LDH_CAEEL
ID LDH_CAEEL Reviewed; 333 AA.
AC Q27888;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=L-lactate dehydrogenase;
DE Short=LDH;
DE EC=1.1.1.27;
GN Name=ldh-1; ORFNames=F13D12.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7999079; DOI=10.1006/bbrc.1994.2701;
RA Tsoi S.C.-M., Li S.S.-L.;
RT "The nucleotide and deduced amino-acid sequences of a cDNA encoding lactate
RT dehydrogenase from Caenorhabditis elegans: the evolutionary relationships
RT of lactate dehydrogenases from mammals, birds, amphibian, fish, nematode,
RT plants, bacteria, mycoplasma, and plasmodium.";
RL Biochem. Biophys. Res. Commun. 205:558-564(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8747535;
RA Mannen H., Li S.S.-L.;
RT "The lactate dehydrogenase gene from nematode Caenorhabditis elegans
RT contains only two of six introns conserved in the protein-encoding sequence
RT of LDH genes from bird and mammals.";
RL Biochem. Mol. Biol. Int. 37:1057-1061(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000305}.
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DR EMBL; U15420; AAA67063.1; -; mRNA.
DR EMBL; L43563; AAC41613.1; -; Genomic_DNA.
DR EMBL; Z49127; CAA88944.1; -; Genomic_DNA.
DR PIR; JC2432; JC2432.
DR RefSeq; NP_496503.1; NM_064102.5.
DR AlphaFoldDB; Q27888; -.
DR SMR; Q27888; -.
DR BioGRID; 40103; 27.
DR IntAct; Q27888; 1.
DR STRING; 6239.F13D12.2; -.
DR EPD; Q27888; -.
DR PaxDb; Q27888; -.
DR PeptideAtlas; Q27888; -.
DR EnsemblMetazoa; F13D12.2a.1; F13D12.2a.1; WBGene00002262.
DR GeneID; 174798; -.
DR UCSC; F13D12.2; c. elegans.
DR CTD; 174798; -.
DR WormBase; F13D12.2a; CE02181; WBGene00002262; ldh-1.
DR eggNOG; KOG1495; Eukaryota.
DR GeneTree; ENSGT00940000164122; -.
DR HOGENOM; CLU_045401_0_2_1; -.
DR InParanoid; Q27888; -.
DR OMA; AFTRHCT; -.
DR PhylomeDB; Q27888; -.
DR Reactome; R-CEL-70268; Pyruvate metabolism.
DR UniPathway; UPA00554; UER00611.
DR PRO; PR:Q27888; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002262; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q27888; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..333
FT /note="L-lactate dehydrogenase"
FT /id="PRO_0000168493"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 29..57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 36065 MW; B9CA8A6BB0E84007 CRC64;
MASTIKEVFA EIAAPVENSH GKVTVVGVGQ VGMACAYSIL QQNLANELCL VDVVADKLKG
EMMDLQHGLA FTRHCTVKAD TDYSITAGSK LCVVTAGARQ REGETRLSLV QRNVEIFKGI
IPQLVKYSPD TCILVVSNPV DVLTYVTWKL SGLPRERVFG SGTNLDSARF RFLLSEKLNI
APSSCHGWII GEHGDSSVAV WSGVNVAGVT LHEIKPDIGE KTDNEHWEAE IHKKVVDSAY
EIIKLKGYTS WAIGLSVAKI AQGIFSNSRN VFALSTNVKG FHGINDDVYL SLPVVLGSAG
LTHVVKQQLT EAEVQKLHNS AKALLEVQNG IVM
