ID F2XL82_9PEZI Unreviewed; 144 AA.
AC F2XL82;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Acyl-protein thioesterase 1 {ECO:0000256|ARBA:ARBA00014923};
DE EC=3.1.2.22 {ECO:0000256|ARBA:ARBA00012423};
DE AltName: Full=Palmitoyl-protein hydrolase {ECO:0000256|ARBA:ARBA00031195};
DE Flags: Fragment;
GN Name=LPL {ECO:0000313|EMBL:AEA09725.1};
OS Grosmannia sp. SMA-2010.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Grosmannia.
OX NCBI_TaxID=999948 {ECO:0000313|EMBL:AEA09725.1};
RN [1] {ECO:0000313|EMBL:AEA09725.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB B6 {ECO:0000313|EMBL:AEA09738.1}, CB CHDSC7
RC {ECO:0000313|EMBL:AEA09743.1}, CB CHEBC10
RC {ECO:0000313|EMBL:AEA09744.1}, CB CHMC3 {ECO:0000313|EMBL:AEA09742.1},
RC CB GCA04 {ECO:0000313|EMBL:AEA09759.1}, CB HR21
RC {ECO:0000313|EMBL:AEA09748.1}, CB KDW4 {ECO:0000313|EMBL:AEA09731.1},
RC NOF 2893 {ECO:0000313|EMBL:AEA09735.1}, UAMH 11150
RC {ECO:0000313|EMBL:AEA09729.1}, UAMH 11151
RC {ECO:0000313|EMBL:AEA09730.1}, UAMH 11153
RC {ECO:0000313|EMBL:AEA09725.1}, UAMH 11154
RC {ECO:0000313|EMBL:AEA09737.1}, UAMH 11155
RC {ECO:0000313|EMBL:AEA09741.1}, and UAMH 4818
RC {ECO:0000313|EMBL:AEA09733.1};
RA Massoumi Alamouti S., Feau N., Wang V., DiGuistini S., Six D., Bohlmann J.,
RA Hamelin R., Breuil C.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEA09725.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CB B6 {ECO:0000313|EMBL:AEA09738.1}, CB CHDSC7
RC {ECO:0000313|EMBL:AEA09743.1}, CB CHEBC10
RC {ECO:0000313|EMBL:AEA09744.1}, CB CHMC3 {ECO:0000313|EMBL:AEA09742.1},
RC CB GCA04 {ECO:0000313|EMBL:AEA09759.1}, CB HR21
RC {ECO:0000313|EMBL:AEA09748.1}, CB KDW4 {ECO:0000313|EMBL:AEA09731.1},
RC NOF 2893 {ECO:0000313|EMBL:AEA09735.1}, UAMH 11150
RC {ECO:0000313|EMBL:AEA09729.1}, UAMH 11151
RC {ECO:0000313|EMBL:AEA09730.1}, UAMH 11153
RC {ECO:0000313|EMBL:AEA09725.1}, UAMH 11154
RC {ECO:0000313|EMBL:AEA09737.1}, UAMH 11155
RC {ECO:0000313|EMBL:AEA09741.1}, and UAMH 4818
RC {ECO:0000313|EMBL:AEA09733.1};
RX PubMed=21557782; DOI=10.1111/j.1365-294X.2011.05109.x;
RA Alamouti S.M., Wang V., Diguistini S., Six D.L., Bohlmann J., Hamelin R.C.,
RA Feau N., Breuil C.;
RT "Gene genealogies reveal cryptic species and host preferences for the pine
RT fungal pathogen Grosmannia clavigera.";
RL Mol. Ecol. 20:2581-2602(2011).
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC proteins with a strong preference for palmitoylated G-alpha proteins
CC over other acyl substrates. Mediates the deacylation of G-alpha
CC proteins such as GPA1 in vivo, but has weak or no activity toward
CC palmitoylated Ras proteins. Has weak lysophospholipase activity in
CC vitro; however such activity may not exist in vivo.
CC {ECO:0000256|ARBA:ARBA00029392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000072};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000256|ARBA:ARBA00006499}.
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DR EMBL; HQ633565; AEA09725.1; -; Genomic_DNA.
DR EMBL; HQ633569; AEA09729.1; -; Genomic_DNA.
DR EMBL; HQ633570; AEA09730.1; -; Genomic_DNA.
DR EMBL; HQ633571; AEA09731.1; -; Genomic_DNA.
DR EMBL; HQ633573; AEA09733.1; -; Genomic_DNA.
DR EMBL; HQ633575; AEA09735.1; -; Genomic_DNA.
DR EMBL; HQ633577; AEA09737.1; -; Genomic_DNA.
DR EMBL; HQ633578; AEA09738.1; -; Genomic_DNA.
DR EMBL; HQ633581; AEA09741.1; -; Genomic_DNA.
DR EMBL; HQ633582; AEA09742.1; -; Genomic_DNA.
DR EMBL; HQ633583; AEA09743.1; -; Genomic_DNA.
DR EMBL; HQ633584; AEA09744.1; -; Genomic_DNA.
DR EMBL; HQ633588; AEA09748.1; -; Genomic_DNA.
DR EMBL; HQ633599; AEA09759.1; -; Genomic_DNA.
DR AlphaFoldDB; F2XL82; -.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR PANTHER; PTHR10655:SF17; PALMITOYL-PROTEIN HYDROLASE; 1.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT DOMAIN 1..144
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEA09725.1"
FT NON_TER 144
FT /evidence="ECO:0000313|EMBL:AEA09725.1"
SQ SEQUENCE 144 AA; 15827 MW; 1D5D03AD67E71EC6 CRC64;
GMRMPGWYDI VSFDSPGTSL RDNEDEAGLV ASRAYFHQLV QQEIDAGVPA ERIVLGGFSQ
GGAMAIFAGI TNPRRLAGIV AMSTYLVLSQ KIESKYLPSP NANAYTPVLW CHGTADPVLP
YKMGELSRDA LRRMGYPVEW KSYP
//
