LIPT_BURCE
ID LIPT_BURCE Reviewed; 56 AA.
AC P29605;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 11-DEC-2019, entry version 57.
DE RecName: Full=Lipase, thermostable;
DE EC=3.1.1.3;
DE AltName: Full=Triacylglycerol lipase;
DE Flags: Fragment;
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1282513; DOI=10.1093/oxfordjournals.jbchem.a123946;
RA Sugihara A., Ueshima M., Shimada Y., Tsunasawa S., Tominaga Y.;
RT "Purification and characterization of a novel thermostable lipase from
RT Pseudomonas cepacia.";
RL J. Biochem. 112:598-603(1992).
CC -!- FUNCTION: This thermostable and solvent-tolerant lipase is rather
CC nonspecific. It can synthesize both primary and secondary alcohol
CC esters. Simple triglycerides of short and middle chain fatty acids
CC (C<13) are the preferred substrates.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable.;
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas lipase
CC family. {ECO:0000305}.
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DR PIR; PX0065; PX0065.
DR ESTHER; burce-lipad; Bacterial_lip_FamI.2.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism.
FT CHAIN 1..>56
FT /note="Lipase, thermostable"
FT /id="PRO_0000090354"
FT NON_TER 56
SQ SEQUENCE 56 AA; 6314 MW; 31C29C6AE8E8CCEE CRC64;
AVDDYAATRY PIILVHGLTT DSKYGGVVEY XYRNPNDLTS HXXAAYVYEL RSDPLD