ID   XYL1_TRIKO              Reviewed;         500 AA.
AC   P48792;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Arabinofuranosidase/B-xylosidase;
DE   Includes:
DE     RecName: Full=Alpha-L-arabinofuranosidase;
DE              Short=Arabinosidase;
DE              EC=3.2.1.55;
DE   Includes:
DE     RecName: Full=Beta-xylosidase;
DE              EC=3.2.1.37;
DE     AltName: Full=1,4-beta-D-xylan xylohydrolase;
DE     AltName: Full=Xylan 1,4-beta-xylosidase;
DE   Flags: Precursor;
GN   Name=xyl1;
OS   Trichoderma koningii (Hypocrea koningii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=97093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G-39;
RA   Huang L.N., Hseu T.H., Lee Y.J.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC         residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC         xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family. {ECO:0000305}.
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DR   EMBL; U38661; AAA81024.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48792; -.
DR   SMR; P48792; -.
DR   CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR   CAZy; GH54; Glycoside Hydrolase Family 54.
DR   CLAE; ZAX54A_TRIKO; -.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031221; P:arabinan metabolic process; IEA:InterPro.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR   InterPro; IPR038964; ABFB.
DR   InterPro; IPR007934; AbfB_ABD.
DR   InterPro; IPR036195; AbfB_ABD_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   PANTHER; PTHR39447; PTHR39447; 1.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF09206; ArabFuran-catal; 1.
DR   SUPFAM; SSF110221; SSF110221; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Multifunctional enzyme; Polysaccharide degradation; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..500
FT                   /note="Arabinofuranosidase/B-xylosidase"
FT                   /id="PRO_0000012225"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   500 AA;  51129 MW;  06DFC319AAFA1149 CRC64;
     MLSNARIIAA GCIAAGSLVA AGPCDIYSSG GTPCVAAHST TRALFSAYTG PLYQVKRGSD
     GATTAISPLS SGVANAAAQD AFCAGTTCLI TIIYDQSGRG NHLREAPPGG FSGPESNGYD
     NLASAIGAPV TLNGQKAYGV FVSPGTGYRN NAASGTAKGD AAEGMYAVLD GTHYNGACCF
     DYGNAETNSR DTGNGHMEAI YFGDSTVWGT GSGKGPWIMA DLENGLFSGS SPGNNAGDPS
     ISYRFVTAAI KGQPNQWAIR GGNAASGSLS TFYSGARPQV SGYNPMSKEG AIILGIGGDN
     SNGGQGTFYE GVMTSGYPSD ATENSVQANI VAARYAVAPL TSGPALTVGS SISLRATTAC
     CTTRYIAHSG STVNTQVVSS SSATALKQQA SWTVRAGLAN NACFSFESQD TSGSYIRHSN
     FGLVLNANDG SKLFAEDATF CTQAGINGQG SSIRSWSYPT RYFRHYNNTL YIASNGGVHV
     FDATAAFNDD VSFVVSGGFA