ID   AXE1_ASPFL              Reviewed;         307 AA.
AC   A9JPE6;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Probable acetylxylan esterase A;
DE            EC=3.1.1.72;
DE   Flags: Precursor;
GN   Name=axeA; Synonyms=aceA;
OS   Aspergillus flavus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 6541;
RX   DOI=10.1128/AEM.02146-08;
RA   Nicholson M.J., Koulman A., Monahan B.J., Pritchard B.L., Payne G.A.,
RA   Scott B.;
RT   "Identification of two aflatrem biosynthesis gene loci in Aspergillus
RT   flavus and metabolic engineering of Penicillium paxilli to elucidate their
RT   function.";
RL   Appl. Environ. Microbiol. 75:7469-7481(2009).
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 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC         EC=3.1.1.72;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; AM921700; CAP53943.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9JPE6; -.
DR   SMR; A9JPE6; -.
DR   ESTHER; aspor-axe1; Esterase_phb.
DR   VEuPathDB; FungiDB:AFLA_045570; -.
DR   VEuPathDB; FungiDB:F9C07_2281031; -.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Hydrolase;
KW   Polysaccharide degradation; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..307
FT                   /note="Probable acetylxylan esterase A"
FT                   /id="PRO_0000393477"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   307 AA;  33286 MW;  7B08600B5BAC16D1 CRC64;
     MILLSYLLTY LLCALTCSAR AIHNGRSLIP RAGSLEQVTD FGDNPSNVKM YIYVPTNLAS
     NPGIIVAIHY CTGTAQAYYQ GSPYAQLAET HGFIVIYPES PYEGTCWDVS SQATLTHNGG
     GNSNSIANMV TWTTKQYNAD SSKVFVTGTS SGAMMTNVMA ATYPNLFAAG VAYAGVPAGC
     FLSTADQPDA WNSTCAQGQS ITTPEHWASI AEAMYPDYSG SRPKMQIYHG NVDTTLYPQN
     YEETCKQWAG VFGYNYDAPE STESNTPEAN WSRTTWGPNL QGILAGGVGH NIQIHGDEDM
     KWFGFTN