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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)DescriptionActionsGraphical viewLength
Active sitei238Nucleophile1 Publication1
Active sitei297Charge relay system1 Publication1
Metal bindingi350CalciumBy similarity1
Active sitei351Charge relay system1 Publication1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Add BLAST24
PropeptideiPRO_000001773125 – 94Add BLAST70
ChainiPRO_000001773295 – 363LipaseAdd BLAST269

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi123 ↔ 3621 Publication
Disulfide bondi134 ↔ 1371 Publication
Disulfide bondi329 ↔ 3381 Publication

Keywords - PTMi

Disulfide bond, Zymogen

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi100 – 102Combined sources3
Helixi105 – 120Combined sources16
Turni124 – 129Combined sources6
Helixi135 – 138Combined sources4
Turni139 – 142Combined sources4
Beta strandi143 – 150Combined sources8
Beta strandi152 – 154Combined sources3
Beta strandi157 – 163Combined sources7
Turni164 – 167Combined sources4
Beta strandi168 – 173Combined sources6
Helixi179 – 185Combined sources7
Beta strandi190 – 192Combined sources3
Beta strandi200 – 202Combined sources3
Helixi203 – 226Combined sources24
Beta strandi230 – 237Combined sources8
Helixi239 – 253Combined sources15
Turni260 – 262Combined sources3
Beta strandi263 – 269Combined sources7
Helixi276 – 284Combined sources9
Beta strandi289 – 294Combined sources6
Helixi299 – 301Combined sources3
Helixi305 – 307Combined sources3
Beta strandi312 – 320Combined sources9
Turni321 – 324Combined sources4
Beta strandi325 – 329Combined sources5
Beta strandi336 – 338Combined sources3
Helixi339 – 342Combined sources4
Helixi349 – 352Combined sources4
Beta strandi357 – 361Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TGLX-ray1.90A95-362[»]
3TGLX-ray1.90A95-363[»]
4TGLX-ray2.60A95-363[»]
5TGLX-ray3.00A95-363[»]
ProteinModelPortaliP19515.
SMRiP19515.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TGLX-ray1.90A95-362[»]
3TGLX-ray1.90A95-363[»]
4TGLX-ray2.60A95-363[»]
5TGLX-ray3.00A95-363[»]
ProteinModelPortaliP19515.
SMRiP19515.
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: November 2, 2016
This is version 85 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.