ID M5GH05_DACPD Unreviewed; 242 AA.
AC M5GH05;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
GN ORFNames=DACRYDRAFT_97864 {ECO:0000313|EMBL:EJU06398.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU06398.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU06398.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU06398.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH795855; EJU06398.1; -; Genomic_DNA.
DR AlphaFoldDB; M5GH05; -.
DR STRING; 1858805.M5GH05; -.
DR HOGENOM; CLU_049413_3_5_1; -.
DR OMA; WYDILAM; -.
DR OrthoDB; 4670340at2759; -.
DR Proteomes; UP000030653; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000030653};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT DOMAIN 13..237
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
SQ SEQUENCE 242 AA; 26672 MW; 39D6EB2DEEB7F419 CRC64;
MAHLQPLKFV QVLPKAKHTA TVFFMHGLGD SGAGWAPVAD MLSEKLPHVK WILPNARTQP
VTVNWGMDSP SWFDIYTLGD RSMPQREDER GMLDSVVSIE ALVADEIEKN NIPSERIIVG
GFSQGGALSM LFGTTTKHKL GGIVVLSAWL PLRDKIASMV SPELKTLPIF QGHGVQDAIV
QCEWGRLSGE YLKEKFGVKV AEPGKLKEGG IIFKTYQGLL HGASDEEIED LSKWLQEVLP
NN
//
