ID LIP_BURCE Reviewed; 364 AA. AC P22088; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 20-APR-2010, entry version 81. DE RecName: Full=Lipase; DE EC=3.1.1.3; DE AltName: Full=Triacylglycerol lipase; DE Flags: Precursor; GN Name=lipA; OS Burkholderia cepacia (Pseudomonas cepacia). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN 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; DOI=10.1016/S0969-2126(97)00177-9; 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 (2.0 ANGSTROMS). RX MEDLINE=97184685; PubMed=9032074; DOI=10.1016/S0969-2126(97)00178-0; 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). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF COMPLEXES WITH RP 1,2-DIBUTYLCARBAMOYLGLYCERO-3-O-P-NITROPHENYL-BUTYLPHOSPHONATE AND RP 1,2-DIOCTYLCARBAMOYLGLYCERO-3-O-P-NITROPHENYL-OCTYLPHOSPHONATE RP INHIBITORS. RC STRAIN=ATCC 21808 / FERM P-1431 / 156-A; RX PubMed=9660188; DOI=10.1046/j.1432-1327.1998.2540333.x; RA Lang D.A., Mannesse M.L., de Haas G.H., Verheij H.M., Dijkstra B.W.; RT "Structural basis of the chiral selectivity of Pseudomonas cepacia RT lipase."; RL Eur. J. Biochem. 254:333-340(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH RP (RP,SP)-O-(2R)-(1-PHENOXYBUT-2-YL)-METHYLPHOSPHONIC ACID CHLORIDE RP INHIBITOR. RX PubMed=11453990; DOI=10.1046/j.1432-1327.2001.02303.x; RA Luic M., Tomic S., Lescic I., Ljubovic E., Sepac D., Sunjic V., RA Vitale L., Saenger W., Kojic-Prodic B.; RT "Complex of Burkholderia cepacia lipase with transition state analogue RT of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling RT study."; RL Eur. J. Biochem. 268:3964-3973(2001). CC -!- FUNCTION: Catalyzes the hydrolysis of triglycerides. CC -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a CC carboxylate. CC -!- COFACTOR: Binds 1 calcium ion per subunit. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas CC 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; -; Genomic_DNA. DR PDB; 1HQD; X-ray; 2.30 A; A=48-364. DR PDB; 1OIL; X-ray; 2.10 A; A/B=48-364. DR PDB; 1YS1; X-ray; 1.10 A; X=48-364. DR PDB; 1YS2; X-ray; 1.50 A; X=48-364. DR PDB; 2LIP; X-ray; 2.10 A; A=48-364. DR PDB; 2NW6; X-ray; 1.80 A; A=48-364. DR PDB; 3LIP; X-ray; 2.00 A; A=48-364. DR PDB; 4LIP; X-ray; 1.75 A; D/E=48-364. DR PDB; 5LIP; X-ray; 2.90 A; A=48-364. DR PDBsum; 1HQD; -. DR PDBsum; 1OIL; -. DR PDBsum; 1YS1; -. DR PDBsum; 1YS2; -. DR PDBsum; 2LIP; -. DR PDBsum; 2NW6; -. DR PDBsum; 3LIP; -. DR PDBsum; 4LIP; -. DR PDBsum; 5LIP; -. DR BRENDA; 3.1.1.3; 74079. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004806; F:triglyceride lipase activity; IEA:EC. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR InterPro; IPR000073; AB_hydrolase_1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PROSITE; PS00120; LIPASE_SER; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond; KW Hydrolase; Lipid degradation; Metal-binding; Signal. FT SIGNAL 1 44 FT CHAIN 45 364 Lipase. FT /FTId=PRO_0000017740. FT ACT_SITE 131 131 Nucleophile. FT ACT_SITE 308 308 Charge relay system. FT ACT_SITE 330 330 Charge relay system. FT METAL 286 286 Calcium. FT METAL 332 332 Calcium. FT METAL 336 336 Calcium. FT METAL 340 340 Calcium; via carbonyl oxygen. FT DISULFID 234 314 FT STRAND 55 58 FT STRAND 65 67 FT TURN 68 70 FT STRAND 71 74 FT HELIX 77 83 FT STRAND 88 90 FT STRAND 99 101 FT HELIX 105 120 FT STRAND 125 130 FT HELIX 132 143 FT HELIX 145 147 FT STRAND 148 155 FT HELIX 162 171 FT HELIX 178 194 FT HELIX 204 211 FT HELIX 213 222 FT STRAND 239 243 FT STRAND 246 255 FT STRAND 258 264 FT STRAND 267 272 FT TURN 277 279 FT HELIX 282 285 FT HELIX 288 300 FT TURN 301 303 FT STRAND 306 312 FT HELIX 313 316 FT STRAND 319 326 FT HELIX 332 334 FT TURN 335 339 FT HELIX 348 361 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 //