ID   AES1_HYPJE              Reviewed;         348 AA.
AC   A7J2C6;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Acetylesterase {ECO:0000303|Ref.2};
DE            EC=3.1.1.6 {ECO:0000269|PubMed:18978092, ECO:0000269|PubMed:24140638, ECO:0000269|Ref.2};
DE   AltName: Full=Carbohydrate esterase family 16 protein {ECO:0000303|PubMed:24140638};
DE   Flags: Precursor;
GN   Name=aes1 {ECO:0000303|PubMed:18978092};
GN   Synonyms=TrAE {ECO:0000303|PubMed:24140638};
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, GLYCOSYLATION, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 56765 / Rut C-30;
RX   PubMed=18978092; DOI=10.1128/aem.00807-08;
RA   Li X.L., Skory C.D., Cotta M.A., Puchart V., Biely P.;
RT   "Novel family of carbohydrate esterases, based on identification of the
RT   Hypocrea jecorina acetyl esterase gene.";
RL   Appl. Environ. Microbiol. 74:7482-7489(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 56765 / Rut C-30;
RX   DOI=10.1007/BF00268207;
RA   Poutanen K., Sundberg M.;
RT   "An acetyl esterase of Trichoderma reesei and its role in the hydrolysis of
RT   acetyl xylans.";
RL   Appl. Microbiol. Biotechnol. 28:419-424(1987).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 56765 / Rut C-30;
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: Acetylesterase that acts as an exo-deacetylase
CC       (PubMed:24140638). Shows activity towards naphtyl acetate, triacetin,
CC       as well as towards glucose- and xylose acetates (PubMed:18978092,
CC       Ref.2). Liberates acetic acid from xylo-oligomers (PubMed:18978092,
CC       Ref.2, PubMed:24140638). {ECO:0000269|PubMed:18978092,
CC       ECO:0000269|PubMed:24140638, ECO:0000269|Ref.2}.
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:18978092, ECO:0000269|PubMed:24140638,
CC         ECO:0000269|Ref.2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.23 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:18978092};
CC         Vmax=20.5 umol/min/mg enzyme toward 4-nitrophenyl acetate
CC         {ECO:0000269|PubMed:18978092};
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. {ECO:0000269|Ref.2};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- INDUCTION: Expression is induced by sophorose, cellulose, oat spelt
CC       xylan, lactose, and arabinose. {ECO:0000269|PubMed:18978092}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18978092}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase CE16 family.
CC       {ECO:0000305}.
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DR   EMBL; DQ866149; ABI34466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7J2C6; -.
DR   SMR; A7J2C6; -.
DR   BRENDA; 3.1.1.6; 6451.
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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..348
FT                   /note="Acetylesterase"
FT                   /id="PRO_5002710640"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   348 AA;  39158 MW;  FB0441DE6021AA4D CRC64;
     MRSILVIPSF VAVLNAFSLF PKPHDDFKYL ITFGDSYTDN GRLGYYGSHQ AHGPPPGVMP
     PEANVTASGG LQWPQYVEAS TGATLYDYAI AGATCDNNNV ERWAAFMNAN YPSIITDEIP
     SFKADRKTKL YRGVTSANTV YALWIGTNDL SYTGILSDSQ VKGTNITTYI DCLWNVFDAI
     HAAGGRRFVI LNNNALQLTG LYRPLSDGGA GDNQFWQNKT LYNQTEYAQK MLEYTTSSNT
     MIDYGVPFHL LVKNRWPGSK VAVYDIHSLI MDIYNQPSRY LEPPHNVVGY YKHCDVNGTN
     CLYGPGRLDS YLWYDELHPS NIIASYIARE FLNVVSGRSK YGTYWEHW