ID Q96569_SOLLC Unreviewed; 350 AA.
AC Q96569;
DT 01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT 01-FEB-1997, sequence version 1.
DT 24-JAN-2024, entry version 163.
DE RecName: Full=L-lactate dehydrogenase {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|RuleBase:RU000496};
DE EC=1.1.1.27 {ECO:0000256|ARBA:ARBA00012967, ECO:0000256|RuleBase:RU000496};
GN Name=ldh {ECO:0000313|EMBL:CAA70100.1};
GN Synonyms=101252012 {ECO:0000313|EnsemblPlants:Solyc08g078850.3.1},
GN ldh1 {ECO:0000313|EMBL:CAA71611.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EMBL:CAA70100.1};
RN [1] {ECO:0000313|EMBL:CAA70100.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9426593; DOI=10.1023/A:1005854002969;
RA Germain V., Raymond P., Ricard B.;
RT "Differential expression of two tomato lactate dehydrogenase genes in
RT response to oxygen deficit.";
RL Plant Mol. Biol. 35:711-721(1997).
RN [2] {ECO:0000313|EMBL:CAA71611.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Fruit {ECO:0000313|EMBL:CAA71611.1};
RX PubMed=9426613; DOI=10.1023/A:1005821304013;
RA Germain V., Ricard B.;
RT "Two ldh genes from tomato and their expression in different organs, during
RT fruit ripening and in response to stress.";
RL Plant Mol. Biol. 35:949-954(1997).
RN [3] {ECO:0000313|EnsemblPlants:Solyc08g078850.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc08g078850.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [4] {ECO:0000313|EnsemblPlants:Solyc08g078850.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc08g078850.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
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:0000256|ARBA:ARBA00001763,
CC ECO:0000256|RuleBase:RU000496};
CC -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate
CC from pyruvate: step 1/1. {ECO:0000256|ARBA:ARBA00004843,
CC ECO:0000256|RuleBase:RU000496}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC {ECO:0000256|ARBA:ARBA00006054}.
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DR EMBL; Y08887; CAA70100.1; -; mRNA.
DR EMBL; Y10602; CAA71611.1; -; Genomic_DNA.
DR PIR; T07061; T07061.
DR RefSeq; NP_001266265.1; NM_001279336.1.
DR AlphaFoldDB; Q96569; -.
DR STRING; 4081.Q96569; -.
DR PaxDb; 4081-Solyc08g078850-2-1; -.
DR EnsemblPlants; Solyc08g078850.3.1; Solyc08g078850.3.1; Solyc08g078850.3.
DR GeneID; 101252012; -.
DR Gramene; Solyc08g078850.3.1; Solyc08g078850.3.1; Solyc08g078850.3.
DR KEGG; sly:101252012; -.
DR eggNOG; KOG1495; Eukaryota.
DR HOGENOM; CLU_045401_0_2_1; -.
DR InParanoid; Q96569; -.
DR OMA; ASCAEYI; -.
DR OrthoDB; 5344346at2759; -.
DR UniPathway; UPA00554; UER00611.
DR Proteomes; UP000004994; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006089; P:lactate metabolic process; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR CDD; cd05293; LDH_1; 1.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01771; L-LDH-NAD; 1.
DR PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
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; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00064; L_LDH; 1.
PE 2: Evidence at transcript level;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000496};
KW Reference proteome {ECO:0000313|Proteomes:UP000004994}.
FT DOMAIN 38..177
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 180..343
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 44..49
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 153..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 350 AA; 37708 MW; 3957C1D4FB04D70F CRC64;
MQNSSSSSSL GPGGLDLTQA FFKSISNAAP PSPTKRHTKI SVIGVGNVGM AIAQTILTQD
LVDELALVDA KSDKLRGEML DLQHAAAFLP RTKIHASIDY SVTAGSDLCI VTAGARQNPG
ESRLNLLQRN MALFRSIIPP LVKYSPETTL LVVSNPVDVL TYVAWKLSGF PANRVIGSGT
NLDSSRFRFL IADHLDVNAQ DVQAYIVGEH GDSSVALWSG ISVGGVPVLS FLERQQIALE
KETLEKIHQE VVHSAYEVIS LKGYTSWAIG YSVANLARTI LRDQRRIHPV SVLAKGFYGI
DGGDVFLSLP AQLGRSGVLG VTNVHLTDEE IEQLRNSAKT ILEVQSQLGI
//