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Protein

Lipase

Gene

lipA

Organism
Burkholderia glumae (Pseudomonas glumae)
Status
Reviewed-Annotation score: 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 Ca2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei126 – 1261Nucleophile
Metal bindingi280 – 2801Calcium
Active sitei302 – 3021Charge relay system
Active sitei324 – 3241Charge relay system
Metal bindingi326 – 3261Calcium
Metal bindingi330 – 3301Calcium
Metal bindingi334 – 3341Calcium; via carbonyl oxygen

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

ESTHERiburgl-lipas. Bacterial_lip_FamI.2.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase (EC:3.1.1.3)
Alternative name(s):
Triacylglycerol lipase
Gene namesi
Name:lipA
OrganismiBurkholderia glumae (Pseudomonas glumae)
Taxonomic identifieri337 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541H → A: No loss of activity. 1 Publication
Mutagenesisi126 – 1261S → A: Complete loss of activity. 1 Publication
Mutagenesisi160 – 1601D → A: No loss of activity. 1 Publication
Mutagenesisi160 – 1601D → E: No loss of activity. 1 Publication
Mutagenesisi280 – 2801D → A: Complete loss of activity. 1 Publication
Mutagenesisi280 – 2801D → E: No loss of activity. 1 Publication
Mutagenesisi302 – 3021D → A: 75% loss of activity. 1 Publication
Mutagenesisi302 – 3021D → E: No loss of activity. 1 Publication
Mutagenesisi324 – 3241H → A: Complete loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 39392 PublicationsAdd
BLAST
Chaini40 – 358319LipasePRO_0000017741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi229 ↔ 308

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
lifOQ054902EBI-993752,EBI-993746

Protein-protein interaction databases

DIPiDIP-29069N.
IntActiQ05489. 1 interaction.

Structurei

Secondary structure

1
358
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 534Combined sources
Beta strandi58 – 625Combined sources
Turni63 – 653Combined sources
Beta strandi66 – 694Combined sources
Helixi72 – 787Combined sources
Beta strandi83 – 853Combined sources
Beta strandi94 – 963Combined sources
Helixi100 – 11516Combined sources
Beta strandi120 – 1256Combined sources
Helixi128 – 13811Combined sources
Helixi140 – 1423Combined sources
Beta strandi143 – 1508Combined sources
Helixi157 – 16610Combined sources
Helixi176 – 18611Combined sources
Helixi195 – 2017Combined sources
Helixi202 – 2065Combined sources
Helixi208 – 21710Combined sources
Turni226 – 2283Combined sources
Beta strandi234 – 2385Combined sources
Beta strandi241 – 25010Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi264 – 2674Combined sources
Helixi276 – 2794Combined sources
Helixi282 – 29514Combined sources
Beta strandi300 – 3067Combined sources
Helixi307 – 3104Combined sources
Beta strandi313 – 3208Combined sources
Helixi326 – 3283Combined sources
Turni329 – 3335Combined sources
Helixi342 – 35514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CVLX-ray1.60A40-358[»]
1QGEX-ray1.70D40-261[»]
E262-358[»]
1TAHX-ray3.00A/B/C/D41-358[»]
2ES4X-ray1.85A/B40-358[»]
ProteinModelPortaliQ05489.
SMRiQ05489. Positions 41-358.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05489.

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.

Q05489-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRSMRSRVA ARAVAWALAV MPLAGAAGLT MAASPAAVAA DTYAATRYPV
60 70 80 90 100
ILVHGLAGTD KFANVVDYWY GIQSDLQSHG AKVYVANLSG FQSDDGPNGR
110 120 130 140 150
GEQLLAYVKQ VLAATGATKV NLIGHSQGGL TSRYVAAVAP QLVASVTTIG
160 170 180 190 200
TPHRGSEFAD FVQDVLKTDP TGLSSTVIAA FVNVFGTLVS SSHNTDQDAL
210 220 230 240 250
AALRTLTTAQ TATYNRNFPS AGLGAPGSCQ TGAATETVGG SQHLLYSWGG
260 270 280 290 300
TAIQPTSTVL GVTGATDTST GTLDVANVTD PSTLALLATG AVMINRASGQ
310 320 330 340 350
NDGLVSRCSS LFGQVISTSY HWNHLDEINQ LLGVRGANAE DPVAVIRTHV

NRLKLQGV
Length:358
Mass (Da):36,929
Last modified:October 1, 1994 - v1
Checksum:iFE7B5D7A22EC6B4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401A → W AA sequence (PubMed:7786905).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70354 Genomic DNA. Translation: CAA49812.1.
PIRiA48952.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70354 Genomic DNA. Translation: CAA49812.1.
PIRiA48952.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CVLX-ray1.60A40-358[»]
1QGEX-ray1.70D40-261[»]
E262-358[»]
1TAHX-ray3.00A/B/C/D41-358[»]
2ES4X-ray1.85A/B40-358[»]
ProteinModelPortaliQ05489.
SMRiQ05489. Positions 41-358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29069N.
IntActiQ05489. 1 interaction.

Protein family/group databases

ESTHERiburgl-lipas. Bacterial_lip_FamI.2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ05489.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiLIP_BURGL
AccessioniPrimary (citable) accession number: Q05489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 14, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally (PubMed:7786905 and PubMed:8683577) thought to originate from Chromobacterium viscosum.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.