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O59952

- LIP_THELA

UniProt

O59952 - LIP_THELA

Protein

Lipase

Gene

LIP

Organism
Thermomyces lanuginosus (Humicola lanuginosa)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    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 – 1681Nucleophile1 Publication
    Active sitei223 – 2231Charge relay system1 PublicationPROSITE-ProRule annotation
    Active sitei280 – 2801Charge relay system1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. triglyceride lipase activity Source: UniProtKB-EC

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW

    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. 2 Publications
    Mutagenesisi111 – 1111W → E, F, G or L: Altered chain length specificity. 3 Publications
    Mutagenesisi168 – 1681S → A: Decrease in liposome binding. 2 Publications

    Protein family/group databases

    Allergomei904. The l Lipase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    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.
    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. 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), ACTIVE SITE.
    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: October 1, 2014
    This is version 82 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