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 02-JUN-2021, entry version 115. 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 Pseudomonas RT genes."; RL J. Bacteriol. 173:559-567(1991). RN [2] RP PROTEIN SEQUENCE OF 45-68, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT. RC STRAIN=ATCC 21808 / FERM P-1431 / 156-A; RX PubMed=1856176; DOI=10.1128/jb.173.15.4836-4841.1991; RA Kordel M., Hofmann B., Schomburg D., Schmid R.D.; RT "Extracellular lipase of Pseudomonas sp. strain ATCC 21808: purification, RT characterization, crystallization, and preliminary X-ray diffraction RT 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; DOI=10.1016/0304-4165(94)90151-1; RA Bornscheuer U., Reif O.W., Lausch R., Freitag R., Scheper T., Kolisis F.N., RA Menge U.; RT "Lipase of Pseudomonas cepacia for biotechnological purposes: purification, RT 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 CALCIUM RP 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 cepacia RT reveals a highly open conformation in the absence of a bound inhibitor."; RL Structure 5:173-185(1997). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 45-364 IN COMPLEX WITH CALCIUM RP 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 SUBSTRATE RP ANALOGS AND CALCIUM ION, COFACTOR, ACTIVITY REGULATION, ACTIVE SITE, AND RP 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 SUBSTRATE RP 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., Vitale L., RA Saenger W., Kojic-Prodic B.; RT "Complex of Burkholderia cepacia lipase with transition state analogue of RT 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study."; RL Eur. J. Biochem. 268:3964-3973(2001). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 45-364 IN COMPLEX WITH SUBSTRATE RP 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 the RT 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 SUBSTRATE RP 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 cepacia RT 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 12 CC carbons. {ECO:0000269|PubMed:1856176, ECO:0000269|PubMed:7522571}. 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 Evidence={ECO:0000305|PubMed:1856176, ECO:0000305|PubMed:7522571}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, CC ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9032073, CC ECO:0000269|PubMed:9032074, 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 -!- ACTIVITY 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 lipase CC 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 SMR; P22088; -. DR STRING; 292.DM42_4137; -. DR DrugBank; DB08419; (1S)-1-(PHENOXYMETHYL)PROPYL METHYLPHOSPHONOCHLORIDOATE. DR DrugBank; DB07990; (RP,SP)-O-(2R)-(1-PHENOXYBUT-2-YL)-METHYLPHOSPHONIC ACID CHLORIDE. 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 eggNOG; COG1075; Bacteria. 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; Secreted; KW Signal. FT SIGNAL 1..44 FT /evidence="ECO:0000269|PubMed:1856176, FT ECO:0000269|PubMed:1987151, ECO:0000269|PubMed:7522571" FT CHAIN 45..364 FT /note="Triacylglycerol lipase" FT /id="PRO_0000017740" FT DOMAIN 54..266 FT /note="AB hydrolase-1" FT /evidence="ECO:0000255" FT ACT_SITE 131 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:11453990, FT ECO:0000305|PubMed:15850979, ECO:0000305|PubMed:18386861, FT ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, FT ECO:0000305|PubMed:9660188, ECO:0007744|PDB:1HQD, FT ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, FT ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP, FT ECO:0007744|PDB:5LIP" FT ACT_SITE 308 FT /note="Charge relay system" FT /evidence="ECO:0000305|PubMed:11453990, FT ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, FT ECO:0000305|PubMed:9660188, ECO:0007744|PDB:4LIP, FT ECO:0007744|PDB:5LIP" FT ACT_SITE 330 FT /note="Charge relay system" FT /evidence="ECO:0000305|PubMed:11453990, FT ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, FT ECO:0000305|PubMed:9660188, ECO:0007744|PDB:4LIP, FT ECO:0007744|PDB:5LIP" FT METAL 286 FT /note="Calcium" FT /evidence="ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, FT ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, FT ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, FT ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, FT ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, FT ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP" FT METAL 332 FT /note="Calcium" FT /evidence="ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, FT ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, FT ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, FT ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, FT ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, FT ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP" FT METAL 336 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, FT ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, FT ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, FT ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, FT ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, FT ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP" FT METAL 340 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, FT ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, FT ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, FT ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, FT ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, FT ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP" FT BINDING 61 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, FT ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, FT ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP" FT BINDING 132 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000269|PubMed:11453990, FT ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, FT ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, FT ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, FT ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP" FT DISULFID 234..314 FT /evidence="ECO:0000269|PubMed:9032073" FT TURN 46..49 FT /evidence="ECO:0007829|PDB:1OIL" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:2LIP" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:1YS1" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 77..83 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:4LIP" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 105..120 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 125..130 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 132..143 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 148..155 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 162..171 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 178..194 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 204..211 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 213..222 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 239..243 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 246..255 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 258..264 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 267..272 FT /evidence="ECO:0007829|PDB:1YS1" FT TURN 277..279 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 282..285 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 288..300 FT /evidence="ECO:0007829|PDB:1YS1" FT TURN 301..303 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 306..312 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 313..316 FT /evidence="ECO:0007829|PDB:1YS1" FT STRAND 319..326 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 332..334 FT /evidence="ECO:0007829|PDB:1YS1" FT TURN 335..339 FT /evidence="ECO:0007829|PDB:1YS1" FT HELIX 348..361 FT /evidence="ECO:0007829|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 //