ID   AES1_MYCTT              Reviewed;         302 AA.
AC   G2QJ27;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Acetylesterase {ECO:0000250|UniProtKB:T2FKR1};
DE            EC=3.1.1.6 {ECO:0000250|UniProtKB:T2FKR1};
DE   AltName: Full=Carbohydrate esterase family 16 protein {ECO:0000250|UniProtKB:T2FKR1};
DE   Flags: Precursor;
GN   Name=aes1 {ECO:0000250|UniProtKB:T2FKR1};
GN   Synonyms=MtAE {ECO:0000250|UniProtKB:T2FKR1}; ORFNames=MYCTH_84133;
OS   Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS   (Sporotrichum thermophile).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX   NCBI_TaxID=573729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX   PubMed=21964414; DOI=10.1038/nbt.1976;
RA   Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA   Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA   Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA   Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA   Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA   Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA   Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA   Tsang A.;
RT   "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT   Myceliophthora thermophila and Thielavia terrestris.";
RL   Nat. Biotechnol. 29:922-927(2011).
CC   -!- FUNCTION: Acetyl esterase that acts as an exo-deacetylase (By
CC       similarity). Liberates acetic acid from xylo-oligomers (By similarity).
CC       {ECO:0000250|UniProtKB:T2FKR1}.
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:0000250|UniProtKB:T2FKR1};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase CE16 family.
CC       {ECO:0000305}.
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DR   EMBL; CP003006; AEO59602.1; -; Genomic_DNA.
DR   RefSeq; XP_003664847.1; XM_003664799.1.
DR   AlphaFoldDB; G2QJ27; -.
DR   SMR; G2QJ27; -.
DR   EnsemblFungi; AEO59602; AEO59602; MYCTH_84133.
DR   GeneID; 11506719; -.
DR   KEGG; mtm:MYCTH_84133; -.
DR   VEuPathDB; FungiDB:MYCTH_84133; -.
DR   eggNOG; ENOG502RS04; Eukaryota.
DR   HOGENOM; CLU_015101_4_2_1; -.
DR   InParanoid; G2QJ27; -.
DR   OrthoDB; 704138at2759; -.
DR   Proteomes; UP000007322; Chromosome 5.
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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..302
FT                   /note="Acetylesterase"
FT                   /id="PRO_5003436452"
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;  32457 MW;  AFC5811B7D514EC0 CRC64;
     MGRFLTTTAL ALLATGGAAT ARPIRACDVS TKYLITFGDS YSQTGFDVTG TKPSASNPLG
     NPPLPGWTAS GGLNWVGFLV SEFNTSTTLS YNFAYGGATT NATIVPPYQP TVLSFIDQVA
     QFSGSIARKP DYAPWNADNA LFGVWIGVND VGNVWWDPNY DSLLEQIMES YFGQLQILYD
     AGARNFVLLS VPPIQRTPAV LLNNSPENQK AEALAVDKYN EALAANLEAF TDKNGGITAK
     IVDTGVPFNT ALDNPTDYGA PDATCYNSDG KSCLWFNDYH PGIEINRLVA QAVADAWKGS
     FF