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LIP_BURCE
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   03-AUG-2022, entry version 118.
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}.
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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.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   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; -; 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   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
 
 
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