Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei126Nucleophile1
Metal bindingi280Calcium1
Active sitei302Charge relay system1
Active sitei324Charge relay system1
Metal bindingi326Calcium1
Metal bindingi330Calcium1
Metal bindingi334Calcium; via carbonyl oxygen1

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)DescriptionActionsGraphical viewLength
Mutagenesisi54H → A: No loss of activity. 1 Publication1
Mutagenesisi126S → A: Complete loss of activity. 1 Publication1
Mutagenesisi160D → A: No loss of activity. 1 Publication1
Mutagenesisi160D → E: No loss of activity. 1 Publication1
Mutagenesisi280D → A: Complete loss of activity. 1 Publication1
Mutagenesisi280D → E: No loss of activity. 1 Publication1
Mutagenesisi302D → A: 75% loss of activity. 1 Publication1
Mutagenesisi302D → E: No loss of activity. 1 Publication1
Mutagenesisi324H → A: Complete loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 392 PublicationsAdd BLAST39
ChainiPRO_000001774140 – 358LipaseAdd BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactor.

Structurei

Secondary structure

1358
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi50 – 53Combined sources4
Beta strandi58 – 62Combined sources5
Turni63 – 65Combined sources3
Beta strandi66 – 69Combined sources4
Helixi72 – 78Combined sources7
Beta strandi83 – 85Combined sources3
Beta strandi94 – 96Combined sources3
Helixi100 – 115Combined sources16
Beta strandi120 – 125Combined sources6
Helixi128 – 138Combined sources11
Helixi140 – 142Combined sources3
Beta strandi143 – 150Combined sources8
Helixi157 – 166Combined sources10
Helixi176 – 186Combined sources11
Helixi195 – 201Combined sources7
Helixi202 – 206Combined sources5
Helixi208 – 217Combined sources10
Turni226 – 228Combined sources3
Beta strandi234 – 238Combined sources5
Beta strandi241 – 250Combined sources10
Beta strandi253 – 255Combined sources3
Beta strandi264 – 267Combined sources4
Helixi276 – 279Combined sources4
Helixi282 – 295Combined sources14
Beta strandi300 – 306Combined sources7
Helixi307 – 310Combined sources4
Beta strandi313 – 320Combined sources8
Helixi326 – 328Combined sources3
Turni329 – 333Combined sources5
Helixi342 – 355Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ05489.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini48 – 327AB hydrolase-1Sequence analysisAdd BLAST280

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)DescriptionActionsGraphical viewLength
Sequence conflicti40A → W AA sequence (PubMed:7786905).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29069N.
IntActiQ05489. 1 interactor.

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: November 2, 2016
This is version 106 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.