P22088 (LIP_BURCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipase
EC=3.1.1.3

Alternative name(s):
Triacylglycerol lipase

Gene names

Name:

lipA

Organism

Burkholderia cepacia (Pseudomonas cepacia)

Taxonomic identifier

292 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Lipid degradation Lipid metabolism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW retinyl-palmitate esterase activity Inferred from electronic annotation. Source: EC triglyceride lipase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 44

44

Ref.1

Chain

45 – 364

320

Lipase

PRO_0000017740

Sites

Active site

131

1

Nucleophile

Active site

308

1

Charge relay system

Active site

330

1

Charge relay system

Metal binding

286

1

Calcium

Metal binding

332

1

Calcium

Metal binding

336

1

Calcium

Metal binding

340

1

Calcium; via carbonyl oxygen

Amino acid modifications

Disulfide bond

234 ↔ 314

Secondary structure

1

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364

Helix Strand Turn

Details...

Beta strand

55 – 58

4

Beta strand

61 – 64

4

Beta strand

65 – 67

3

Turn

68 – 70

3

Beta strand

71 – 74

4

Helix

77 – 83

7

Beta strand

88 – 90

3

Beta strand

95 – 97

3

Beta strand

99 – 101

3

Helix

105 – 120

16

Beta strand

125 – 130

6

Helix

132 – 143

12

Helix

145 – 147

3

Beta strand

148 – 155

8

Helix

162 – 171

10

Helix

178 – 194

17

Helix

204 – 211

8

Helix

213 – 222

10

Beta strand

239 – 243

5

Beta strand

246 – 255

10

Beta strand

258 – 264

7

Beta strand

267 – 272

6

Turn

277 – 279

3

Helix

282 – 285

4

Helix

288 – 300

13

Turn

301 – 303

3

Beta strand

306 – 312

7

Helix

313 – 316

4

Beta strand

319 – 326

8

Helix

332 – 334

3

Turn

335 – 339

5

Helix

348 – 361

14

Sequences

	Sequence		Length	Mass (Da)
	P22088 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: E9CD2DBFB55658E9	FASTA	364	37,494
	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

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HQD	X-ray	2.30	A	48-364	[»]
1OIL	X-ray	2.10	A/B	48-364	[»]
1YS1	X-ray	1.10	X	48-364	[»]
1YS2	X-ray	1.50	X	48-364	[»]
2LIP	X-ray	2.10	A	48-364	[»]
2NW6	X-ray	1.80	A	48-364	[»]
3LIP	X-ray	2.00	A	48-364	[»]
4LIP	X-ray	1.75	D/E	48-364	[»]
5LIP	X-ray	2.90	A	48-364	[»]

ProteinModelPortal

P22088.

SMR

P22088. Positions 48-364.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000073. AB_hydrolase_1.
[Graphical view]

Pfam

PF00561. Abhydrolase_1. 1 hit.
[Graphical view]

PROSITE

PS00120. LIPASE_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P22088.

Entry information

Entry name

LIP_BURCE

Accession

Primary (citable) accession number: P22088

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program