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P22088

- LIP_BURCE

UniProt

P22088 - LIP_BURCE

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Protein
Lipase
Gene
lipA
Organism
Burkholderia cepacia (Pseudomonas cepacia)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of triglycerides.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Cofactori

Binds 1 calcium ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311Nucleophile
Metal bindingi286 – 2861Calcium
Active sitei308 – 3081Charge relay system
Active sitei330 – 3301Charge relay system
Metal bindingi332 – 3321Calcium
Metal bindingi336 – 3361Calcium
Metal bindingi340 – 3401Calcium; via carbonyl oxygen

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. triglyceride lipase activity Source: UniProtKB-EC

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase (EC:3.1.1.3)
Alternative name(s):
Triacylglycerol lipase
Gene namesi
Name:lipA
OrganismiBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifieri292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 44441 Publication
Add
BLAST
Chaini45 – 364320Lipase
PRO_0000017740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi234 ↔ 314

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni46 – 494
Beta strandi55 – 584
Beta strandi61 – 644
Beta strandi65 – 673
Turni68 – 703
Beta strandi71 – 744
Helixi77 – 837
Beta strandi88 – 903
Beta strandi95 – 973
Beta strandi99 – 1013
Helixi105 – 12016
Beta strandi125 – 1306
Helixi132 – 14312
Helixi145 – 1473
Beta strandi148 – 1558
Helixi162 – 17110
Helixi178 – 19417
Helixi204 – 2118
Helixi213 – 22210
Beta strandi239 – 2435
Beta strandi246 – 25510
Beta strandi258 – 2647
Beta strandi267 – 2726
Turni277 – 2793
Helixi282 – 2854
Helixi288 – 30013
Turni301 – 3033
Beta strandi306 – 3127
Helixi313 – 3164
Beta strandi319 – 3268
Helixi332 – 3343
Turni335 – 3395
Helixi348 – 36114

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP22088.
SMRiP22088. Positions 48-364.

Miscellaneous databases

EvolutionaryTraceiP22088.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22088-1 [UniParc]FASTAAdd to Basket

« Hide

MARTMRSRVV AGAVACAMSI APFAGTTAVM TLATTHAAMA ATAPAAGYAA    50
TRYPIILVHG LSGTDKYAGV LEYWYGIQED LQQNGATVYV ANLSGFQSDD 100
GPNGRGEQLL AYVKTVLAAT GATKVNLVGH SQGGLSSRYV AAVAPDLVAS 150
VTTIGTPHRG SEFADFVQDV LAYDPTGLSS SVIAAFVNVF GILTSSSHNT 200
NQDALAALQT LTTARAATYN QNYPSAGLGA PGSCQTGAPT ETVGGNTHLL 250
YSWAGTAIQP TLSVFGVTGA TDTSTLPLVD PANVLDLSTL ALFGTGTVMI 300
NRGSGQNDGL VSKCSALYGK VLSTSYKWNH LDEINQLLGV RGAYAEDPVA 350
VIRTHANRLK LAGV 364
Length:364
Mass (Da):37,494
Last modified:February 1, 1996 - v2
Checksum:iE9CD2DBFB55658E9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58494 Genomic DNA. Translation: AAA50466.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58494 Genomic DNA. Translation: AAA50466.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HQD X-ray 2.30 A 45-364 [» ]
1OIL X-ray 2.10 A/B 45-364 [» ]
1YS1 X-ray 1.10 X 45-364 [» ]
1YS2 X-ray 1.50 X 45-364 [» ]
2LIP X-ray 2.10 A 45-364 [» ]
2NW6 X-ray 1.80 A 45-364 [» ]
3LIP X-ray 2.00 A 45-364 [» ]
4LIP X-ray 1.75 D/E 45-364 [» ]
5LIP X-ray 2.90 A 45-364 [» ]
ProteinModelPortali P22088.
SMRi P22088. Positions 48-364.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P22088.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view ]
Pfami PF00561. Abhydrolase_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiLIP_BURCE
AccessioniPrimary (citable) accession number: P22088
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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