LIPB_PSEA2
ID LIPB_PSEA2 Reviewed; 342 AA.
AC P41365;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Lipase B;
DE EC=3.1.1.3;
DE AltName: Full=CALB;
DE Flags: Precursor;
OS Pseudozyma antarctica (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=84753;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS),
RP AND GLYCOSYLATION AT ASN-99.
RC STRAIN=LF058;
RX PubMed=8087556; DOI=10.1016/s0969-2126(00)00031-9;
RA Uppenberg J., Hansen M.T., Patkar S., Jones T.A.;
RT "The sequence, crystal structure determination and refinement of two
RT crystal forms of lipase B from Candida antarctica.";
RL Structure 2:293-308(1994).
RN [2]
RP ERRATUM OF PUBMED:8087556.
RA Uppenberg J., Hansen M.T., Patkar S., Jones T.A.;
RL Structure 2:453-454(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND GLYCOSYLATION AT ASN-99.
RX PubMed=8527460; DOI=10.1021/bi00051a035;
RA Uppenberg J., Oehrner N., Norin M., Hult K., Kleywegt G.J., Patkar S.,
RA Waagen V., Anthonsen T., Jones T.A.;
RT "Crystallographic and molecular-modeling studies of lipase B from Candida
RT antarctica reveal a stereospecificity pocket for secondary alcohols.";
RL Biochemistry 34:16838-16851(1995).
CC -!- FUNCTION: Hydrolysis of triglycerides. Is very stereospecific both in
CC hydrolysis and in organic synthesis and has a potentially important
CC application in glucolipid synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
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DR EMBL; Z30645; CAA83122.1; -; Genomic_DNA.
DR PIR; S47165; S47165.
DR PDB; 1LBS; X-ray; 2.60 A; A/B/C/D/E/F=26-342.
DR PDB; 1LBT; X-ray; 2.50 A; A/B=26-342.
DR PDB; 1TCA; X-ray; 1.55 A; A=26-342.
DR PDB; 1TCB; X-ray; 2.10 A; A/B=26-342.
DR PDB; 1TCC; X-ray; 2.50 A; A/B=26-342.
DR PDB; 3ICV; X-ray; 1.49 A; A=26-340.
DR PDB; 3ICW; X-ray; 1.69 A; A=26-340.
DR PDB; 3W9B; X-ray; 2.90 A; A/B/C/D=26-342.
DR PDB; 4K5Q; X-ray; 1.49 A; A=26-342.
DR PDB; 4K6G; X-ray; 1.50 A; A/B=26-342.
DR PDB; 4K6H; X-ray; 1.60 A; A/B=26-342.
DR PDB; 4K6K; X-ray; 1.60 A; A/B=26-342.
DR PDB; 4ZV7; X-ray; 2.00 A; A=26-342.
DR PDB; 5A6V; X-ray; 2.28 A; A/B=26-342.
DR PDB; 5A71; X-ray; 0.91 A; A/B=26-342.
DR PDB; 5GV5; X-ray; 2.89 A; A/B/C/D/E/F/G/H=26-342.
DR PDB; 6ISP; X-ray; 1.88 A; A/B/C/D=26-342.
DR PDB; 6ISQ; X-ray; 1.86 A; A/B=26-342.
DR PDB; 6ISR; X-ray; 2.60 A; A/B=26-342.
DR PDB; 6J1P; X-ray; 1.76 A; A/B=26-342.
DR PDB; 6J1Q; X-ray; 1.60 A; A/B=26-342.
DR PDB; 6J1R; X-ray; 1.60 A; A/B=26-342.
DR PDB; 6J1S; X-ray; 1.83 A; A/B=26-342.
DR PDB; 6J1T; X-ray; 1.78 A; A/B=26-342.
DR PDB; 6TP8; X-ray; 1.55 A; A/B/C=26-342.
DR PDBsum; 1LBS; -.
DR PDBsum; 1LBT; -.
DR PDBsum; 1TCA; -.
DR PDBsum; 1TCB; -.
DR PDBsum; 1TCC; -.
DR PDBsum; 3ICV; -.
DR PDBsum; 3ICW; -.
DR PDBsum; 3W9B; -.
DR PDBsum; 4K5Q; -.
DR PDBsum; 4K6G; -.
DR PDBsum; 4K6H; -.
DR PDBsum; 4K6K; -.
DR PDBsum; 4ZV7; -.
DR PDBsum; 5A6V; -.
DR PDBsum; 5A71; -.
DR PDBsum; 5GV5; -.
DR PDBsum; 6ISP; -.
DR PDBsum; 6ISQ; -.
DR PDBsum; 6ISR; -.
DR PDBsum; 6J1P; -.
DR PDBsum; 6J1Q; -.
DR PDBsum; 6J1R; -.
DR PDBsum; 6J1S; -.
DR PDBsum; 6J1T; -.
DR PDBsum; 6TP8; -.
DR AlphaFoldDB; P41365; -.
DR SASBDB; P41365; -.
DR SMR; P41365; -.
DR ESTHER; canar-LipB; Canar_LipB.
DR iPTMnet; P41365; -.
DR SABIO-RK; P41365; -.
DR EvolutionaryTrace; P41365; -.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Signal;
KW Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..25
FT /id="PRO_0000021595"
FT CHAIN 26..342
FT /note="Lipase B"
FT /id="PRO_0000021596"
FT ACT_SITE 130
FT /evidence="ECO:0000269|PubMed:8527460"
FT ACT_SITE 212
FT /evidence="ECO:0000269|PubMed:8527460"
FT ACT_SITE 249
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8087556,
FT ECO:0000269|PubMed:8527460"
FT DISULFID 47..89
FT DISULFID 241..283
FT DISULFID 318..336
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1LBT"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:5A71"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5A71"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5A71"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:5A71"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 256..267
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1TCA"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3ICW"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:5A71"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:5A71"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:5A71"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5A71"
SQ SEQUENCE 342 AA; 35518 MW; ACF1D83AED2E1A57 CRC64;
MKLLSLTGVA GVLATCVAAT PLVKRLPSGS DPAFSQPKSV LDAGLTCQGA SPSSVSKPIL
LVPGTGTTGP QSFDSNWIPL STQLGYTPCW ISPPPFMLND TQVNTEYMVN AITALYAGSG
NNKLPVLTWS QGGLVAQWGL TFFPSIRSKV DRLMAFAPDY KGTVLAGPLD ALAVSAPSVW
QQTTGSALTT ALRNAGGLTQ IVPTTNLYSA TDEIVQPQVS NSPLDSSYLF NGKNVQAQAV
CGPLFVIDHA GSLTSQFSYV VGRSALRSTT GQARSADYGI TDCNPLPAND LTPEQKVAAA
ALLAPAAAAI VAGPKQNCEP DLMPYARPFA VGKRTCSGIV TP
