LDHD_ECOLI
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 03-AUG-2022, entry version 161.
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., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CHARACTERIZATION AS A 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 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., 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; 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; 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_SSZK01000012.1.
DR PDB; 5Z1Z; X-ray; 1.97 A; A/B/C/D=1-329.
DR PDBsum; 5Z1Z; -.
DR AlphaFoldDB; P52643; -.
DR SMR; P52643; -.
DR BioGRID; 4259502; 26.
DR DIP; DIP-10087N; -.
DR IntAct; P52643; 4.
DR STRING; 511145.b1380; -.
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 eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_6; -.
DR InParanoid; P52643; -.
DR OMA; VIVTAHQ; -.
DR PhylomeDB; P52643; -.
DR BioCyc; EcoCyc:DLACTDEHYDROGNAD-MON; -.
DR BioCyc; MetaCyc:DLACTDEHYDROGNAD-MON; -.
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 3D-structure; NAD; Oxidoreductase; Reference proteome; Stress response.
FT CHAIN 1..329
FT /note="D-lactate dehydrogenase"
FT /id="PRO_0000075952"
FT ACT_SITE 234
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 263
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT ACT_SITE 295
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 154..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P26297"
FT BINDING 205..206
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT BINDING 232..234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT BINDING 258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P30901"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT HELIX 301..319
FT /evidence="ECO:0007829|PDB:5Z1Z"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:5Z1Z"
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
