LIP_PSEU0
ID LIP_PSEU0 Reviewed; 311 AA.
AC P26877;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Triacylglycerol lipase {ECO:0000303|PubMed:1917947};
DE EC=3.1.1.3 {ECO:0000305|PubMed:1917947};
DE AltName: Full=Extracellular lipase {ECO:0000303|PubMed:1917947};
DE AltName: Full=Lactonizing lipase {ECO:0000303|PubMed:1917947};
DE AltName: Full=Lipase P {ECO:0000303|PubMed:1917947};
DE AltName: Full=Triacylglycerol ester hydrolase {ECO:0000250|UniProtKB:P26876};
DE Flags: Precursor;
GN Name=lipL {ECO:0000303|PubMed:1917947};
OS Pseudomonas sp. (strain 109).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=72584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-45, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=109;
RX PubMed=1917947; DOI=10.1016/s0021-9258(18)55246-7;
RA Ihara F., Kageyama Y., Hirata M., Nihira T., Yamada Y.;
RT "Purification, characterization, and molecular cloning of lactonizing
RT lipase from Pseudomonas species.";
RL J. Biol. Chem. 266:18135-18140(1991).
CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerol. Also able to
CC catalyze, in anhydrous organic solvents, intramolecular
CC transesterification of omega-hydroxyfatty acid esters to form
CC macrocyclic lactones. This biosynthesis is dependent on the chain
CC length of the substrates, and the formation of monomer lactone is
CC maximum with methyl 18-hydroxyoctadecanoate. With shorter substrates,
CC monomer lactone decreases and the formation of diolide (dimer lactone)
CC increases. {ECO:0000269|PubMed:1917947}.
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:0000305|PubMed:1917947};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P26876};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P26876};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P26876}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26876}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas lipase
CC family. {ECO:0000305}.
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DR EMBL; D10166; BAA01035.1; -; Genomic_DNA.
DR PIR; A40943; A40943.
DR AlphaFoldDB; P26877; -.
DR SMR; P26877; -.
DR ESTHER; psesp-llipa; Bacterial_lip_FamI.1.
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; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:1917947"
FT CHAIN 27..311
FT /note="Triacylglycerol lipase"
FT /id="PRO_0000017746"
FT DOMAIN 35..280
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT ACT_SITE 255
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT ACT_SITE 277
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P26876"
FT DISULFID 209..261
FT /evidence="ECO:0000250|UniProtKB:P26876"
SQ SEQUENCE 311 AA; 32737 MW; 27AC2F3DD3B334D1 CRC64;
MKKKSLLPLG LAIGLASLAA SPLIQASTYT QTKYPIVLAH GMLGFDNILG VDYWFGIPSA
LRRDGAQVYV TEVSQLDTSE VRGEQLLQQV EEIVALSGQP KVNLIGHSHG GPTIRYVAAV
RPDLMPSATS VGAPHKGSDT ADFLRQIPPG SAGEAVLSGL VNSLGALISF LSSGSAGTQN
SLGSLESLNS EGAARFNAKY PQGIPTSACG EGAYKVNGVS YYSWSGSSPL TNFLDPSDAF
LGASSLTFKN GTANDGLVGT CSSHLGMVIR DNYRMNHLDE VNQVFGLTSL FETSPVSVYR
QHANRLKNAS L
