ID   AXE1_ASPCL              Reviewed;         308 AA.
AC   A1CSZ8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Probable acetylxylan esterase A;
DE            EC=3.1.1.72;
DE   Flags: Precursor;
GN   Name=axeA; Synonyms=aceA; ORFNames=ACLA_081220;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027060; EAW06435.1; -; Genomic_DNA.
DR   RefSeq; XP_001267861.1; XM_001267860.1.
DR   AlphaFoldDB; A1CSZ8; -.
DR   SMR; A1CSZ8; -.
DR   STRING; 344612.A1CSZ8; -.
DR   ESTHER; aspcl-axe1; Esterase_phb.
DR   EnsemblFungi; EAW06435; EAW06435; ACLA_081220.
DR   GeneID; 4700180; -.
DR   KEGG; act:ACLA_081220; -.
DR   VEuPathDB; FungiDB:ACLA_081220; -.
DR   eggNOG; ENOG502QTDU; Eukaryota.
DR   HOGENOM; CLU_027551_1_1_1; -.
DR   OMA; IANMVKW; -.
DR   OrthoDB; 1169544at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006701; 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..308
FT                   /note="Probable acetylxylan esterase A"
FT                   /id="PRO_0000393475"
FT   ACT_SITE        151
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   308 AA;  33365 MW;  7589A0B5B5147F5E CRC64;
     MAPFSFLLTL LLYTLSAGAS VLESRSSALL PRAGSLQQVT NFGDNPTNVG MYIYVPNNLA
     SNPGIIVAIH YCTGTAEAYY NGSPYAKLAE KHGFIVIYPE SPYQGKCWDV SSRASLTHNG
     GGNSNSIANM VKWTIKKYKT NTSKVFVTGS SSGAMMTNVM AATYPDMFAA GVVYSGVAAG
     CFMSNTNQQA AWNSTCAHGK SIATPEAWAH VAKAMYPGYD GPRPRMQIYH GSADTTLYPQ
     NYQETCKEWA GVFGYDYNAP RSVENNKPQA NYKTTTWGKE LQGIYATGVG HTVPINGDRD
     MAWFGFAK