ID H6BKZ6_EXODN Unreviewed; 255 AA.
AC H6BKZ6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=HMPREF1120_00025 {ECO:0000313|EMBL:EHY51798.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY51798.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY51798.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY51798.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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; JH226130; EHY51798.1; -; Genomic_DNA.
DR RefSeq; XP_009152259.1; XM_009154011.1.
DR AlphaFoldDB; H6BKZ6; -.
DR STRING; 858893.H6BKZ6; -.
DR GeneID; 20304664; -.
DR VEuPathDB; FungiDB:HMPREF1120_00025; -.
DR eggNOG; KOG2112; Eukaryota.
DR HOGENOM; CLU_049413_3_4_1; -.
DR InParanoid; H6BKZ6; -.
DR OMA; WIIPNAM; -.
DR OrthoDB; 3672446at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR PANTHER; PTHR10655:SF17; LYSOPHOSPHOLIPASE-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT DOMAIN 19..251
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
SQ SEQUENCE 255 AA; 28620 MW; E9A44D29BB2FC5BF CRC64;
MSDRPPYIVP PTKPSSSPDR AATLIFLHGY GDDADGLPLG IAQQFQFYNK LEYLKWVLPY
APHNHEAMSR AWYVPKALPN AMKPRVPGHE EDETAPDDEV AIMKSVDIID KLVEEEIKNG
TPAKRILVGG FSQGCAVSLV WGLTSRFKNE VGGMVCLSGY MPLRDRIAQL RRERRPEGCP
EEAELPEKGG KKWFYVHGTM DMLIPTKMFA QGMEELAKWV DKEDIEVHLY PGMGHSTATA
ELRDLLGFLD RVVPP
//