ID   AXE1_NEOFI              Reviewed;         368 AA.
AC   A1DBP9;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Probable acetylxylan esterase A;
DE            EC=3.1.1.72;
DE   Flags: Precursor;
GN   Name=axeA; Synonyms=aceA; ORFNames=NFIA_099230;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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   -!- DOMAIN: Has a modular structure: a carbohydrate esterase catalytic
CC       module at the N-terminus, a linker rich in serines and threonines, and
CC       a C-terminal carbohydrate-binding module (CBM). The genes for catalytic
CC       modules and CBMs seem to have evolved separately and have been linked
CC       by gene fusion.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DS027694; EAW20289.1; -; Genomic_DNA.
DR   RefSeq; XP_001262186.1; XM_001262185.1.
DR   AlphaFoldDB; A1DBP9; -.
DR   SMR; A1DBP9; -.
DR   STRING; 331117.A1DBP9; -.
DR   ESTHER; neofi-axe1; Esterase_phb.
DR   EnsemblFungi; EAW20289; EAW20289; NFIA_099230.
DR   GeneID; 4588439; -.
DR   KEGG; nfi:NFIA_099230; -.
DR   VEuPathDB; FungiDB:NFIA_099230; -.
DR   eggNOG; ENOG502QTDU; Eukaryota.
DR   HOGENOM; CLU_027551_1_1_1; -.
DR   OMA; IANMVKW; -.
DR   OrthoDB; 1169544at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000006702; 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:0030248; F:cellulose binding; IEA:InterPro.
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; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR010126; Esterase_phb.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF10503; Esterase_PHB; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF53474; SSF53474; 2.
DR   TIGRFAMs; TIGR01840; esterase_phb; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation;
KW   Cleavage on pair of basic residues; Glycoprotein; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Serine esterase;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..28
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000393483"
FT   CHAIN           29..368
FT                   /note="Probable acetylxylan esterase A"
FT                   /id="PRO_0000393484"
FT   DOMAIN          332..368
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          32..304
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   REGION          305..333
FT                   /note="Ser/Thr-rich linker"
FT   REGION          306..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   368 AA;  38975 MW;  C6C4FFBBA6C000BA CRC64;
     MRALSVFFAL FCFLALSSAS PGQDVVKRVT SGSLQQVTNF GSNPSGTLMY IYVPKNLATK
     PGIVVAIHYC TGTAQAYYTG SPYAQLAEQY GFIVIYPQSP YSGTCWDVSS QSALTHNGGG
     DSNSIANMVT WTISQYNADT SKVFVTGSSS GAMMTNVMAA TYPELFAAAT VYSGVSAGCF
     YSSSNQVDAW NSSCAQGNVI STPEVWGGIA KAMYPGYTGP RPRMQIYHGS TDTTLYPQNY
     YETCKQWAGV FGYNYNSPQS TQSNTPQANY QTTIWGPNLQ GIFATGVGHT VPIHGEQDME
     WFGFAGGSST TTTQPTTTST TTSSGGSSTG TGVAAHWGQC GGNGWTGPTV CASGYTCTVV
     NAWYSQCL