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 30-AUG-2017, entry version 104. DE RecName: Full=Triacylglycerol lipase {ECO:0000303|PubMed:1987151}; DE EC=3.1.1.3 {ECO:0000305|PubMed:1856176, ECO:0000305|PubMed:7522571}; DE AltName: Full=Extracellular lipase {ECO:0000303|PubMed:1987151}; DE AltName: Full=Triacylglycerol ester hydrolase {ECO:0000250|UniProtKB:P26876}; DE Flags: Precursor; GN Name=lip {ECO:0000305}; Synonyms=lipA {ECO:0000303|PubMed:1987151}; 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], PROTEIN SEQUENCE OF 45-66, AND RP NOMENCLATURE. RC STRAIN=DSM 3959; RX PubMed=1987151; DOI=10.1128/jb.173.2.559-567.1991; 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 PROTEIN SEQUENCE OF 45-68, FUNCTION, CATALYTIC ACTIVITY, ENZYME RP REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT. RC STRAIN=ATCC 21808 / FERM P-1431 / 156-A; RX PubMed=1856176; RA Kordel M., Hofmann B., Schomburg D., Schmid R.D.; RT "Extracellular lipase of Pseudomonas sp. strain ATCC 21808: RT purification, characterization, crystallization, and preliminary X-ray RT diffraction data."; RL J. Bacteriol. 173:4836-4841(1991). RN [3] RP PROTEIN SEQUENCE OF 45-66, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE RP SPECIFICITY, AND SUBUNIT. RX PubMed=7522571; RA Bornscheuer U., Reif O.W., Lausch R., Freitag R., Scheper T., RA Kolisis F.N., Menge U.; RT "Lipase of Pseudomonas cepacia for biotechnological purposes: RT purification, crystallization and characterization."; RL Biochim. Biophys. Acta 1201:55-60(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 45-364 IN COMPLEX WITH RP CALCIUM ION, COFACTOR, DISULFIDE BOND, AND ACTIVE SITE. RX 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 [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 45-364 IN COMPLEX WITH RP CALCIUM ION, COFACTOR, AND ACTIVE SITE. RX 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 [6] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 45-364 IN COMPLEX WITH RP SUBSTRATE ANALOGS AND CALCIUM ION, COFACTOR, ENZYME REGULATION, ACTIVE RP SITE, AND SUBUNIT. 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 [7] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 45-364 IN COMPLEX WITH RP SUBSTRATE ANALOG AND CALCIUM ION, COFACTOR, AND ACTIVE SITE. 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). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 45-364 IN COMPLEX WITH RP SUBSTRATE ANALOG AND CALCIUM ION, COFACTOR, AND ACTIVE SITE. RX PubMed=15850979; DOI=10.1016/j.chembiol.2005.01.016; RA Mezzetti A., Schrag J.D., Cheong C.S., Kazlauskas R.J.; RT "Mirror-image packing in enantiomer discrimination molecular basis for RT the enantioselectivity of B.cepacia lipase toward 2-methyl-3-phenyl-1- RT propanol."; RL Chem. Biol. 12:427-437(2005). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 45-364 IN COMPLEX WITH RP SUBSTRATE ANALOG AND CALCIUM ION, COFACTOR, AND ACTIVE SITE. RX PubMed=18386861; DOI=10.1021/jp077717u; RA Luic M., Stefanic Z., Ceilinger I., Hodoscek M., Janezic D., Lenac T., RA Asler I.L., Sepac D., Tomic S.; RT "Combined X-ray diffraction and QM/MM study of the Burkholderia RT cepacia lipase-catalyzed secondary alcohol esterification."; RL J. Phys. Chem. B 112:4876-4883(2008). CC -!- FUNCTION: Catalyzes the hydrolysis of triacylglycerol. It shows a CC preference for triacylglycerols with a chain length between 6 and CC 12 carbons. {ECO:0000269|PubMed:1856176, CC ECO:0000269|PubMed:7522571}. CC -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a CC carboxylate. {ECO:0000305|PubMed:1856176, CC ECO:0000305|PubMed:7522571}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:11453990, CC ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, CC ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, CC ECO:0000269|PubMed:9660188}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11453990, CC ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, CC ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, CC ECO:0000269|PubMed:9660188}; CC -!- ENZYME REGULATION: Inhibited by RC-(Rp,Sp)- and SC-(Rp,Sp)-1,2- CC dioctylcarbamoylglycero-3-O-p-nitrophenyl octylphosphonate CC (PubMed:9660188). Also inhibited by diethyl-p-nitrophenylphosphate CC (E600) (PubMed:1856176). {ECO:0000269|PubMed:1856176, CC ECO:0000269|PubMed:9660188}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9660188, CC ECO:0000305|PubMed:1856176, ECO:0000305|PubMed:7522571}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q05489}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Pseudomonas CC lipase family. {ECO:0000305}. 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=45-364. DR PDB; 1OIL; X-ray; 2.10 A; A/B=45-364. DR PDB; 1YS1; X-ray; 1.10 A; X=45-364. DR PDB; 1YS2; X-ray; 1.50 A; X=45-364. DR PDB; 2LIP; X-ray; 2.10 A; A=45-364. DR PDB; 2NW6; X-ray; 1.80 A; A=45-364. DR PDB; 3LIP; X-ray; 2.00 A; A=45-364. DR PDB; 4LIP; X-ray; 1.75 A; D/E=45-364. DR PDB; 5LIP; X-ray; 2.90 A; A=45-364. 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 ProteinModelPortal; P22088; -. DR SMR; P22088; -. DR DrugBank; DB08419; (1S)-1-(PHENOXYMETHYL)PROPYL METHYLPHOSPHONOCHLORIDOATE. DR DrugBank; DB06965; HEXYLPHOSPHONIC ACID (R)-2-METHYL-3-PHENYLPROPYL ESTER. DR DrugBank; DB06966; HEXYLPHOSPHONIC ACID (S)-2-METHYL-3-PHENYLPROPYL ESTER. DR ESTHER; burce-lipaa; Bacterial_lip_FamI.2. DR BRENDA; 3.1.1.3; 1028. DR EvolutionaryTrace; P22088; -. 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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond; KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; KW Secreted; Signal. FT SIGNAL 1 44 {ECO:0000269|PubMed:1856176, FT ECO:0000269|PubMed:1987151, FT ECO:0000269|PubMed:7522571}. FT CHAIN 45 364 Triacylglycerol lipase. FT /FTId=PRO_0000017740. FT DOMAIN 54 266 AB hydrolase-1. {ECO:0000255}. FT ACT_SITE 131 131 Nucleophile. {ECO:0000244|PDB:1HQD, FT ECO:0000244|PDB:1YS1, FT ECO:0000244|PDB:1YS2, FT ECO:0000244|PDB:2NW6, FT ECO:0000244|PDB:4LIP, FT ECO:0000244|PDB:5LIP, FT ECO:0000305|PubMed:11453990, FT ECO:0000305|PubMed:15850979, FT ECO:0000305|PubMed:18386861, FT ECO:0000305|PubMed:9032073, FT ECO:0000305|PubMed:9032074, FT ECO:0000305|PubMed:9660188}. FT ACT_SITE 308 308 Charge relay system. FT {ECO:0000244|PDB:4LIP, FT ECO:0000244|PDB:5LIP, FT ECO:0000305|PubMed:11453990, FT ECO:0000305|PubMed:9032073, FT ECO:0000305|PubMed:9032074, FT ECO:0000305|PubMed:9660188}. FT ACT_SITE 330 330 Charge relay system. FT {ECO:0000244|PDB:4LIP, FT ECO:0000244|PDB:5LIP, FT ECO:0000305|PubMed:11453990, FT ECO:0000305|PubMed:9032073, FT ECO:0000305|PubMed:9032074, FT ECO:0000305|PubMed:9660188}. FT METAL 286 286 Calcium. {ECO:0000244|PDB:1HQD, FT ECO:0000244|PDB:1OIL, FT ECO:0000244|PDB:1YS1, FT ECO:0000244|PDB:1YS2, FT ECO:0000244|PDB:2LIP, FT ECO:0000244|PDB:2NW6, FT ECO:0000244|PDB:3LIP, FT ECO:0000244|PDB:4LIP, FT ECO:0000244|PDB:5LIP, FT ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, FT ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9032073, FT ECO:0000269|PubMed:9032074, FT ECO:0000269|PubMed:9660188}. FT METAL 332 332 Calcium. {ECO:0000244|PDB:1HQD, FT ECO:0000244|PDB:1OIL, FT ECO:0000244|PDB:1YS1, FT ECO:0000244|PDB:1YS2, FT ECO:0000244|PDB:2LIP, FT ECO:0000244|PDB:2NW6, FT ECO:0000244|PDB:3LIP, FT ECO:0000244|PDB:4LIP, FT ECO:0000244|PDB:5LIP, FT ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, FT ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9032073, FT ECO:0000269|PubMed:9032074, FT ECO:0000269|PubMed:9660188}. FT METAL 336 336 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:1HQD, FT ECO:0000244|PDB:1OIL, FT ECO:0000244|PDB:1YS1, FT ECO:0000244|PDB:1YS2, FT ECO:0000244|PDB:2LIP, FT ECO:0000244|PDB:2NW6, FT ECO:0000244|PDB:3LIP, FT ECO:0000244|PDB:4LIP, FT ECO:0000244|PDB:5LIP, FT ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, FT ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9032073, FT ECO:0000269|PubMed:9032074, FT ECO:0000269|PubMed:9660188}. FT METAL 340 340 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:1HQD, FT ECO:0000244|PDB:1OIL, FT ECO:0000244|PDB:1YS1, FT ECO:0000244|PDB:1YS2, FT ECO:0000244|PDB:2LIP, FT ECO:0000244|PDB:2NW6, FT ECO:0000244|PDB:3LIP, FT ECO:0000244|PDB:4LIP, FT ECO:0000244|PDB:5LIP, FT ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, FT ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9032073, FT ECO:0000269|PubMed:9032074, FT ECO:0000269|PubMed:9660188}. FT BINDING 61 61 Substrate; via amide nitrogen. FT {ECO:0000244|PDB:1HQD, FT ECO:0000244|PDB:1YS1, FT ECO:0000244|PDB:1YS2, FT ECO:0000244|PDB:2NW6, FT ECO:0000244|PDB:4LIP, FT ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, FT ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9660188}. FT BINDING 132 132 Substrate; via amide nitrogen. FT {ECO:0000244|PDB:1HQD, FT ECO:0000244|PDB:1YS1, FT ECO:0000244|PDB:1YS2, FT ECO:0000244|PDB:2NW6, FT ECO:0000244|PDB:4LIP, FT ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, FT ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9660188}. FT DISULFID 234 314 {ECO:0000269|PubMed:9032073}. FT TURN 46 49 {ECO:0000244|PDB:1OIL}. FT STRAND 55 58 {ECO:0000244|PDB:1YS1}. FT STRAND 61 64 {ECO:0000244|PDB:2LIP}. FT STRAND 65 67 {ECO:0000244|PDB:1YS1}. FT TURN 68 70 {ECO:0000244|PDB:1YS1}. FT STRAND 71 74 {ECO:0000244|PDB:1YS1}. FT HELIX 77 83 {ECO:0000244|PDB:1YS1}. FT STRAND 88 90 {ECO:0000244|PDB:1YS1}. FT STRAND 95 97 {ECO:0000244|PDB:4LIP}. FT STRAND 99 101 {ECO:0000244|PDB:1YS1}. FT HELIX 105 120 {ECO:0000244|PDB:1YS1}. FT STRAND 125 130 {ECO:0000244|PDB:1YS1}. FT HELIX 132 143 {ECO:0000244|PDB:1YS1}. FT HELIX 145 147 {ECO:0000244|PDB:1YS1}. FT STRAND 148 155 {ECO:0000244|PDB:1YS1}. FT HELIX 162 171 {ECO:0000244|PDB:1YS1}. FT HELIX 178 194 {ECO:0000244|PDB:1YS1}. FT HELIX 204 211 {ECO:0000244|PDB:1YS1}. FT HELIX 213 222 {ECO:0000244|PDB:1YS1}. FT STRAND 239 243 {ECO:0000244|PDB:1YS1}. FT STRAND 246 255 {ECO:0000244|PDB:1YS1}. FT STRAND 258 264 {ECO:0000244|PDB:1YS1}. FT STRAND 267 272 {ECO:0000244|PDB:1YS1}. FT TURN 277 279 {ECO:0000244|PDB:1YS1}. FT HELIX 282 285 {ECO:0000244|PDB:1YS1}. FT HELIX 288 300 {ECO:0000244|PDB:1YS1}. FT TURN 301 303 {ECO:0000244|PDB:1YS1}. FT STRAND 306 312 {ECO:0000244|PDB:1YS1}. FT HELIX 313 316 {ECO:0000244|PDB:1YS1}. FT STRAND 319 326 {ECO:0000244|PDB:1YS1}. FT HELIX 332 334 {ECO:0000244|PDB:1YS1}. FT TURN 335 339 {ECO:0000244|PDB:1YS1}. FT HELIX 348 361 {ECO:0000244|PDB:1YS1}. 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 //