LDH1_YEAST
ID LDH1_YEAST Reviewed; 375 AA.
AC P38139; D6VQK2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Lipid droplet hydrolase 1 {ECO:0000303|PubMed:21478434};
DE EC=3.1.1.3 {ECO:0000269|PubMed:21478434};
DE AltName: Full=Lipid esterase {ECO:0000303|PubMed:21478434};
DE AltName: Full=Triacylglycerol lipase {ECO:0000303|PubMed:21478434};
GN Name=LDH1 {ECO:0000303|PubMed:21478434}; OrderedLocusNames=YBR204C;
GN ORFNames=YBR1444;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8368014; DOI=10.1002/yea.320090714;
RA Bussereau F., Mallet L., Gaillon L., Jacquet M.;
RT "A 12.8 kb segment, on the right arm of chromosome II from Saccharomyces
RT cerevisiae including part of the DUR1,2 gene, contains five putative new
RT genes.";
RL Yeast 9:797-806(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 63.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PREDICTION OF FUNCTION.
RX PubMed=14645503; DOI=10.1074/mcp.m300082-mcp200;
RA Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S.,
RA Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.;
RT "Synergistic computational and experimental proteomics approaches for more
RT accurate detection of active serine hydrolases in yeast.";
RL Mol. Cell. Proteomics 3:209-225(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=21478430; DOI=10.1128/ec.05038-11;
RA Thoms S., Debelyy M.O., Connerth M., Daum G., Erdmann R.;
RT "The putative yeast hydrolase Ldh1p is localized to Lipid droplets.";
RL Eukaryot. Cell 10:770-775(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP SER-177, AND DISRUPTION PHENOTYPE.
RX PubMed=21478434; DOI=10.1128/ec.05040-11;
RA Debelyy M.O., Thoms S., Connerth M., Daum G., Erdmann R.;
RT "Involvement of the yeast hydrolase Ldh1p in lipid homeostasis.";
RL Eukaryot. Cell 10:776-781(2011).
CC -!- FUNCTION: Serine hydrolase required for the maintenance of steady state
CC level of non-polar and polar lipids of lipid droplets and thus plays a
CC role in maintaining the lipids homeostasis (PubMed:21478434). Exhibits
CC both esterase and triacylglycerol lipase activity (PubMed:21478434).
CC {ECO:0000269|PubMed:21478434}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:21478434};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.77 uM for p-nitrophenyl butyrate (PNB)
CC {ECO:0000269|PubMed:21478434};
CC KM=3.3 mM for 1,2-dioleoyl-3-(pyren-1-yl)-decanoyl-rac-glycerol (DPG)
CC {ECO:0000269|PubMed:21478434};
CC Vmax=0.041 umol/min/mg enzyme for esterase activity using PNB as a
CC substrate {ECO:0000269|PubMed:21478434};
CC Vmax=1 umol/min/mg enzyme for triacylglycerol lipase activity using
CC DPG as a substrate {ECO:0000269|PubMed:21478434};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:21478430}.
CC -!- DISRUPTION PHENOTYPE: Leads to the appearance of giant lipid droplets
CC and an excessive accumulation of non-polar lipids and phospholipids
CC upon growth on medium containing oleic acid as a sole carbon source.
CC {ECO:0000269|PubMed:21478434}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; Z21487; CAA79692.1; -; Genomic_DNA.
DR EMBL; Z36073; CAA85168.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07322.2; -; Genomic_DNA.
DR PIR; S34927; S34927.
DR RefSeq; NP_009763.2; NM_001178552.2.
DR AlphaFoldDB; P38139; -.
DR BioGRID; 32901; 45.
DR DIP; DIP-4009N; -.
DR IntAct; P38139; 1.
DR STRING; 4932.YBR204C; -.
DR ESTHER; yeast-LDH1; AlphaBeta_hydrolase.
DR iPTMnet; P38139; -.
DR MaxQB; P38139; -.
DR PaxDb; P38139; -.
DR PRIDE; P38139; -.
DR EnsemblFungi; YBR204C_mRNA; YBR204C; YBR204C.
DR GeneID; 852503; -.
DR KEGG; sce:YBR204C; -.
DR SGD; S000000408; LDH1.
DR VEuPathDB; FungiDB:YBR204C; -.
DR eggNOG; ENOG502QVGS; Eukaryota.
DR GeneTree; ENSGT00940000176535; -.
DR HOGENOM; CLU_068926_0_0_1; -.
DR InParanoid; P38139; -.
DR OMA; YRKLWQF; -.
DR BioCyc; YEAST:YBR204C-MON; -.
DR Reactome; R-SCE-426048; Arachidonate production from DAG.
DR PRO; PR:P38139; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38139; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:SGD.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:SGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:SGD.
DR GO; GO:0046464; P:acylglycerol catabolic process; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..375
FT /note="Lipid droplet hydrolase 1"
FT /id="PRO_0000090373"
FT DOMAIN 88..358
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 373..375
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT MUTAGEN 177
FT /note="S->A: Abolishes serine hydrolase activity."
FT /evidence="ECO:0000269|PubMed:21478434"
FT CONFLICT 63
FT /note="V -> E (in Ref. 1; CAA79692 and 2; CAA85168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 43287 MW; CAE37B5107D79745 CRC64;
MNMAERAEAT KSWSCEPLSG KTLEEIVQNA ENAADLVAYI RKPEVDLDFR LKFIAEHEEF
FNVQLSDRNS RIRTCHNLSD KGIRGDTVFV FVPGLAGNLE QFEPLLELVD SDQKAFLTLD
LPGFGHSSEW SDYPMLKVVE LIFVLVCDVL RKWSTAVPNN DNVNPFNGHK IVLVGHSMGC
FLACHLYEQH MADTKAVQTL VLLTPPKAHI EQLSKDKHII QWALYGVFKL PWLFDVYRNK
FDQVKGLQSS GIKQYFYQQG DDVKLKYRKF WQFKNNISNK SRTIIGYLLG WETVDWVKFN
GVLTQTDMKQ KIIIFGAEKD PIAPIENLEF YKQTINKECL RKVIILPDCS HNLCFDRPEL
VCENFQREVI DNSKL
