ID   AXE1_ASPFI              Reviewed;         303 AA.
AC   Q96W96;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Acetylxylan esterase A;
DE            EC=3.1.1.72;
DE   Flags: Precursor;
GN   Name=axeA; Synonyms=aceA;
OS   Aspergillus ficuum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, GLYCOSYLATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   DOI=10.1016/S0141-0229(02)00122-9;
RA   Chung H.-J., Park S.-M., Kim H.-R., Yang M.-S., Kim D.-H.;
RT   "Cloning the gene encoding acetyl xylan esterase from Aspergillus ficuum
RT   and its expression in Pichia pastoris.";
RL   Enzyme Microb. Technol. 31:384-391(2002).
CC   -!- FUNCTION: Acetylxylan esterase involved in the hydrolysis of xylan, a
CC       major structural heterogeneous polysaccharide found in plant biomass
CC       representing the second most abundant polysaccharide in the biosphere,
CC       after cellulose. Degrades acetylated xylans by cleaving acetyl side
CC       groups from the hetero-xylan backbone. {ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC         EC=3.1.1.72;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Thermal stability decreased at temperatures above 40 degrees Celsius.
CC         {ECO:0000269|Ref.1};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: The C-terminal carbohydrate-binding module (CBM) extension
CC       found in some acetylxylan esterases from other species is absent.
CC       {ECO:0000305}.
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DR   EMBL; AF331757; AAK60128.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q96W96; -.
DR   SMR; Q96W96; -.
DR   ESTHER; aspnc-axe1; Esterase_phb.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR010126; Esterase_phb.
DR   Pfam; PF10503; Esterase_PHB; 1.
DR   SUPFAM; SSF53474; SSF53474; 2.
DR   TIGRFAMs; TIGR01840; esterase_phb; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Hydrolase;
KW   Polysaccharide degradation; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..303
FT                   /note="Acetylxylan esterase A"
FT                   /id="PRO_0000393476"
FT   ACT_SITE        147
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   303 AA;  32591 MW;  281C57BD9D3996A3 CRC64;
     MLSTHLLFLA TTLLTSLFHP IAAHVAKRSG SLQQITDFGD NPTGVGMYIY VPNNLASNPG
     IVVAIHYCTG TGPGYYSNSP YATLSEQYGF IVIYPSSPYS GGCWDVSSQA TLTHNGGGNS
     NSIANMVTWT ISEYGADSKK VYVTGSSSGA MMTNVMAATY PELFAAGTVY SGVSAGCFYS
     DTNQVDGWNS TCAQGDVITT PEHWASIAEA MYPGYSGSRP KMQIYHGSVD TTLYPQNYYE
     TCKQWAGVFG YDYSAPESTE ANTPQTNYET TIWGDNLQGI FATGVGHTVP IHGDKDMEWF
     GFA