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Protein

Lipase

Gene
N/A
Organism
Rhizopus niveus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes ester bonds of triglycerides as well as of their derived partial glycerides with a strong 1,3-positional specificity.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Enzyme regulationi

Lipase activity is maximal at a lipid-water interface (interfacial activation), probably by an induced conformational change that results in an increased accessibility of the active site to the substrate.

pH dependencei

Optimum pH is 6.0-6.5.2 Publications

Temperature dependencei

Optimum temperature is 35 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei268 – 2681Nucleophile1 Publication
Active sitei327 – 3271Charge relay system1 Publication
Metal bindingi379 – 3791CalciumBy similarity
Active sitei380 – 3801Charge relay system1 Publication

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

ESTHERirhidl-lipas. Lipase_3.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase (EC:3.1.1.3)
Alternative name(s):
Lipase II
RNL
Triacylglycerol lipase
OrganismiRhizopus niveus
Taxonomic identifieri4844 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi313 – 3131E → V: Increases the optimum temperature to 50 degrees Celsius. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Propeptidei27 – 95691 PublicationPRO_0000017733Add
BLAST
Chaini96 – 392297LipasePRO_0000017734Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi152 ↔ 3911 Publication
Disulfide bondi163 ↔ 1661 Publication
Disulfide bondi358 ↔ 3671 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi129 – 1313Combined sources
Helixi134 – 14916Combined sources
Turni153 – 1586Combined sources
Helixi164 – 1696Combined sources
Beta strandi174 – 1818Combined sources
Turni182 – 1854Combined sources
Beta strandi186 – 1938Combined sources
Turni194 – 1974Combined sources
Beta strandi198 – 2047Combined sources
Helixi210 – 2145Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi230 – 2323Combined sources
Helixi233 – 25624Combined sources
Beta strandi261 – 2677Combined sources
Helixi269 – 28416Combined sources
Turni290 – 2923Combined sources
Beta strandi293 – 2997Combined sources
Helixi306 – 31510Combined sources
Beta strandi319 – 3246Combined sources
Helixi329 – 3313Combined sources
Helixi335 – 3373Combined sources
Beta strandi342 – 3509Combined sources
Turni351 – 3533Combined sources
Beta strandi354 – 3585Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi365 – 3673Combined sources
Helixi368 – 3703Combined sources
Helixi378 – 3814Combined sources
Beta strandi386 – 3905Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LGYX-ray2.20A/B/C124-392[»]
ProteinModelPortaliP61871.
SMRiP61871. Positions 128-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61871.

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.
[Graphical view]
PfamiPF01764. 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.

P61871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFISISQG VSLCLLVSSM MLGSSAVPVS GKSGSSNTAV SASDNAALPP
60 70 80 90 100
LISSRCAPPS NKGSKSDLQA EPYNMQKNTE WYESHGGNLT SIGKRDDNLV
110 120 130 140 150
GGMTLDLPSD APPISLSSST NSASDGGKVV AATTAQIQEF TKYAGIAATA
160 170 180 190 200
YCRSVVPGNK WDCVQCQKWV PDGKIITTFT SLLSDTNGYV LRSDKQKTIY
210 220 230 240 250
LVFRGTNSFR SAITDIVFNF SDYKPVKGAK VHAGFLSSYE QVVNDYFPVV
260 270 280 290 300
QEQLTAHPTY KVIVTGHSLG GAQALLAGMD LYQREPRLSP KNLSIFTVGG
310 320 330 340 350
PRVGNPTFAY YVESTGIPFQ RTVHKRDIVP HVPPQSFGFL HPGVESWIKS
360 370 380 390
GTSNVQICTS EIETKDCSNS IVPFTSILDH LSYFDINEGS CL
Length:392
Mass (Da):42,139
Last modified:June 7, 2004 - v1
Checksum:iD08F651EE77AA5A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti348 – 3481I → M in AAC60540 (PubMed:1368341).Curated
Sequence conflicti348 – 3481I → M in BAA02181 (PubMed:1368341).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013496 Genomic DNA. Translation: BAA31548.1.
D13206 Genomic DNA. Translation: BAA02493.1.
S39525 mRNA. Translation: AAC60540.2.
D12680 mRNA. Translation: BAA02181.1.
PIRiJT0604.
PC2171.
PC2172.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013496 Genomic DNA. Translation: BAA31548.1.
D13206 Genomic DNA. Translation: BAA02493.1.
S39525 mRNA. Translation: AAC60540.2.
D12680 mRNA. Translation: BAA02181.1.
PIRiJT0604.
PC2171.
PC2172.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LGYX-ray2.20A/B/C124-392[»]
ProteinModelPortaliP61871.
SMRiP61871. Positions 128-392.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERirhidl-lipas. Lipase_3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP61871.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
[Graphical view]
PfamiPF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "High-level expression of Rhizopus niveus lipase in the yeast Saccharomyces cerevisiae and structural properties of the expressed enzyme."
    Kohno M., Enatsu M., Yoshiizumi M., Kugimiya W.
    Protein Expr. Purif. 15:327-335(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Primary structure of Rhizopus niveus lipase from DNA and protein analyses."
    Kugimiya W., Kohno M., Sasaki M., Hashimoto Y., Morita Y.
    Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning and sequence analysis of cDNA encoding Rhizopus niveus lipase."
    Kugimiya W., Otani Y., Kohno M., Hashimoto Y.
    Biosci. Biotechnol. Biochem. 56:716-719(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 96-392.
  4. "Purification, characterization, and crystallization of two types of lipase from Rhizopus niveus."
    Kohno M., Kugimiya W., Hashimoto Y., Morita Y.
    Biosci. Biotechnol. Biochem. 58:1007-1012(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 44-53; 96-105 AND 124-134, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: NBRC 4759 / AS 3.4816.
  5. "Improvement of the optimum temperature of lipase activity for Rhizopus niveus by random mutagenesis and its structural interpretation."
    Kohno M., Enatsu M., Funatsu J., Yoshiizumi M., Kugimiya W.
    J. Biotechnol. 87:203-210(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-313, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "The crystal structure of lipase II from Rhizopus niveus at 2.2-A resolution."
    Kohno M., Funatsu J., Mikami B., Kugimiya W., Matsuo T., Morita Y.
    J. Biochem. 120:505-510(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 124-392, ACTIVE SITES, DISULFIDE BOND.
    Strain: NBRC 4759 / AS 3.4816.

Entry informationi

Entry nameiLIP_RHINI
AccessioniPrimary (citable) accession number: P61871
Secondary accession number(s): O74166, P21811, Q12237
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 13, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Limited proteolysis produces a smaller peptide starting at residue Ser-124, that has altered substrate specificity and biophysicochemical properties.

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.