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O59952

- LIP_THELA

UniProt

O59952 - LIP_THELA

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Protein

Lipase

Gene
LIP
Organism
Thermomyces lanuginosus (Humicola lanuginosa)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei168 – 1681Nucleophile
Active sitei223 – 2231Charge relay system By similarity
Active sitei280 – 2801Charge relay system By similarity

GO - Molecular functioni

  1. 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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091E → A: 35-70% of wild-type activity. 1 Publication
Mutagenesisi111 – 1111W → E, F, G or L: Altered chain length specificity. 2 Publications
Mutagenesisi168 – 1681S → A: Decrease in liposome binding. 1 Publication

Protein family/group databases

Allergomei904. The l Lipase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed predictionAdd
BLAST
Propeptidei18 – 225PRO_0000017737
Chaini23 – 291269LipasePRO_0000017738Add
BLAST

Keywords - PTMi

Cleavage on pair of basic residues, Zymogen

Structurei

Secondary structure

1
291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 4116
Helixi45 – 473
Beta strandi52 – 554
Helixi59 – 613
Helixi64 – 685
Beta strandi72 – 809
Turni81 – 844
Beta strandi85 – 928
Turni93 – 964
Beta strandi97 – 1026
Helixi109 – 1124
Beta strandi119 – 1213
Turni123 – 1253
Beta strandi130 – 1323
Helixi133 – 15624
Beta strandi160 – 1678
Helixi169 – 18113
Beta strandi184 – 1863
Beta strandi188 – 1947
Helixi201 – 2099
Beta strandi211 – 2133
Beta strandi215 – 2206
Helixi225 – 2273
Helixi231 – 2333
Beta strandi241 – 2444
Helixi254 – 2563
Beta strandi257 – 2604
Beta strandi266 – 2694
Beta strandi271 – 2733
Helixi278 – 2814
Beta strandi282 – 2865

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO59952.
SMRiO59952. Positions 23-291.

Miscellaneous databases

EvolutionaryTraceiO59952.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Lipase_3.
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

MRSSLVLFFV SAWTALASPI RREVSQDLFN QFNLFAQYSA AAYCGKNNDA    50
PAGTNITCTG NACPEVEKAD ATFLYSFEDS GVGDVTGFLA LDNTNKLIVL 100
SFRGSRSIEN WIGNLNFDLK EINDICSGCR GHDGFTSSWR SVADTLRQKV 150
EDAVREHPDY RVVFTGHSLG GALATVAGAD LRGNGYDIDV FSYGAPRVGN 200
RAFAEFLTVQ TGGTLYRITH TNDIVPRLPP REFGYSHSSP EYWIKSGTLV 250
PVTRNDIVKI EGIDATGGNN QPNIPDIPAH LWYFGLIGTC L 291
Length:291
Mass (Da):31,807
Last modified:August 1, 1998 - v1
Checksum:i170ACEDF791DB07B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF054513 mRNA. Translation: AAC08588.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF054513 mRNA. Translation: AAC08588.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DT3 X-ray 2.60 A/B 23-291 [» ]
1DT5 X-ray 2.40 A/B/C/D/E/F/G/H 23-291 [» ]
1DTE X-ray 2.35 A/B 23-291 [» ]
1DU4 X-ray 2.50 A/B/C/D 23-291 [» ]
1EIN X-ray 3.00 A/B/C 23-291 [» ]
1GT6 X-ray 2.20 A/B 23-291 [» ]
1TIB X-ray 1.84 A 23-291 [» ]
4DYH X-ray 2.00 A/B 23-291 [» ]
4EA6 X-ray 2.30 A/B 23-291 [» ]
4FLF X-ray 2.15 A/B 23-291 [» ]
4GBG X-ray 2.90 A/B 23-291 [» ]
4GHW X-ray 2.60 A/B 23-291 [» ]
4GI1 X-ray 2.43 A/B 23-291 [» ]
4GLB X-ray 2.69 A/B 23-291 [» ]
4GWL X-ray 2.55 A/B 23-291 [» ]
4KJX X-ray 2.10 A/B 23-291 [» ]
4N8S X-ray 2.30 A/B 23-291 [» ]
ProteinModelPortali O59952.
SMRi O59952. Positions 23-291.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2021756.

Protein family/group databases

Allergomei 904. The l Lipase.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O59952.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002921. Lipase_3.
IPR005592. Mono/diacylglycerol_lipase_N.
[Graphical view ]
Pfami PF03893. Lipase3_N. 1 hit.
PF01764. Lipase_3. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00120. LIPASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Wild type Humicola lanuginosa cDNA encoding a lipolytic enzyme."
    Boel E., Muller S., Sandal T., Kamp-Hansen P., Dalboge H.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Trp89 in the lid of Humicola lanuginosa lipase is important for efficient hydrolysis of tributyrin."
    Holmquist M., Martinelle M., Clausen I.G., Patkar S.A., Svendsen A., Hult K.
    Lipids 29:599-603(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TRP-111.
  3. "The importance of non-charged amino acids in antibody binding to Humicola lanuginosa lipase."
    Naver H., Lovborg U.
    Scand. J. Immunol. 41:443-448(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  4. "The role of Glu87 and Trp89 in the lid of Humicola lanuginosa lipase."
    Martinelle M., Holmquist M., Clausen I.G., Patkar S.A., Svendsen A., Hult K.
    Protein Eng. 9:519-524(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-109 AND TRP-111.
  5. "Active serine involved in the stabilization of the active site loop in the Humicola lanuginosa lipase."
    Peters G.H., Svendsen A., Langberg H., Vind J., Patkar S.A., Toxvaerd S., Kinnunen P.K.J.
    Biochemistry 37:12375-12383(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-168.
  6. "Conformational lability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar."
    Derewenda U., Swenson L., Wei Y., Green R., Kobos P.M., Joerger R., Haas M.J., Derewenda Z.S.
    J. Lipid Res. 35:524-534(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS).
  7. "Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase."
    Brzozowski A.M., Savage H., Verma C.S., Turkenburg J.P., Lawson D.M., Svendsen A., Patkar S.A.
    Biochemistry 39:15071-15082(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-291.

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: June 11, 2014
This is version 81 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

External Data

Dasty 3

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