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Protein

Lipase

Gene

LIP

Organism
Thermomyces lanuginosus (Humicola lanuginosa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

pH dependencei

Active at alkaline pHs (up to pH 12 approximately).

Temperature dependencei

Active over a broad temperature range.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei168Nucleophile1 Publication1
Active sitei223Charge relay system1 Publication1
Active sitei280Charge relay system1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.3. 2711.
SABIO-RKO59952.

Protein family/group databases

ESTHERihumla-1lipa. Lipase_3.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase (EC:3.1.1.3)
Alternative name(s):
Triacylglycerol lipase
Gene namesi
Name:LIP
OrganismiThermomyces lanuginosus (Humicola lanuginosa)
Taxonomic identifieri5541 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeThermomyces

Pathology & Biotechi

Biotechnological usei

Used as a detergent lipase. Sold under the name Lipolase by Novozymes. Engineered variants are sold under the names Lipolase Ultra and LipoPrime.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi109E → A: 35-70% of wild-type activity. 1 Publication1
Mutagenesisi111W → E, F, G or L: Altered chain length specificity. 2 Publications1
Mutagenesisi168S → A: Decrease in liposome binding. 1 Publication1

Protein family/group databases

Allergomei904. The l Lipase.

Chemistry databases

ChEMBLiCHEMBL2021756.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000001773718 – 225
ChainiPRO_000001773823 – 291LipaseAdd BLAST269

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi44 ↔ 2901 Publication
Disulfide bondi58 ↔ 631 Publication
Disulfide bondi126 ↔ 1291 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Structurei

Secondary structure

1291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 41Combined sources16
Helixi45 – 47Combined sources3
Beta strandi52 – 55Combined sources4
Helixi59 – 61Combined sources3
Helixi64 – 68Combined sources5
Beta strandi72 – 80Combined sources9
Turni81 – 84Combined sources4
Beta strandi85 – 92Combined sources8
Turni93 – 96Combined sources4
Beta strandi97 – 102Combined sources6
Beta strandi106 – 108Combined sources3
Helixi109 – 112Combined sources4
Beta strandi119 – 121Combined sources3
Turni123 – 125Combined sources3
Beta strandi130 – 132Combined sources3
Helixi133 – 156Combined sources24
Beta strandi160 – 167Combined sources8
Helixi169 – 181Combined sources13
Beta strandi184 – 186Combined sources3
Beta strandi188 – 194Combined sources7
Helixi201 – 209Combined sources9
Beta strandi211 – 213Combined sources3
Beta strandi215 – 220Combined sources6
Helixi225 – 227Combined sources3
Helixi231 – 233Combined sources3
Beta strandi241 – 244Combined sources4
Helixi254 – 256Combined sources3
Beta strandi257 – 260Combined sources4
Beta strandi266 – 269Combined sources4
Beta strandi271 – 273Combined sources3
Helixi278 – 281Combined sources4
Beta strandi282 – 286Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DT3X-ray2.60A/B23-291[»]
1DT5X-ray2.40A/B/C/D/E/F/G/H23-291[»]
1DTEX-ray2.35A/B23-291[»]
1DU4X-ray2.50A/B/C/D23-291[»]
1EINX-ray3.00A/B/C23-291[»]
1GT6X-ray2.20A/B23-291[»]
1TIBX-ray1.84A23-291[»]
4DYHX-ray2.00A/B23-291[»]
4EA6X-ray2.30A/B23-291[»]
4FLFX-ray2.15A/B23-291[»]
4GBGX-ray2.90A/B23-291[»]
4GHWX-ray2.60A/B23-291[»]
4GI1X-ray2.43A/B23-291[»]
4GLBX-ray2.69A/B23-291[»]
4GWLX-ray2.55A/B23-291[»]
4KJXX-ray2.10A/B23-291[»]
4N8SX-ray2.30A/B23-291[»]
4S0XX-ray2.10A/B23-291[»]
4ZGBX-ray2.30A/B23-291[»]
5AP9X-ray1.80A/B23-291[»]
ProteinModelPortaliO59952.
SMRiO59952.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59952.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
IPR005592. Mono/diacylglycerol_lipase_N.
[Graphical view]
PfamiPF03893. Lipase3_N. 1 hit.
PF01764. Lipase_3. 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.

O59952-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSSLVLFFV SAWTALASPI RREVSQDLFN QFNLFAQYSA AAYCGKNNDA
60 70 80 90 100
PAGTNITCTG NACPEVEKAD ATFLYSFEDS GVGDVTGFLA LDNTNKLIVL
110 120 130 140 150
SFRGSRSIEN WIGNLNFDLK EINDICSGCR GHDGFTSSWR SVADTLRQKV
160 170 180 190 200
EDAVREHPDY RVVFTGHSLG GALATVAGAD LRGNGYDIDV FSYGAPRVGN
210 220 230 240 250
RAFAEFLTVQ TGGTLYRITH TNDIVPRLPP REFGYSHSSP EYWIKSGTLV
260 270 280 290
PVTRNDIVKI EGIDATGGNN QPNIPDIPAH LWYFGLIGTC L
Length:291
Mass (Da):31,807
Last modified:August 1, 1998 - v1
Checksum:i170ACEDF791DB07B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054513 mRNA. Translation: AAC08588.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054513 mRNA. Translation: AAC08588.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DT3X-ray2.60A/B23-291[»]
1DT5X-ray2.40A/B/C/D/E/F/G/H23-291[»]
1DTEX-ray2.35A/B23-291[»]
1DU4X-ray2.50A/B/C/D23-291[»]
1EINX-ray3.00A/B/C23-291[»]
1GT6X-ray2.20A/B23-291[»]
1TIBX-ray1.84A23-291[»]
4DYHX-ray2.00A/B23-291[»]
4EA6X-ray2.30A/B23-291[»]
4FLFX-ray2.15A/B23-291[»]
4GBGX-ray2.90A/B23-291[»]
4GHWX-ray2.60A/B23-291[»]
4GI1X-ray2.43A/B23-291[»]
4GLBX-ray2.69A/B23-291[»]
4GWLX-ray2.55A/B23-291[»]
4KJXX-ray2.10A/B23-291[»]
4N8SX-ray2.30A/B23-291[»]
4S0XX-ray2.10A/B23-291[»]
4ZGBX-ray2.30A/B23-291[»]
5AP9X-ray1.80A/B23-291[»]
ProteinModelPortaliO59952.
SMRiO59952.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL2021756.

Protein family/group databases

Allergomei904. The l Lipase.
ESTHERihumla-1lipa. Lipase_3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.1.3. 2711.
SABIO-RKO59952.

Miscellaneous databases

EvolutionaryTraceiO59952.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
IPR005592. Mono/diacylglycerol_lipase_N.
[Graphical view]
PfamiPF03893. Lipase3_N. 1 hit.
PF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIP_THELA
AccessioniPrimary (citable) accession number: O59952
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.