LIP_PSEFR
ID LIP_PSEFR Reviewed; 293 AA.
AC P08658; Q9EV86;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Triacylglycerol lipase {ECO:0000303|PubMed:6052627};
DE EC=3.1.1.3 {ECO:0000269|PubMed:12084074, ECO:0000269|PubMed:6052627, ECO:0000305|PubMed:15848176};
DE AltName: Full=Cold-adapted lipase {ECO:0000303|PubMed:15848176};
DE AltName: Full=Extracellular lipase {ECO:0000303|PubMed:5881339};
DE AltName: Full=Triacylglycerol ester hydrolase {ECO:0000250|UniProtKB:P26876};
GN Name=lips; ORFNames=SAMN05216594_0967 {ECO:0000312|EMBL:SDU12804.1};
OS Pseudomonas fragi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=296;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=JCM 20237 / NBRC 12049 / IAM 1650;
RX PubMed=3060375; DOI=10.1016/0014-5793(88)80980-3;
RA Aoyama S., Yoshida N., Inouye S.;
RT "Cloning, sequencing and expression of the lipase gene from Pseudomonas
RT fragi IFO-12049 in E. coli.";
RL FEBS Lett. 242:36-40(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF THR-137; THR-138 AND SER-141, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 4973 / DSM 3456 / LMG 2191 / NBRC 3458 / NRRL B-25 / VKM B-898;
RX PubMed=15848176; DOI=10.1016/j.febslet.2005.03.037;
RA Santarossa G., Lafranconi P.G., Alquati C., DeGioia L., Alberghina L.,
RA Fantucci P., Lotti M.;
RT "Mutations in the lid region affect chain length specificity and
RT thermostability of a Pseudomonas fragi lipase.";
RL FEBS Lett. 579:2383-2386(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-727 {ECO:0000312|EMBL:SDU12804.1};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC STRAIN=ATCC 4973 / DSM 3456 / LMG 2191 / NBRC 3458 / NRRL B-25 / VKM B-898;
RX PubMed=3800995; DOI=10.1016/s0006-291x(86)80352-7;
RA Kugimiya W., Otani Y., Hashimoto Y., Takagi Y.;
RT "Molecular cloning and nucleotide sequence of the lipase gene from
RT Pseudomonas fragi.";
RL Biochem. Biophys. Res. Commun. 141:185-190(1986).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=5881339; DOI=10.1016/0005-2760(65)90079-2;
RA Mencher J.R., Ng H., Alford J.A.;
RT "The extracellular nature of the lipase of Pseudomonas fragi.";
RL Biochim. Biophys. Acta 106:628-630(1965).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 4973 / DSM 3456 / LMG 2191 / NBRC 3458 / NRRL B-25 / VKM B-898;
RX PubMed=6052627; DOI=10.1099/00221287-48-3-317;
RA Mencher J.R., Alford J.A.;
RT "Purification and characterization of the lipase of Pseudomonas fragi.";
RL J. Gen. Microbiol. 48:317-328(1967).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBSTRATE SPECIFICITY, AND 3D-STRUCTURE MODELING.
RX PubMed=12084074; DOI=10.1046/j.1432-1033.2002.03012.x;
RA Alquati C., De Gioia L., Santarossa G., Alberghina L., Fantucci P.,
RA Lotti M.;
RT "The cold-active lipase of Pseudomonas fragi. Heterologous expression,
RT biochemical characterization and molecular modeling.";
RL Eur. J. Biochem. 269:3321-3328(2002).
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerols, with the
CC highest activity with tributyrin (C4), lower activity with tricaprylin
CC (C8), and much lower activity with triacetin (C2), trilaurin (C12) and
CC triolein (C18). {ECO:0000269|PubMed:12084074,
CC ECO:0000269|PubMed:15848176, ECO:0000269|PubMed:6052627}.
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:12084074, ECO:0000269|PubMed:6052627,
CC ECO:0000305|PubMed:15848176};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12084074};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P26876};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 mM for tributyrin {ECO:0000269|PubMed:6052627};
CC pH dependence:
CC Optimum pH is 8.8-9. {ECO:0000269|PubMed:12084074,
CC ECO:0000269|PubMed:6052627};
CC Temperature dependence:
CC Optimum temperature is 29 degrees Celsius (PubMed:12084074). Stable
CC at 10 degrees Celsius, but above this temperature the activity
CC decreases. The enzyme is completely inactivated at 40 degrees Celsius
CC (PubMed:6052627, PubMed:12084074). {ECO:0000269|PubMed:12084074,
CC ECO:0000269|PubMed:6052627};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:3060375,
CC ECO:0000305|PubMed:5881339}.
CC -!- MISCELLANEOUS: The lack of a signal peptide at the N-terminal suggests
CC that this lipase might be secreted by a signal peptide-independent
CC pathway. {ECO:0000305|PubMed:12084074}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas lipase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25879.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA32193.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X14033; CAA32193.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ250176; CAC07191.1; -; Genomic_DNA.
DR EMBL; LT629783; SDU12804.1; -; Genomic_DNA.
DR EMBL; M14604; AAA25879.1; ALT_FRAME; Genomic_DNA.
DR PIR; S02005; S02005.
DR RefSeq; WP_016781240.1; NZ_NQKM01000041.1.
DR AlphaFoldDB; P08658; -.
DR SMR; P08658; -.
DR STRING; 1136138.JH604622_gene2244; -.
DR ESTHER; psefr-lipas; Bacterial_lip_FamI.1.
DR GeneID; 67385294; -.
DR eggNOG; COG1075; Bacteria.
DR BRENDA; 3.1.1.3; 5123.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Secreted.
FT CHAIN 1..293
FT /note="Triacylglycerol lipase"
FT /id="PRO_0000017744"
FT DOMAIN 10..206
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22088"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22088"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:12084074"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:12084074"
FT MUTAGEN 137
FT /note="T->V: Increases the activity toward tricaprylin
FT (C8). The lipase is slightly destabilized at 27 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:15848176"
FT MUTAGEN 138
FT /note="T->N: Increases the activity toward tricaprylin
FT (C8). The lipase is slightly destabilized at 27 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:15848176"
FT MUTAGEN 141
FT /note="S->G: Increases the activity toward trilaurin (C12).
FT The lipase is destabilized at 27 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:15848176"
SQ SEQUENCE 293 AA; 32086 MW; 22C210CD542EB5DD CRC64;
MDDSVNTRYP ILLVHGLFGF DRIGSHHYFH GIKQALNECG ASVFVPIISA ANDNEARGDQ
LLKQIHNLRR QVGAQRVNLI GHSQGALTAR YVAAIAPELI ASVTSVSGPN HGSELADRLR
LAFVPGRLGE TVAAALTTSF SAFLSALSGH PRLPQNALNA LNALTTDGVA AFNRQYPQGL
PDRWGGMGPA QVNAVHYYSW SGIIKGSRLA ESLNLLDPLH NALRVFDSFF TRETRENDGM
VGRFSSHLGQ VIRSDYPLDH LDTINHMARG SRRRINPVEL YIEHAKRLKE AGL
