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 02-SEP-2026, entry version 87. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P48792; 1 site, No reported glycans. 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:0045490; P:pectin catabolic process; IEA:TreeGrafter. DR CDD; cd23399; beta-trefoil_ABD_ABFB; 1. DR FunFam; 2.60.120.200:FF:000131; Probable alpha-L-arabinofuranosidase B; 1. DR FunFam; 2.80.10.50:FF:000059; Probable alpha-L-arabinofuranosidase B; 1. DR Gene3D; 2.60.120.200; -; 1. DR Gene3D; 2.80.10.50; -; 1. 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; ALPHA-L-ARABINOFURANOSIDASE B; 1. DR PANTHER; PTHR39447:SF2; ALPHA-L-ARABINOFURANOSIDASE B; 1. DR Pfam; PF05270; AbfB; 1. DR Pfam; PF09206; ArabFuran-catal; 1. DR SUPFAM; SSF110221; AbfB domain; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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 //