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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

Ca2+Note: Binds 1 Ca(2+) 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 PublicationAdd
BLAST
Chaini45 – 364320LipasePRO_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

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni46 – 494Combined sources
Beta strandi55 – 584Combined sources
Beta strandi61 – 644Combined sources
Beta strandi65 – 673Combined sources
Turni68 – 703Combined sources
Beta strandi71 – 744Combined sources
Helixi77 – 837Combined sources
Beta strandi88 – 903Combined sources
Beta strandi95 – 973Combined sources
Beta strandi99 – 1013Combined sources
Helixi105 – 12016Combined sources
Beta strandi125 – 1306Combined sources
Helixi132 – 14312Combined sources
Helixi145 – 1473Combined sources
Beta strandi148 – 1558Combined sources
Helixi162 – 17110Combined sources
Helixi178 – 19417Combined sources
Helixi204 – 2118Combined sources
Helixi213 – 22210Combined sources
Beta strandi239 – 2435Combined sources
Beta strandi246 – 25510Combined sources
Beta strandi258 – 2647Combined sources
Beta strandi267 – 2726Combined sources
Turni277 – 2793Combined sources
Helixi282 – 2854Combined sources
Helixi288 – 30013Combined sources
Turni301 – 3033Combined sources
Beta strandi306 – 3127Combined sources
Helixi313 – 3164Combined sources
Beta strandi319 – 3268Combined sources
Helixi332 – 3343Combined sources
Turni335 – 3395Combined sources
Helixi348 – 36114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MARTMRSRVV AGAVACAMSI APFAGTTAVM TLATTHAAMA ATAPAAGYAA
60 70 80 90 100
TRYPIILVHG LSGTDKYAGV LEYWYGIQED LQQNGATVYV ANLSGFQSDD
110 120 130 140 150
GPNGRGEQLL AYVKTVLAAT GATKVNLVGH SQGGLSSRYV AAVAPDLVAS
160 170 180 190 200
VTTIGTPHRG SEFADFVQDV LAYDPTGLSS SVIAAFVNVF GILTSSSHNT
210 220 230 240 250
NQDALAALQT LTTARAATYN QNYPSAGLGA PGSCQTGAPT ETVGGNTHLL
260 270 280 290 300
YSWAGTAIQP TLSVFGVTGA TDTSTLPLVD PANVLDLSTL ALFGTGTVMI
310 320 330 340 350
NRGSGQNDGL VSKCSALYGK VLSTSYKWNH LDEINQLLGV RGAYAEDPVA
360
VIRTHANRLK LAGV
Length:364
Mass (Da):37,494
Last modified:February 1, 1996 - v2
Checksum:iE9CD2DBFB55658E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58494 Genomic DNA. Translation: AAA50466.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58494 Genomic DNA. Translation: AAA50466.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 94 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