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Protein

Lipase

Gene
N/A
Organism
Rhizomucor miehei
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei238 – 2381Nucleophile1 Publication
Active sitei297 – 2971Charge relay system1 Publication
Metal bindingi350 – 3501CalciumBy similarity
Active sitei351 – 3511Charge 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

Enzyme and pathway databases

SABIO-RKP19515.

Protein family/group databases

ESTHERirhimi-lipas. Lipase_3.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase (EC:3.1.1.3)
Alternative name(s):
Triacylglycerol lipase
OrganismiRhizomucor miehei
Taxonomic identifieri4839 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisMucoromycotinaMucoralesLichtheimiaceaeRhizomucor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Propeptidei25 – 9470PRO_0000017731Add
BLAST
Chaini95 – 363269LipasePRO_0000017732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi123 ↔ 3621 Publication
Disulfide bondi134 ↔ 1371 Publication
Disulfide bondi329 ↔ 3381 Publication

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

Secondary structure

1
363
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi100 – 1023Combined sources
Helixi105 – 12016Combined sources
Turni124 – 1296Combined sources
Helixi135 – 1384Combined sources
Turni139 – 1424Combined sources
Beta strandi143 – 1508Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi157 – 1637Combined sources
Turni164 – 1674Combined sources
Beta strandi168 – 1736Combined sources
Helixi179 – 1857Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi200 – 2023Combined sources
Helixi203 – 22624Combined sources
Beta strandi230 – 2378Combined sources
Helixi239 – 25315Combined sources
Turni260 – 2623Combined sources
Beta strandi263 – 2697Combined sources
Helixi276 – 2849Combined sources
Beta strandi289 – 2946Combined sources
Helixi299 – 3013Combined sources
Helixi305 – 3073Combined sources
Beta strandi312 – 3209Combined sources
Turni321 – 3244Combined sources
Beta strandi325 – 3295Combined sources
Beta strandi336 – 3383Combined sources
Helixi339 – 3424Combined sources
Helixi349 – 3524Combined sources
Beta strandi357 – 3615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TGLX-ray1.90A95-362[»]
3TGLX-ray1.90A95-363[»]
4TGLX-ray2.60A95-363[»]
5TGLX-ray3.00A95-363[»]
ProteinModelPortaliP19515.
SMRiP19515. Positions 99-363.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19515.

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.

P19515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLKQRANYL GFLIVFFTAF LVEAVPIKRQ SNSTVDSLPP LIPSRTSAPS
60 70 80 90 100
SSPSTTDPEA PAMSRNGPLP SDVETKYGMA LNATSYPDSV VQAMSIDGGI
110 120 130 140 150
RAATSQEINE LTYYTTLSAN SYCRTVIPGA TWDCIHCDAT EDLKIIKTWS
160 170 180 190 200
TLIYDTNAMV ARGDSEKTIY IVFRGSSSIR NWIADLTFVP VSYPPVSGTK
210 220 230 240 250
VHKGFLDSYG EVQNELVATV LDQFKQYPSY KVAVTGHSLG GATALLCALD
260 270 280 290 300
LYQREEGLSS SNLFLYTQGQ PRVGDPAFAN YVVSTGIPYR RTVNERDIVP
310 320 330 340 350
HLPPAAFGFL HAGEEYWITD NSPETVQVCT SDLETSDCSN SIVPFTSVLD
360
HLSYFGINTG LCT
Length:363
Mass (Da):39,602
Last modified:October 1, 1993 - v2
Checksum:iDAB3C66E024F0E39
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TGLX-ray1.90A95-362[»]
3TGLX-ray1.90A95-363[»]
4TGLX-ray2.60A95-363[»]
5TGLX-ray3.00A95-363[»]
ProteinModelPortaliP19515.
SMRiP19515. Positions 99-363.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERirhimi-lipas. Lipase_3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP19515.

Miscellaneous databases

EvolutionaryTraceiP19515.

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...

Entry informationi

Entry nameiLIP_RHIMI
AccessioniPrimary (citable) accession number: P19515
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1993
Last modified: April 13, 2016
This is version 83 of the entry and version 2 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.