LDH_DEIRA
ID LDH_DEIRA Reviewed; 304 AA.
AC P50933; O32512;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:8654970};
DE Short=L-LDH {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:8654970};
DE EC=1.1.1.27 {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781};
DE AltName: Full=2-ketoacid:NAD-dependent dehydrogenase {ECO:0000303|PubMed:17936781};
GN Name=ldh {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000303|PubMed:8654970};
GN OrderedLocusNames=DR_2364;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=8654970; DOI=10.1016/0378-1119(96)00108-4;
RA Narumi I., Watanabe H.;
RT "Sequence analysis of the L-lactate dehydrogenase-encoding gene of
RT Deinococcus radiodurans, a suitable mesophilic counterpart for Thermus.";
RL Gene 172:117-119(1996).
RN [2]
RP SEQUENCE REVISION TO 270 AND 277.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RA Narumi I., Watanabe H.;
RT "Revised nucleotide sequence of the Deinococcus radiodurans L-lactate
RT dehydrogenase gene and the gene expression in Escherichia coli.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17936781; DOI=10.1016/j.jmb.2007.09.049;
RA Coquelle N., Fioravanti E., Weik M., Vellieux F., Madern D.;
RT "Activity, stability and structural studies of lactate dehydrogenases
RT adapted to extreme thermal environments.";
RL J. Mol. Biol. 374:547-562(2007).
CC -!- FUNCTION: Catalyzes the conversion of lactate to pyruvate.
CC {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:17936781}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate;
CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00488,
CC ECO:0000269|PubMed:17936781};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 1,6-
CC bisphosphate (FBP). {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.21 mM for pyruvate {ECO:0000269|PubMed:17936781};
CC Note=kcat is 884 sec(-1) for pyruvate as substrate.
CC {ECO:0000269|PubMed:17936781};
CC Temperature dependence:
CC Optimum temperature is 48 degrees Celsius.
CC {ECO:0000269|PubMed:17936781};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00488,
CC ECO:0000269|PubMed:17936781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305}.
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DR EMBL; AB005539; BAA21471.1; -; Genomic_DNA.
DR EMBL; AE000513; AAF11912.1; -; Genomic_DNA.
DR PIR; E75282; E75282.
DR RefSeq; NP_296085.1; NC_001263.1.
DR RefSeq; WP_010888990.1; NZ_CP015081.1.
DR PDB; 2V6B; X-ray; 2.50 A; A/B/C/D=1-304.
DR PDBsum; 2V6B; -.
DR AlphaFoldDB; P50933; -.
DR SMR; P50933; -.
DR STRING; 243230.DR_2364; -.
DR EnsemblBacteria; AAF11912; AAF11912; DR_2364.
DR KEGG; dra:DR_2364; -.
DR PATRIC; fig|243230.17.peg.2598; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_1_1_0; -.
DR InParanoid; P50933; -.
DR OMA; CYIIVLT; -.
DR OrthoDB; 870724at2; -.
DR BRENDA; 1.1.1.27; 1856.
DR UniPathway; UPA00554; UER00611.
DR EvolutionaryTrace; P50933; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_00488; Lactate_dehydrog; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR011304; L-lactate_DH.
DR InterPro; IPR018177; L-lactate_DH_AS.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR PRINTS; PR00086; LLDHDRGNASE.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Cytoplasm; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..304
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000168341"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 76..77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 117..120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 143..146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 148
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 163
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00488"
FT CONFLICT 270
FT /note="Q -> R (in Ref. 2; BAA21471)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:2V6B"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:2V6B"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:2V6B"
FT HELIX 282..296
FT /evidence="ECO:0007829|PDB:2V6B"
SQ SEQUENCE 304 AA; 32164 MW; F4CF3298673010CD CRC64;
MKVGVVGTGF VGSTAAFALV LRGSCSELVL VDRDEDRAQA EAEDIAHAAP VSHGTRVWHG
GHSELADAQV VILTAGANQK PGESRLDLLE KNADIFRELV PQITRAAPDA VLLVTSNPVD
LLTDLATQLA PGQPVIGSGT VLDSARFRHL MAQHAGVDGT HAHGYVLGEH GDSEVLAWSS
AMVAGMPVAD FMQAQNLPWN EQVRAKIDEG TRNAAASIIE GKRATYYGIG AALARITEAV
LRDRRAVLTV SAPTPEYGVS LSLPRVVGRQ GVLSTLHPKL TGDEQQKLEQ SAGVLRGFKQ
QLGL
