ID   AES1_THETO              Reviewed;         302 AA.
AC   T2FKR1;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Acetylesterase {ECO:0000303|PubMed:24140638};
DE            EC=3.1.1.6 {ECO:0000269|PubMed:24140638};
DE   AltName: Full=Carbohydrate esterase family 16 protein {ECO:0000303|PubMed:24140638};
DE   Flags: Precursor;
GN   Name=aes1 {ECO:0000305}; Synonyms=MtAE {ECO:0000303|PubMed:24140638};
OS   Thermothelomyces thermophilus (Myceliophthora thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX   NCBI_TaxID=78579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=VKM F-3500-D;
RX   PubMed=24140638; DOI=10.1016/j.jbiotec.2013.10.009;
RA   Koutaniemi S., van Gool M.P., Juvonen M., Jokela J., Hinz S.W.,
RA   Schols H.A., Tenkanen M.;
RT   "Distinct roles of carbohydrate esterase family CE16 acetyl esterases and
RT   polymer-acting acetyl xylan esterases in xylan deacetylation.";
RL   J. Biotechnol. 168:684-692(2013).
CC   -!- FUNCTION: Acetyl esterase that acts as an exo-deacetylase
CC       (PubMed:24140638). Liberates acetic acid from xylo-oligomers
CC       (PubMed:24140638). {ECO:0000269|PubMed:24140638}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC         Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6;
CC         Evidence={ECO:0000269|PubMed:24140638};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase CE16 family.
CC       {ECO:0000305}.
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DR   EMBL; KF170220; AGW01024.1; -; Genomic_DNA.
DR   AlphaFoldDB; T2FKR1; -.
DR   SMR; T2FKR1; -.
DR   VEuPathDB; FungiDB:MYCTH_84133; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008126; F:acetylesterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF00657; Lipase_GDSL; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..302
FT                   /note="Acetylesterase"
FT                   /id="PRO_5004588075"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   302 AA;  32473 MW;  1A90D4477D514EC6 CRC64;
     MGRFLTTTAL ALLATGGAAT ARPIRACDVS TKYLITFGDS YSQTGFDVTG TKPSASNPLG
     NPLLPGWTAS GGLNWVGFLV SEFNTSTTLS YNFAYGGATT NATIVPPYQP TVLSFIDQVA
     QFSGSIARKP DYAPWNADNA LFGVWIGVND VGNVWWDPNY DSLLEQIMES YFGQLQILYD
     AGARNFVLLS VPPIQRTPAV LLNNSPENQK AEALAVDKYN EALAANLEAF TDKNGGITAK
     IVDTGVPFNT ALDNPTDYGA PDATCYNSDG KSCLWFNDYH PGIEINRLVA QAVADAWKGS
     FF