LIPA_SODAL
ID LIPA_SODAL Reviewed; 416 AA.
AC P0CT91;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=Lipase A {ECO:0000303|PubMed:23915965};
DE EC=3.1.1.3 {ECO:0000269|PubMed:23915965};
DE EC=3.1.1.72 {ECO:0000269|PubMed:23915965};
DE AltName: Full=Acetylxylan esterase;
DE Flags: Precursor;
GN Name=lipA {ECO:0000303|PubMed:23915965};
GN ORFNames=fgenesh2_kg.3_#_445_#_Contig6955;
OS Sodiomyces alcalophilus (Acremonium alcalophilum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=398408;
RN [1]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP GLYCOSYLATION.
RC STRAIN=ATCC 90507 / BCRC 33522 / CBS 114.92 / JCM 7366 / KCTC 16719;
RX PubMed=23915965; DOI=10.1186/1754-6834-6-111;
RA Pereira E.O., Tsang A., McAllister T.A., Menassa R.;
RT "The production and characterization of a new active lipase from Acremonium
RT alcalophilum using a plant bioreactor.";
RL Biotechnol. Biofuels 6:111-111(2013).
CC -!- FUNCTION: Lipolytic enzyme that possesses both lipase and acetylxylan
CC esterase activity. Active towards p-nitrophenol esters of various
CC carbon chain length with preference for medium-chain fatty acids (C-8).
CC Also highly active on the acetylated compounds xylose tetra-acetate and
CC oat spelt xylan. {ECO:0000269|PubMed:23915965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC EC=3.1.1.72; Evidence={ECO:0000269|PubMed:23915965};
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:23915965};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for p-nitrophenol acetate {ECO:0000269|PubMed:23915965};
CC KM=0.16 mM for p-nitrophenol butyrate {ECO:0000269|PubMed:23915965};
CC KM=0.10 mM for p-nitrophenol caprylate {ECO:0000269|PubMed:23915965};
CC KM=0.07 mM for p-nitrophenol myristate {ECO:0000269|PubMed:23915965};
CC KM=0.10 mM for p-nitrophenol palmitate {ECO:0000269|PubMed:23915965};
CC Vmax=0.24 umol/min/mg enzyme toward p-nitrophenol acetate
CC {ECO:0000269|PubMed:23915965};
CC Vmax=4.73 umol/min/mg enzyme toward p-nitrophenol butyrate
CC {ECO:0000269|PubMed:23915965};
CC Vmax=9.45 umol/min/mg enzyme toward p-nitrophenol caprylate
CC {ECO:0000269|PubMed:23915965};
CC Vmax=3.42 umol/min/mg enzyme toward p-nitrophenol myristate
CC {ECO:0000269|PubMed:23915965};
CC Vmax=1.84 umol/min/mg enzyme toward p-nitrophenol palmitate
CC {ECO:0000269|PubMed:23915965};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:23915965};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius. Thermostable from 20 to 50
CC degrees Celsius. {ECO:0000269|PubMed:23915965};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:23915965}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0CT91; -.
DR SMR; P0CT91; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002921; Fungal_lipase-like.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Polysaccharide degradation; Secreted;
KW Serine esterase; Signal; Xylan degradation.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..416
FT /note="Lipase A"
FT /id="PRO_0000435968"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O59952"
FT ACT_SITE 287
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O59952"
FT ACT_SITE 381
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O59952"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 67..391
FT /evidence="ECO:0000250|UniProtKB:O59952"
FT DISULFID 177..180
FT /evidence="ECO:0000250|UniProtKB:O59952"
SQ SEQUENCE 416 AA; 45645 MW; B6C4B8EBDCD20500 CRC64;
MRLAPQKPLL LSTVLHLLLS IWMLGFASLA GATVQEPLAA SDTPKPVSAA LFSSIERLSR
LVDITYCVGN TGVWKPFACA SRCNEFPTLT LERTWRTGIL MSDSCGLIAV DHGTPRHDAG
EGKDDPLAEK AIIVAFRGTY SLTNTIIDLS TIPQEYVPYP SPDDGGNEPP REPSHRCDNC
TVHSGFLASW RHARKVVLPE LKVLRQKYPE YPIRLVGHSL GGAVAMLAAL EMRVSLGWRD
TVVTTFGEPR VGNRQLCDYL NAVFELNLGD EMDPAEREYR RVTHADDPVP LLPPAEWGYS
SHGGEFFISK KDLPPSVEDV LVCHGDHDEN CIARGKSSAV SVPAGDYDDA LSTLEEQDVM
LADALPWIPA RLKLWELFFA HRDYFWRLGL CVPGGDPANW GRKGGEGAAE SISAEG
