LIPA_PSEA5
ID LIPA_PSEA5 Reviewed; 462 AA.
AC W3VKA4; D4PHA8;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 2.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Lipase A {ECO:0000303|PubMed:18155238};
DE Short=CalA {ECO:0000303|PubMed:18155238};
DE EC=3.1.1.3 {ECO:0000269|PubMed:16575565, ECO:0000269|PubMed:17631665};
DE Flags: Precursor;
GN ORFNames=PaG_04054;
OS Pseudozyma aphidis (strain ATCC 32657 / CBS 517.83 / DSM 70725 / JCM 10318
OS / NBRC 10182 / NRRL Y-7954 / St-0401) (Yeast) (Sterigmatomyces aphidis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1391700;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 32657 / CBS 517.83 / DSM 70725 / JCM 10318 / NBRC 10182 / NRRL
RC Y-7954 / St-0401;
RX PubMed=24526638; DOI=10.1128/genomea.00053-14;
RA Lorenz S., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT "Genome sequence of the basidiomycetous fungus Pseudozyma aphidis DSM70725,
RT an efficient producer of biosurfactant mannosylerythritol lipids.";
RL Genome Announc. 2:E0005314-E0005314(2014).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 32657 / CBS 517.83 / DSM 70725 / JCM 10318 / NBRC 10182 / NRRL
RC Y-7954 / St-0401;
RX PubMed=16575565; DOI=10.1007/s00253-006-0400-z;
RA Pfeffer J., Richter S., Nieveler J., Hansen C.E., Rhlid R.B., Schmid R.D.,
RA Rusnak M.;
RT "High yield expression of lipase A from Candida antarctica in the
RT methylotrophic yeast Pichia pastoris and its purification and
RT characterisation.";
RL Appl. Microbiol. Biotechnol. 72:931-938(2006).
RN [3]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-204; SER-205; SER-231; GLU-319;
RP HIS-351; ASP-355 AND HIS-387, AND ACTIVE SITE.
RC STRAIN=ATCC 32657 / CBS 517.83 / DSM 70725 / JCM 10318 / NBRC 10182 / NRRL
RC Y-7954 / St-0401;
RX PubMed=17631665; DOI=10.1002/cbic.200700179;
RA Kasrayan A., Bocola M., Sandstroem A.G., Laven G., Baeckvall J.E.;
RT "Prediction of the Candida antarctica lipase A protein structure by
RT comparative modeling and site-directed mutagenesis.";
RL ChemBioChem 8:1409-1415(2007).
RN [4] {ECO:0000312|PDB:3GUU}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 32-462, AND DISULFIDE BOND.
RA Brandt A.-M., Li X.-G., Nymalm-Rejstrom Y., Airenne T., Kanerva L.T.,
RA Salminen T.A.;
RT "The crystal structure of lipase A from Candida antarctica.";
RL Submitted (MAR-2009) to the PDB data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 32-462, SUBUNIT, DISULFIDE BOND,
RP AND ACTIVE SITE.
RC STRAIN=ATCC 32657 / CBS 517.83 / DSM 70725 / JCM 10318 / NBRC 10182 / NRRL
RC Y-7954 / St-0401;
RX PubMed=18155238; DOI=10.1016/j.jmb.2007.10.079;
RA Ericsson D.J., Kasrayan A., Johansson P., Bergfors T., Sandstroem A.G.,
RA Baeckvall J.E., Mowbray S.L.;
RT "X-ray structure of Candida antarctica lipase A shows a novel lid structure
RT and a likely mode of interfacial activation.";
RL J. Mol. Biol. 376:109-119(2008).
CC -!- FUNCTION: Hydrolyzes triglycerides, with a preference for substrates
CC with short-chain lengths (C4 to C8). Has the highest activity with
CC tributyrin (C4), followed by tricaproin (C6) and tricaprylin (C8). Can
CC also hydrolyze vinylacetate (C2) and triolein (C18), but with lower
CC efficiency. Has no activity with tripalmitin (C16).
CC {ECO:0000269|PubMed:16575565}.
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;
CC Evidence={ECO:0000269|PubMed:16575565, ECO:0000269|PubMed:17631665};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4483 uM for tributyrin {ECO:0000269|PubMed:16575565};
CC pH dependence:
CC Optimum pH is between 7-9. {ECO:0000269|PubMed:16575565};
CC Temperature dependence:
CC Optimum temperature is 40-70 degrees Celsius.
CC {ECO:0000269|PubMed:16575565};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18155238}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16575565}.
CC -!- BIOTECHNOLOGY: In addition to their capacity to hydrolyze a wide
CC variety of natural and non-natural substrates, lipases can also
CC catalyze the formation of ester bonds between carboxylic acids and
CC alcohols, making them attractive biocatalysts that can contribute to
CC the synthesis of pharmaceuticals and other fine chemicals. Sold under
CC the name lipase novozym 735. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ETS61940.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWNI01000013; ETS61940.1; ALT_INIT; Genomic_DNA.
DR PDB; 2VEO; X-ray; 2.20 A; A/B=22-462.
DR PDB; 3GUU; X-ray; 2.10 A; A/B=1-462.
DR PDBsum; 2VEO; -.
DR PDBsum; 3GUU; -.
DR AlphaFoldDB; W3VKA4; -.
DR SMR; W3VKA4; -.
DR ESTHER; canan-lipasA; Fungal-Bact_LIP.
DR EnsemblFungi; ETS61940; ETS61940; PaG_04054.
DR HOGENOM; CLU_029538_5_0_1; -.
DR Proteomes; UP000019462; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 InterPro; IPR005152; Lipase_secreted.
DR PANTHER; PTHR34853; PTHR34853; 1.
DR Pfam; PF03583; LIP; 1.
DR PIRSF; PIRSF029171; Esterase_LipA; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..462
FT /note="Lipase A"
FT /id="PRO_0000433085"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:17631665,
FT ECO:0000305|PubMed:18155238"
FT ACT_SITE 355
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:17631665,
FT ECO:0000305|PubMed:18155238"
FT ACT_SITE 387
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:17631665,
FT ECO:0000305|PubMed:18155238"
FT DISULFID 122..294
FT /evidence="ECO:0000269|PubMed:18155238, ECO:0000269|Ref.4"
FT DISULFID 371..415
FT /evidence="ECO:0000269|PubMed:18155238, ECO:0000269|Ref.4"
FT MUTAGEN 204
FT /note="Y->A: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:17631665"
FT MUTAGEN 205
FT /note="S->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:17631665"
FT MUTAGEN 231
FT /note="S->A: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:17631665"
FT MUTAGEN 319
FT /note="E->A: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:17631665"
FT MUTAGEN 351
FT /note="H->A: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:17631665"
FT MUTAGEN 355
FT /note="D->A: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:17631665"
FT MUTAGEN 387
FT /note="H->A: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:17631665"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3GUU"
FT TURN 163..168
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 173..190
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 206..221
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 322..328
FT /evidence="ECO:0007829|PDB:3GUU"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 376..384
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 387..393
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 395..407
FT /evidence="ECO:0007829|PDB:3GUU"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:3GUU"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:3GUU"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:3GUU"
SQ SEQUENCE 462 AA; 49265 MW; 700908D4C645981B CRC64;
MRVSLRSITS LLAAATAAVL AAPATETLDR RAALPNPYDD PFYTTPSNIG TFAKGQVIQS
RKVPTDIGNA NNAASFQLQY RTTNTQNEAV ADVATVWIPA KPASPPKIFS YQVYEDATAL
DCAPSYSYLT GLDQPNKVTA VLDTPIIIGW ALQQGYYVVS SDHEGFKAAF IAGYEEGMAI
LDGIRALKNY QNLPSDSKVA LEGYSGGAHA TVWATSLADS YAPELNIVGA SHGGTPVSAK
DTFTFLNGGP FAGFALAGVS GLSLAHPDME SFIEARLNAK GQQTLKQIRG RGFCLPQVVL
TYPFLNVFSL VNDTNLLNEA PIAGILKQET VVQAEASYTV SVPKFPRFIW HAIPDEIVPY
QPAATYVKEQ CAKGANINFS PYPIAEHLTA EIFGLVPSLW FIKQAFDGTT PKVICGTPIP
AIAGITTPSA DQVLGSDLAN QLRSLNGKQS AFGKPFGPIT PP
