ID   AXE1_ASPTN              Reviewed;         311 AA.
AC   Q0C8Z1;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Probable acetylxylan esterase A;
DE            EC=3.1.1.72;
DE   Flags: Precursor;
GN   Name=axeA; Synonyms=aceA; ORFNames=ATEG_09843;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476608; EAU30034.1; -; Genomic_DNA.
DR   RefSeq; XP_001218465.1; XM_001218464.1.
DR   AlphaFoldDB; Q0C8Z1; -.
DR   SMR; Q0C8Z1; -.
DR   STRING; 341663.Q0C8Z1; -.
DR   ESTHER; asptn-axe1; Esterase_phb.
DR   EnsemblFungi; EAU30034; EAU30034; ATEG_09843.
DR   GeneID; 4354490; -.
DR   VEuPathDB; FungiDB:ATEG_09843; -.
DR   eggNOG; ENOG502QTDU; Eukaryota.
DR   HOGENOM; CLU_027551_1_1_1; -.
DR   OMA; IANMVKW; -.
DR   OrthoDB; 1169544at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..311
FT                   /note="Probable acetylxylan esterase A"
FT                   /id="PRO_0000393481"
FT   ACT_SITE        153
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   311 AA;  33537 MW;  87A6415C2342612F CRC64;
     MAPFSFILTV LLYALTCSAR ALGHAHALLP RAGSLEQVTD FGDNPTNVGM YIYVPNNLAS
     SPGIVVAIHY SPEGTGTAEA YYTGSPYAQL AEQYGFIVIY PQSPYEGTCW DVSSQETLTH
     NGGGNSNSIA NMVTWAISKY NADSSKVFVT GSSSGAMMTH QNVMAATYPE LFAAATVYSG
     VPAGCFYSSS NQQDGWNSTC AQGQVITTPE NWANVAKGMY PGYNGTRPKM QIYHGSVDTT
     LLPQNYYETC KQWAGVFGYN YDSPQQVQDN TPQSNYATTT WGDDLQGIFA TGVGHTVPIR
     GDDDMAWFGF A