404; F:NADH binding; IDA:EcoliWiki.
DR   GO; GO:0019664; P:mixed acid fermentation; IDA:EcoCyc.
DR   GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
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   Complete proteome; NAD; Oxidoreductase; Reference proteome;
KW   Stress response.
FT   CHAIN         1    329       D-lactate dehydrogenase.
FT                                /FTId=PRO_0000075952.
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   329 AA;  36535 MW;  EF85419988438D6D CRC64;
     MKLAVYSTKQ YDKKYLQQVN ESFGFELEFF DFLLTEKTAK TANGCEAVCI FVNDDGSRPV
     LEELKKHGVK YIALRCAGFN NVDLDAAKEL GLKVVRVPAY DPEAVAEHAI GMMMTLNRRI
     HRAYQRTRDA NFSLEGLTGF TMYGKTAGVI GTGKIGVAML RILKGFGMRL LAFDPYPSAA
     ALELGVEYVD LPTLFSESDV ISLHCPLTPE NYHLLNEAAF EQMKNGVMIV NTSRGALIDS
     QAAIEALKNQ KIGSLGMDVY ENERDLFFED KSNDVIQDDV FRRLSACHNV LFTGHQAFLT
     AEALTSISQT TLQNLSNLEK GETCPNELV
//
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