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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei130 – 13011 Publication
Active sitei212 – 21211 Publication
Active sitei249 – 2491

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 257PRO_0000021595
Chaini26 – 342317Lipase BPRO_0000021596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 89
Glycosylationi99 – 991N-linked (GlcNAc...)2 Publications
Disulfide bondi241 ↔ 283
Disulfide bondi318 ↔ 336

Keywords - PTMi

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

Structurei

Secondary structure

1
342
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 436Combined sources
Beta strandi45 – 473Combined sources
Helixi52 – 543Combined sources
Beta strandi56 – 627Combined sources
Helixi69 – 735Combined sources
Turni74 – 763Combined sources
Helixi77 – 837Combined sources
Beta strandi87 – 915Combined sources
Turni94 – 974Combined sources
Helixi101 – 11818Combined sources
Beta strandi124 – 1296Combined sources
Helixi131 – 14212Combined sources
Helixi144 – 1463Combined sources
Turni147 – 1493Combined sources
Beta strandi150 – 1578Combined sources
Helixi164 – 1663Combined sources
Helixi167 – 1715Combined sources
Helixi177 – 1815Combined sources
Helixi187 – 1948Combined sources
Turni195 – 1984Combined sources
Beta strandi204 – 2085Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi232 – 2365Combined sources
Helixi237 – 2415Combined sources
Helixi251 – 2544Combined sources
Helixi256 – 26712Combined sources
Beta strandi269 – 2724Combined sources
Helixi275 – 2773Combined sources
Helixi280 – 2823Combined sources
Beta strandi286 – 2883Combined sources
Helixi293 – 3008Combined sources
Helixi303 – 31210Combined sources
Beta strandi316 – 3183Combined sources
Turni324 – 3263Combined sources
Helixi327 – 3293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 26-342.
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
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. Positions 26-342.
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: April 13, 2016
This is version 79 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.