ID   AXE1_ASPNC              Reviewed;         303 AA.
AC   A2QZI3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable acetylxylan esterase A;
DE            EC=3.1.1.72;
DE   Flags: Precursor;
GN   Name=axeA; Synonyms=aceA; ORFNames=An12g05010;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270272; CAK46215.1; -; Genomic_DNA.
DR   RefSeq; XP_001395572.1; XM_001395535.2.
DR   AlphaFoldDB; A2QZI3; -.
DR   SMR; A2QZI3; -.
DR   ESTHER; aspnc-axe1; Esterase_phb.
DR   PaxDb; A2QZI3; -.
DR   EnsemblFungi; CAK46215; CAK46215; An12g05010.
DR   GeneID; 4985851; -.
DR   KEGG; ang:ANI_1_652104; -.
DR   VEuPathDB; FungiDB:An12g05010; -.
DR   HOGENOM; CLU_027551_1_1_1; -.
DR   BRENDA; 3.1.1.72; 518.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006706; Chromosome 3L.
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; Reference proteome; Secreted; Serine esterase;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..303
FT                   /note="Probable acetylxylan esterase A"
FT                   /id="PRO_5000220742"
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;  32625 MW;  68E78452C05C6353 CRC64;
     MLSTHLLFLA TTLLTSLFHP IAAHVAKRSG SLQQITDFGD NPTGVGMYIY VPNNLASNPG
     IVVAIHYCTG TGPGYYSNSF YATLSEQYGF IVIYPSSPYS GGCWDVSSQA TLTHNGGGNS
     NSIANMVTWT ISEYGADSKK VFVTGSSSGA MMTNVMAATY PELFAAGTVY SGVSAGCFYS
     DTNQVDGWNS TCAQGDVITT PEHWASIAEA MYPGYSGSRP KMQIYHGSVD TTLYPQNYYE
     TCKQWAGVFG YDYSAPESTE ANTPQTNYET TIWGDNLQGI FATGVGHTVP IHGDKDMEWF
     GFA