(data stored in ACNUC7421 zone)

SWISSPROT: APTH1_ASHGO

ID   APTH1_ASHGO             Reviewed;         235 AA.
AC   Q750X7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=Acyl-protein thioesterase 1;
DE            EC=3.1.2.-;
GN   OrderedLocusNames=AGL188W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000305}.
DR   EMBL; AE016820; AAS54303.1; -; Genomic_DNA.
DR   RefSeq; NP_986479.1; NM_211541.1.
DR   SMR; Q750X7; -.
DR   STRING; 33169.AAS54303; -.
DR   ESTHER; ashgo-apth1; LYsophospholipase_carboxylesterase.
DR   EnsemblFungi; AAS54303; AAS54303; AGOS_AGL188W.
DR   GeneID; 4622772; -.
DR   KEGG; ago:AGOS_AGL188W; -.
DR   HOGENOM; HOG000260139; -.
DR   InParanoid; Q750X7; -.
DR   KO; K06999; -.
DR   OMA; GYVMPAW; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0002084; P:protein depalmitoylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750X7.
DR   SWISS-2DPAGE; Q750X7.
KW   Cytoplasm; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW   Reference proteome; Serine esterase.
FT   CHAIN           1..235
FT                   /note="Acyl-protein thioesterase 1"
FT                   /id="PRO_0000229003"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        172
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        206
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   235 AA;  25544 MW;  BCB6BB17792ED677 CRC64;
     MSATAPIRIA ARAQPAKYAF IIFHGLGDSG AGWTFLAEYL QRDPALASAQ FVFPTAPVRP
     ITANNFAPAT AWLDVRSWLS HESVDLEGFN ESMKLVPKLI EEQVAQGIPY ERIWIGGFSQ
     GAALTMGTAL SFPHRLGGFL SFSGPPSYRW LEHTVSDANT GAPVFQSHGT MDEVFPSSGA
     EAVHRSFTSQ YGFKNHRLKI YDGLGHSISP QLLDDALAFI KANLDAEKPA PRPAL
//

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