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 24-JAN-2024, entry version 122.
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; Pseudomonadota; 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}.
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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 AlphaFoldDB; P22088; -.
DR SMR; P22088; -.
DR STRING; 292.WI67_21750; -.
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 SABIO-RK; P22088; -.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 BINDING 61
FT /ligand="substrate"
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 /ligand="substrate"
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 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 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
//
