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P22088 (LIP_BURCE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipase

EC=3.1.1.3
Alternative name(s):
Triacylglycerol lipase
Gene names
Name:lipA
OrganismBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifier292 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of triglycerides.

Catalytic activity

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer.

Sequence similarities

Belongs to the AB hydrolase superfamily. Pseudomonas lipase family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

triglyceride lipase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4444 Ref.1
Chain45 – 364320Lipase
PRO_0000017740

Sites

Active site1311Nucleophile
Active site3081Charge relay system
Active site3301Charge relay system
Metal binding2861Calcium
Metal binding3321Calcium
Metal binding3361Calcium
Metal binding3401Calcium; via carbonyl oxygen

Amino acid modifications

Disulfide bond234 ↔ 314

Secondary structure

............................................................ 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22088 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: E9CD2DBFB55658E9

FASTA36437,494
        10         20         30         40         50         60 
MARTMRSRVV AGAVACAMSI APFAGTTAVM TLATTHAAMA ATAPAAGYAA TRYPIILVHG 

        70         80         90        100        110        120 
LSGTDKYAGV LEYWYGIQED LQQNGATVYV ANLSGFQSDD GPNGRGEQLL AYVKTVLAAT 

       130        140        150        160        170        180 
GATKVNLVGH SQGGLSSRYV AAVAPDLVAS VTTIGTPHRG SEFADFVQDV LAYDPTGLSS 

       190        200        210        220        230        240 
SVIAAFVNVF GILTSSSHNT NQDALAALQT LTTARAATYN QNYPSAGLGA PGSCQTGAPT 

       250        260        270        280        290        300 
ETVGGNTHLL YSWAGTAIQP TLSVFGVTGA TDTSTLPLVD PANVLDLSTL ALFGTGTVMI 

       310        320        330        340        350        360 
NRGSGQNDGL VSKCSALYGK VLSTSYKWNH LDEINQLLGV RGAYAEDPVA VIRTHANRLK 


LAGV 

« Hide

References

[1]"Cloning, sequence, and expression of a lipase gene from Pseudomonas cepacia: lipase production in heterologous hosts requires two Pseudomonas genes."
Joergensen S., Skov K.W., Diderichsen B.
J. Bacteriol. 173:559-567(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 45-66.
Strain: DSM 3959.
[2]"The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor."
Kim K.K., Song H.K., Shin D.H., Hwang K.Y., Suh S.W.
Structure 5:173-185(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[3]"The open conformation of a Pseudomonas lipase."
Schrag J.D., Li Y., Cygler M., Lang D., Burgdorf T., Hecht H.-J., Schmid R., Schomburg D., Rydel T.J., Oliver J.D., Strickland L.C., Dunaway C.M., Larson S.B., Day J., McPherson A.
Structure 5:187-202(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[4]"Structural basis of the chiral selectivity of Pseudomonas cepacia lipase."
Lang D.A., Mannesse M.L., de Haas G.H., Verheij H.M., Dijkstra B.W.
Eur. J. Biochem. 254:333-340(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF COMPLEXES WITH 1,2-DIBUTYLCARBAMOYLGLYCERO-3-O-P-NITROPHENYL-BUTYLPHOSPHONATE AND 1,2-DIOCTYLCARBAMOYLGLYCERO-3-O-P-NITROPHENYL-OCTYLPHOSPHONATE INHIBITORS.
Strain: ATCC 21808 / FERM P-1431 / 156-A.
[5]"Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study."
Luic M., Tomic S., Lescic I., Ljubovic E., Sepac D., Sunjic V., Vitale L., Saenger W., Kojic-Prodic B.
Eur. J. Biochem. 268:3964-3973(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH (RP,SP)-O-(2R)-(1-PHENOXYBUT-2-YL)-METHYLPHOSPHONIC ACID CHLORIDE INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58494 Genomic DNA. Translation: AAA50466.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HQDX-ray2.30A45-364[»]
1OILX-ray2.10A/B45-364[»]
1YS1X-ray1.10X45-364[»]
1YS2X-ray1.50X45-364[»]
2LIPX-ray2.10A45-364[»]
2NW6X-ray1.80A45-364[»]
3LIPX-ray2.00A45-364[»]
4LIPX-ray1.75D/E45-364[»]
5LIPX-ray2.90A45-364[»]
ProteinModelPortalP22088.
SMRP22088. Positions 48-364.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22088.

Entry information

Entry nameLIP_BURCE
AccessionPrimary (citable) accession number: P22088
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references