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Lipase (EC 3.1.1.3) (Lip 42) (Thermostable organic solvent tolerant lipase) (Triacylglycerol hydrolase)

 LIP_BACSP               Reviewed;         416 AA.
Q5U780;
31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
14-OCT-2015, sequence version 3.
12-SEP-2018, entry version 37.
RecName: Full=Lipase;
EC=3.1.1.3;
AltName: Full=Lip 42;
AltName: Full=Thermostable organic solvent tolerant lipase;
AltName: Full=Triacylglycerol hydrolase;
Flags: Precursor;
Bacillus sp.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=1409;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SOLVENT
STABILITY, AND ACTIVITY REGULATION.
STRAIN=42;
DOI=10.1007/BF03175607;
Hamid T.H.T.A., Eltaweel M.A., Rahman R.N.Z.R.A., Basri M.,
Salleh A.B.;
"Characterization and solvent stable features of Strep-tagged purified
recombinant lipase from thermostable and solvent tolerant Bacillus sp.
strain 42.";
Ann. Microbiol. 59:111-118(2009).
[2]
SEQUENCE REVISION TO 175.
Khusaini M.S., Rahman R.N.Z.R.A.;
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
[3]
X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 29-416 IN COMPLEX WITH
CALCIUM, SUBUNIT, AND ACTIVE SITES.
STRAIN=42;
Zaliha R.N., Rahman R.A., Khusaini M.S.;
"An Organic solvent tolerant lipase 42.";
Submitted (JUN-2012) to the PDB data bank.
-!- FUNCTION: Triacylglycerol hydrolase that shows hydrolysis
preference towards some of the natural oils such as olive,
sunflower and corn oils. {ECO:0000269|Ref.1}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate. {ECO:0000269|Ref.1}.
-!- ACTIVITY REGULATION: Activity is inhibited by zinc and iron ions,
and activated in vitro in 25% v/v DMSO and acetone.
{ECO:0000269|Ref.1}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.0. Is stable in a broad pH range of 7-10.
{ECO:0000269|Ref.1};
Temperature dependence:
Optimum temperature is 70 degrees Celsius. Highly thermostable
with a half-life of 315 minutes at 60 degrees Celsius, 125
minutes at 65 degrees Celsius and 45 minutes at 70 degrees
Celsius. {ECO:0000269|Ref.1};
-!- SUBUNIT: Homodimer. {ECO:0000269|Ref.3}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- MISCELLANEOUS: Is stable in polar organic solvents such as DMSO,
DMF, acetone, methanol, ethanol, heptanol and octanol, which could
make it as a potential biocatalyst for the use in industrial
biodiesel production.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily.
{ECO:0000305}.
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EMBL; AY787835; AAV35102.2; -; Genomic_DNA.
PDB; 4FKB; X-ray; 1.22 A; A/B=29-416.
PDBsum; 4FKB; -.
SMR; Q5U780; -.
ESTHER; bacsp-lip; Bacterial_lip_FamI.5.
PRIDE; Q5U780; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Calcium; Hydrolase; Lipid degradation; Lipid metabolism;
Metal-binding; Secreted; Signal.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 416 Lipase.
/FTId=PRO_0000419954.
ACT_SITE 141 141 Nucleophile. {ECO:0000269|Ref.3}.
ACT_SITE 345 345 Charge relay system. {ECO:0000269|Ref.3}.
ACT_SITE 386 386 Charge relay system. {ECO:0000269|Ref.3}.
METAL 314 314 Calcium; via carbonyl oxygen.
{ECO:0000269|Ref.3}.
METAL 385 385 Calcium. {ECO:0000250}.
METAL 388 388 Calcium. {ECO:0000269|Ref.3}.
METAL 393 393 Calcium. {ECO:0000269|Ref.3}.
METAL 394 394 Calcium; via carbonyl oxygen.
{ECO:0000269|Ref.3}.
STRAND 38 41 {ECO:0000244|PDB:4FKB}.
HELIX 52 54 {ECO:0000244|PDB:4FKB}.
TURN 57 59 {ECO:0000244|PDB:4FKB}.
HELIX 60 62 {ECO:0000244|PDB:4FKB}.
HELIX 65 71 {ECO:0000244|PDB:4FKB}.
STRAND 76 78 {ECO:0000244|PDB:4FKB}.
STRAND 83 85 {ECO:0000244|PDB:4FKB}.
HELIX 87 99 {ECO:0000244|PDB:4FKB}.
STRAND 101 104 {ECO:0000244|PDB:4FKB}.
HELIX 107 113 {ECO:0000244|PDB:4FKB}.
STRAND 117 122 {ECO:0000244|PDB:4FKB}.
HELIX 127 130 {ECO:0000244|PDB:4FKB}.
STRAND 135 140 {ECO:0000244|PDB:4FKB}.
HELIX 143 156 {ECO:0000244|PDB:4FKB}.
HELIX 159 168 {ECO:0000244|PDB:4FKB}.
HELIX 174 176 {ECO:0000244|PDB:4FKB}.
STRAND 183 190 {ECO:0000244|PDB:4FKB}.
HELIX 197 200 {ECO:0000244|PDB:4FKB}.
HELIX 204 218 {ECO:0000244|PDB:4FKB}.
STRAND 223 225 {ECO:0000244|PDB:4FKB}.
HELIX 237 239 {ECO:0000244|PDB:4FKB}.
HELIX 249 257 {ECO:0000244|PDB:4FKB}.
HELIX 260 263 {ECO:0000244|PDB:4FKB}.
STRAND 264 267 {ECO:0000244|PDB:4FKB}.
HELIX 268 272 {ECO:0000244|PDB:4FKB}.
HELIX 274 283 {ECO:0000244|PDB:4FKB}.
STRAND 290 297 {ECO:0000244|PDB:4FKB}.
STRAND 300 302 {ECO:0000244|PDB:4FKB}.
STRAND 304 307 {ECO:0000244|PDB:4FKB}.
STRAND 309 311 {ECO:0000244|PDB:4FKB}.
HELIX 317 322 {ECO:0000244|PDB:4FKB}.
HELIX 324 327 {ECO:0000244|PDB:4FKB}.
HELIX 333 335 {ECO:0000244|PDB:4FKB}.
HELIX 339 341 {ECO:0000244|PDB:4FKB}.
STRAND 344 349 {ECO:0000244|PDB:4FKB}.
HELIX 350 353 {ECO:0000244|PDB:4FKB}.
STRAND 364 366 {ECO:0000244|PDB:4FKB}.
STRAND 375 383 {ECO:0000244|PDB:4FKB}.
TURN 386 391 {ECO:0000244|PDB:4FKB}.
HELIX 400 412 {ECO:0000244|PDB:4FKB}.
SEQUENCE 416 AA; 46353 MW; 83E9005EDC6729BE CRC64;
MKCCRIMFVL LGLWFVFGLS VPGGRTEAAS LRANDAPIVL LHGFTGWGRE EMFGFKYWGG
VRGDIEQWLN DNGYRTYTLA VGPLSSNWDR ACEAYAQLVG GTVDYGAAHA AKHGHARFGR
TYPGLLPELK RGGRIHIIAH SQGGQTARML VSLLENGSQE EREYAKAHNV SLSPLFEGGH
HFVLSVTTIA TPHDGTTLVN MVDFTDRFFD LQKAVLEAAA VASNVPYTSQ VYDFKLDQWG
LRRQPGESFD HYFERLKRSP VWTSTDTARY DLSVSGAEKL NQWVQASPNT YYLSFSTERT
YRGALTGNHY PELGMNAFSA VVCAPFLGSY RNPTLGIDDR WLENDGIVNT VSMNGPKRGS
SDRIVPYDGT LKKGVWNDMG TYNVDHLEII GVDPNPSFDI RAFYLRLAEQ LASLRP


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