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-JUN-2002 (Rel. 41, 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. OX NCBI_TaxID=292; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 45-66. RC STRAIN=DSM 3959; RX MEDLINE=91100343; PubMed=1987151; RA Joergensen 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; PubMed=9032073; 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; PubMed=9032074; 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 + a CC fatty acid anion. CC -!- COFACTOR: REQUIRES CALCIUM. CC -!- SIMILARITY: BELONGS TO THE AB HYDROLASE SUPERFAMILY. PSEUDOMONAS CC LIPASE FAMILY. CC -!- SIMILARITY: BELONGS TO THE ABHYDROLASE SUPERFAMILY. LIPASE FAMILY. 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 InterPro; IPR000073; Abhydrolase. DR InterPro; IPR000734; Lipase. DR InterPro; IPR000379; Ser_estrs_site. 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. FT TURN 48 49 FT STRAND 55 58 FT TURN 61 62 FT STRAND 66 67 FT TURN 68 70 FT STRAND 71 72 FT TURN 75 76 FT HELIX 77 83 FT TURN 84 85 FT STRAND 88 90 FT TURN 102 103 FT HELIX 105 120 FT TURN 121 121 FT STRAND 125 130 FT TURN 131 132 FT HELIX 133 143 FT HELIX 145 147 FT STRAND 148 154 FT TURN 158 159 FT HELIX 162 171 FT TURN 172 173 FT TURN 175 176 FT HELIX 178 194 FT TURN 196 197 FT HELIX 204 210 FT TURN 211 211 FT HELIX 213 222 FT TURN 226 227 FT STRAND 228 228 FT TURN 231 232 FT STRAND 236 236 FT STRAND 240 242 FT STRAND 247 255 FT STRAND 258 264 FT TURN 265 266 FT STRAND 267 272 FT TURN 273 274 FT TURN 277 279 FT TURN 281 281 FT HELIX 282 285 FT HELIX 287 300 FT TURN 301 303 FT STRAND 307 307 FT STRAND 312 312 FT HELIX 313 316 FT STRAND 320 326 FT TURN 330 331 FT HELIX 332 334 FT TURN 335 339 FT TURN 343 344 FT HELIX 348 362 FT TURN 363 364 SQ SEQUENCE 364 AA; 37494 MW; E9CD2DBFB55658E9 CRC64; 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 //