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Protein

Triacylglycerol lipase

Gene

lip

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

Functioni

Catalyzes the hydrolysis of triacylglycerol. It shows a preference for triacylglycerols with a chain length between 6 and 12 carbons.2 Publications

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.2 Publications

Cofactori

Ca2+6 PublicationsNote: Binds 1 Ca2+ ion per subunit.6 Publications

Enzyme regulationi

Inhibited by RC-(Rp,Sp)- and SC-(Rp,Sp)-1,2-dioctylcarbamoylglycero-3-O-p-nitrophenyl octylphosphonate (PubMed:9660188). Also inhibited by diethyl-p-nitrophenylphosphate (E600) (PubMed:1856176).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei61Substrate; via amide nitrogenCombined sources4 Publications1
Active sitei131NucleophileCombined sources6 Publications1
Binding sitei132Substrate; via amide nitrogenCombined sources4 Publications1
Metal bindingi286CalciumCombined sources6 Publications1
Active sitei308Charge relay systemCombined sources4 Publications1
Active sitei330Charge relay systemCombined sources4 Publications1
Metal bindingi332CalciumCombined sources6 Publications1
Metal bindingi336Calcium; via carbonyl oxygenCombined sources6 Publications1
Metal bindingi340Calcium; via carbonyl oxygenCombined sources6 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.1.3. 1028.

Protein family/group databases

ESTHERiburce-lipaa. Bacterial_lip_FamI.2.

Names & Taxonomyi

Protein namesi
Recommended name:
Triacylglycerol lipase1 Publication (EC:3.1.1.32 Publications)
Alternative name(s):
Extracellular lipase1 Publication
Triacylglycerol ester hydrolaseBy similarity
Gene namesi
Name:lipCurated
Synonyms:lipA1 Publication
OrganismiBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifieri292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

DrugBankiDB08419. (1S)-1-(PHENOXYMETHYL)PROPYL METHYLPHOSPHONOCHLORIDOATE.
DB06965. HEXYLPHOSPHONIC ACID (R)-2-METHYL-3-PHENYLPROPYL ESTER.
DB06966. HEXYLPHOSPHONIC ACID (S)-2-METHYL-3-PHENYLPROPYL ESTER.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 443 PublicationsAdd BLAST44
ChainiPRO_000001774045 – 364Triacylglycerol lipaseAdd BLAST320

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi234 ↔ 3141 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.2 Publications1 Publication

Structurei

Secondary structure

1364
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni46 – 49Combined sources4
Beta strandi55 – 58Combined sources4
Beta strandi61 – 64Combined sources4
Beta strandi65 – 67Combined sources3
Turni68 – 70Combined sources3
Beta strandi71 – 74Combined sources4
Helixi77 – 83Combined sources7
Beta strandi88 – 90Combined sources3
Beta strandi95 – 97Combined sources3
Beta strandi99 – 101Combined sources3
Helixi105 – 120Combined sources16
Beta strandi125 – 130Combined sources6
Helixi132 – 143Combined sources12
Helixi145 – 147Combined sources3
Beta strandi148 – 155Combined sources8
Helixi162 – 171Combined sources10
Helixi178 – 194Combined sources17
Helixi204 – 211Combined sources8
Helixi213 – 222Combined sources10
Beta strandi239 – 243Combined sources5
Beta strandi246 – 255Combined sources10
Beta strandi258 – 264Combined sources7
Beta strandi267 – 272Combined sources6
Turni277 – 279Combined sources3
Helixi282 – 285Combined sources4
Helixi288 – 300Combined sources13
Turni301 – 303Combined sources3
Beta strandi306 – 312Combined sources7
Helixi313 – 316Combined sources4
Beta strandi319 – 326Combined sources8
Helixi332 – 334Combined sources3
Turni335 – 339Combined sources5
Helixi348 – 361Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP22088.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini54 – 266AB hydrolase-1Sequence analysisAdd BLAST213

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiView protein in InterPro
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
PfamiView protein in Pfam
PF00561. Abhydrolase_1. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiView protein in PROSITE
PS00120. LIPASE_SER. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiLIP_BURCE
AccessioniPrimary (citable) accession number: P22088
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 1, 1996
Last modified: August 30, 2017
This is version 104 of the entry and version 2 of the sequence. See 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