ID LIP_BURCE STANDARD; PRT; 364 AA. AC P22088; DT 01-AUG-1991 (Rel. 19, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE LIPASE PRECURSOR (EC 3.1.1.3) (TRIACYLGLYCEROL LIPASE). GN LIPA. OS Burkholderia cepacia (Pseudomonas cepacia). OC Bacteria; Proteobacteria; beta subdivision; Burkholderia group; OC Burkholderia. RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 45-66. RC STRAIN=DSM 3959; RX MEDLINE; 91100343. RA JORGENSEN S., SKOV K.W., DIDERICHSEN B.; RT "Cloning, sequence, and expression of a lipase gene from Pseudomonas RT cepacia: lipase production in heterologous hosts requires two RT Pseudomonas genes."; RL J. Bacteriol. 173:559-567(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX MEDLINE; 97184684. RA KIM K.K., SONG H.K., SHIN D.H., HWANG K.Y., SUH S.W.; RT "The crystal structure of a triacylglycerol lipase from Pseudomonas RT cepacia reveals a highly open conformation in the absence of a bound RT inhibitor."; RL Structure 5:173-185(1997). RN [3] RP X-RAY CRYSTALLOGRAPHY. RX MEDLINE; 97184685. RA SCHRAG J.D., LI Y., CYGLER M., LANG D., BURGDORF T., HECHT H.-J., RA SCHMID R., SCHOMBURG D., RYDEL T.J., OLIVER J.D., STRICKLAND L.C., RA DUNAWAY C.M., LARSON S.B., DAY J., MCPHERSON A.; RT "The open conformation of a Pseudomonas lipase."; RL Structure 5:187-202(1997). CC -!- CATALYTIC ACTIVITY: TRIACYLGLYCEROL + H(2)O = DIACYLGLYCEROL + CC A FATTY ACID ANION. CC -!- COFACTOR: REQUIRES CALCIUM. CC -!- SIMILARITY: STRONG TO OTHER PSEUDOMONAS LIPASES. CC -!- SIMILARITY: PARTIAL WITH OTHER LIPASES (PANCREATIC, GASTRIC, CC HEPATIC, LINGUAL, LIPOPROTEIN, BACTERIAL, ETC.). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M58494; AAA50466.1; -. DR PIR; A39133; A39133. DR PDB; 1OIL; 15-MAY-97. DR PDB; 2LIP; 12-MAR-97. DR PDB; 3LIP; 16-JUN-97. DR PFAM; PF00561; abhydrolase; 1. DR PROSITE; PS00120; LIPASE_SER; 1. KW Hydrolase; Lipid degradation; Signal; Calcium; 3D-structure. FT SIGNAL 1 44 FT CHAIN 45 364 LIPASE. FT ACT_SITE 131 131 CHARGE RELAY SYSTEM. FT ACT_SITE 286 286 CHARGE RELAY SYSTEM. FT ACT_SITE 330 330 CHARGE RELAY SYSTEM. SQ SEQUENCE 364 AA; 37494 MW; D030832A CRC32; MARTMRSRVV AGAVACAMSI APFAGTTAVM TLATTHAAMA ATAPAAGYAA TRYPIILVHG LSGTDKYAGV LEYWYGIQED LQQNGATVYV ANLSGFQSDD GPNGRGEQLL AYVKTVLAAT GATKVNLVGH SQGGLSSRYV AAVAPDLVAS VTTIGTPHRG SEFADFVQDV LAYDPTGLSS SVIAAFVNVF GILTSSSHNT NQDALAALQT LTTARAATYN QNYPSAGLGA PGSCQTGAPT ETVGGNTHLL YSWAGTAIQP TLSVFGVTGA TDTSTLPLVD PANVLDLSTL ALFGTGTVMI NRGSGQNDGL VSKCSALYGK VLSTSYKWNH LDEINQLLGV RGAYAEDPVA VIRTHANRLK LAGV //