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Protein

Lipase B

Gene
N/A
Organism
Pseudozyma antarctica (Yeast) (Candida antarctica)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1301 Publication1
Active sitei2121 Publication1
Active sitei2491

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Protein family/group databases

ESTHERicanar-LipB. Canar_LipB.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase B (EC:3.1.1.3)
Alternative name(s):
CALB
OrganismiPseudozyma antarctica (Yeast) (Candida antarctica)
Taxonomic identifieri84753 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeMoesziomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000002159519 – 257
ChainiPRO_000002159626 – 342Lipase BAdd BLAST317

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi47 ↔ 89
Glycosylationi99N-linked (GlcNAc...)2 Publications1
Disulfide bondi241 ↔ 283
Disulfide bondi318 ↔ 336

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Structurei

Secondary structure

1342
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 43Combined sources6
Beta strandi45 – 47Combined sources3
Helixi52 – 54Combined sources3
Beta strandi56 – 62Combined sources7
Helixi69 – 73Combined sources5
Turni74 – 76Combined sources3
Helixi77 – 83Combined sources7
Beta strandi87 – 91Combined sources5
Turni94 – 97Combined sources4
Helixi101 – 118Combined sources18
Beta strandi124 – 129Combined sources6
Helixi131 – 142Combined sources12
Helixi144 – 146Combined sources3
Turni147 – 149Combined sources3
Beta strandi150 – 157Combined sources8
Helixi164 – 166Combined sources3
Helixi167 – 171Combined sources5
Helixi177 – 181Combined sources5
Helixi187 – 194Combined sources8
Turni195 – 198Combined sources4
Beta strandi204 – 208Combined sources5
Beta strandi213 – 215Combined sources3
Beta strandi220 – 222Combined sources3
Beta strandi232 – 236Combined sources5
Helixi237 – 241Combined sources5
Helixi251 – 254Combined sources4
Helixi256 – 267Combined sources12
Beta strandi269 – 272Combined sources4
Helixi275 – 277Combined sources3
Helixi280 – 282Combined sources3
Beta strandi286 – 288Combined sources3
Helixi293 – 300Combined sources8
Helixi303 – 312Combined sources10
Beta strandi316 – 318Combined sources3
Turni324 – 326Combined sources3
Helixi327 – 329Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LBSX-ray2.60A/B/C/D/E/F26-342[»]
1LBTX-ray2.50A/B26-342[»]
1TCAX-ray1.55A26-342[»]
1TCBX-ray2.10A/B26-342[»]
1TCCX-ray2.50A/B26-342[»]
3ICVX-ray1.49A26-340[»]
3ICWX-ray1.69A26-340[»]
3W9BX-ray2.90A/B/C/D26-342[»]
4K5QX-ray1.49A26-342[»]
4K6GX-ray1.50A/B26-342[»]
4K6HX-ray1.60A/B26-342[»]
4K6KX-ray1.60A/B26-342[»]
4ZV7X-ray2.00A26-342[»]
5A6VX-ray2.28A/B26-342[»]
5A71X-ray0.91A/B26-342[»]
ProteinModelPortaliP41365.
SMRiP41365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41365.

Family & Domainsi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P41365-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLSLTGVA GVLATCVAAT PLVKRLPSGS DPAFSQPKSV LDAGLTCQGA
60 70 80 90 100
SPSSVSKPIL LVPGTGTTGP QSFDSNWIPL STQLGYTPCW ISPPPFMLND
110 120 130 140 150
TQVNTEYMVN AITALYAGSG NNKLPVLTWS QGGLVAQWGL TFFPSIRSKV
160 170 180 190 200
DRLMAFAPDY KGTVLAGPLD ALAVSAPSVW QQTTGSALTT ALRNAGGLTQ
210 220 230 240 250
IVPTTNLYSA TDEIVQPQVS NSPLDSSYLF NGKNVQAQAV CGPLFVIDHA
260 270 280 290 300
GSLTSQFSYV VGRSALRSTT GQARSADYGI TDCNPLPAND LTPEQKVAAA
310 320 330 340
ALLAPAAAAI VAGPKQNCEP DLMPYARPFA VGKRTCSGIV TP
Length:342
Mass (Da):35,518
Last modified:November 1, 1995 - v1
Checksum:iACF1D83AED2E1A57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30645 Genomic DNA. Translation: CAA83122.1.
PIRiS47165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30645 Genomic DNA. Translation: CAA83122.1.
PIRiS47165.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LBSX-ray2.60A/B/C/D/E/F26-342[»]
1LBTX-ray2.50A/B26-342[»]
1TCAX-ray1.55A26-342[»]
1TCBX-ray2.10A/B26-342[»]
1TCCX-ray2.50A/B26-342[»]
3ICVX-ray1.49A26-340[»]
3ICWX-ray1.69A26-340[»]
3W9BX-ray2.90A/B/C/D26-342[»]
4K5QX-ray1.49A26-342[»]
4K6GX-ray1.50A/B26-342[»]
4K6HX-ray1.60A/B26-342[»]
4K6KX-ray1.60A/B26-342[»]
4ZV7X-ray2.00A26-342[»]
5A6VX-ray2.28A/B26-342[»]
5A71X-ray0.91A/B26-342[»]
ProteinModelPortaliP41365.
SMRiP41365.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERicanar-LipB. Canar_LipB.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP41365.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLIPB_PSEA2
AccessioniPrimary (citable) accession number: P41365
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
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

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.