Reviewed, UniProtKB/Swiss-Prot P41365 (LIPB_CANAR)

Names and origin

Protein names	Recommended name:     Lipase B     EC=3.1.1.3 Alternative name(s):     CALB
Organism	Candida antarctica (Yeast) (Trichosporon oryzae)
Taxonomic identifier	34362 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis.
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Ontologies

Keywords
Biological process	Lipid degradation
Domain	Signal
Molecular function	Hydrolase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	triglyceride lipase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Propeptide

19 – 25

7

PRO_0000021595

Chain

26 – 342

317

Lipase B

PRO_0000021596

Sites

Active site

130

1

Ref.3

Active site

212

1

Ref.3

Active site

249

1

Amino acid modifications

Glycosylation

99

1

N-linked (GlcNAc...) Ref.1 Ref.3

Disulfide bond

47 ↔ 89

Disulfide bond

241 ↔ 283

Disulfide bond

318 ↔ 336

Secondary structure

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342

Helix Strand Turn

Details...

Helix

38 – 43

6

Beta strand

45 – 47

3

Beta strand

56 – 62

7

Helix

69 – 73

5

Turn

74 – 76

3

Helix

77 – 82

6

Turn

83 – 85

3

Beta strand

87 – 91

5

Turn

94 – 97

4

Helix

101 – 118

18

Beta strand

124 – 129

6

Helix

131 – 142

12

Helix

144 – 146

3

Turn

147 – 149

3

Beta strand

150 – 157

8

Helix

164 – 166

3

Helix

167 – 171

5

Helix

177 – 181

5

Helix

187 – 194

8

Turn

195 – 198

4

Beta strand

204 – 208

5

Beta strand

213 – 215

3

Beta strand

220 – 222

3

Beta strand

232 – 236

5

Helix

237 – 241

5

Helix

251 – 254

4

Helix

256 – 267

12

Beta strand

269 – 272

4

Helix

275 – 277

3

Helix

280 – 282

3

Helix

293 – 300

8

Helix

303 – 312

10

Beta strand

316 – 318

3

Turn

324 – 326

3

Helix

327 – 329

3

Sequences

	Sequence		Length	Mass (Da)
	P41365-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: ACF1D83AED2E1A57	FASTA	342	35,518
	10 20 30 40 50 60 MKLLSLTGVA GVLATCVAAT PLVKRLPSGS DPAFSQPKSV LDAGLTCQGA SPSSVSKPIL 70 80 90 100 110 120 LVPGTGTTGP QSFDSNWIPL STQLGYTPCW ISPPPFMLND TQVNTEYMVN AITALYAGSG 130 140 150 160 170 180 NNKLPVLTWS QGGLVAQWGL TFFPSIRSKV DRLMAFAPDY KGTVLAGPLD ALAVSAPSVW 190 200 210 220 230 240 QQTTGSALTT ALRNAGGLTQ IVPTTNLYSA TDEIVQPQVS NSPLDSSYLF NGKNVQAQAV 250 260 270 280 290 300 CGPLFVIDHA GSLTSQFSYV VGRSALRSTT GQARSADYGI TDCNPLPAND LTPEQKVAAA 310 320 330 340 ALLAPAAAAI VAGPKQNCEP DLMPYARPFA VGKRTCSGIV TP

References

[1]	"The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica." Uppenberg J., Hansen M.T., Patkar S., Jones T.A. Structure 2:293-308(1994) [PubMed: 8087556] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), GLYCOSYLATION AT ASN-99. Strain: LF058.
[2]	Erratum Uppenberg J., Hansen M.T., Patkar S., Jones T.A. Structure 2:453-454(1994)
[3]	"Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols." Uppenberg J., Oehrner N., Norin M., Hult K., Kleywegt G.J., Patkar S., Waagen V., Anthonsen T., Jones T.A. Biochemistry 34:16838-16851(1995) [PubMed: 8527460] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), GLYCOSYLATION AT ASN-99.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z30645 Genomic DNA. Translation: CAA83122.1.

PIR

S47165.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LBS	X-ray	2.60	A/B/C/D/E/F	26-342	[»]
1LBT	X-ray	2.50	A/B	26-342	[»]
1TCA	X-ray	1.55	A	26-342	[»]
1TCB	X-ray	2.10	A/B	26-342	[»]
1TCC	X-ray	2.50	A/B	26-342	[»]
3ICV	X-ray	1.49	A	26-340	[»]
3ICW	X-ray	1.69	A	26-340	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.1.1.3. 97324.

Family and domain databases

ProtoNet

Search...

Entry information

Entry name

LIPB_CANAR

Accession

Primary (citable) accession number: P41365

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)