ID   O08457_THEST            Unreviewed;       491 AA.
AC   O08457;
DT   01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT   01-JUL-1997, sequence version 1.
DT   04-NOV-2026, entry version 70.
DE   RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE            EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN   Name=arfB {ECO:0000313|EMBL:AAC28125.1};
OS   Thermoclostridium stercorarium (Clostridium stercorarium).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC   Oscillospiraceae; Thermoclostridium.
OX   NCBI_TaxID=1510 {ECO:0000313|EMBL:AAC28125.1};
RN   [1] {ECO:0000313|EMBL:AAC28125.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=7576552; DOI=10.1007/s002530050496;
RA   Schwarz W.H., Bronnenmeier K., Krause B., Lottspeich F., Staudenbauer W.L.;
RT   "Debranching of arabinoxylan: properties of the thermoactive recombinant
RT   alpha-L-arabinofuranosidase from Clostridium stercorarium (ArfB).";
RL   Appl. Microbiol. Biotechnol. 43:856-860(1995).
RN   [2] {ECO:0000313|EMBL:AAC28125.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schwarz W.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AAC28125.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9682483;
RA   Zverlov V.V., Liebl W., Bachleitner M., Schwarz W.H.;
RT   "Nucleotide sequence of arfB of Clostridium stercorarium, and prediction of
RT   catalytic residues of alpha-L-arabinofuranosidases based on local
RT   similarity with several families of glycosyl hydrolases.";
RL   FEMS Microbiol. Lett. 164:337-343(1998).
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         Evidence={ECO:0000256|ARBA:ARBA00001462};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers.
CC       {ECO:0000256|ARBA:ARBA00011165}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC       {ECO:0000256|ARBA:ARBA00007186}.
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; AF002664; AAC28125.1; -; Genomic_DNA.
DR   AlphaFoldDB; O08457; -.
DR   SMR; O08457; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   BRENDA; 3.2.1.55; 1520.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:TreeGrafter.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR055235; ASD1_cat.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   PANTHER; PTHR43576; ALPHA-L-ARABINOFURANOSIDASE C-RELATED; 1.
DR   PANTHER; PTHR43576:SF2; INTRACELLULAR EXO-ALPHA-L-ARABINOFURANOSIDASE 2; 1.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   Pfam; PF22848; ASD1_dom; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:AAC28125.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAC28125.1}.
FT   DOMAIN          293..484
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   491 AA;  56166 MW;  DB076C17A480E60E CRC64;
     MAKYVINTLN RKSKINREIY GHFSEHLGRC IYGGFYVGEN SPIPNTKGIR NDVVNALKKI
     RIPVLRWPGG CFADEYHWMD GIGPKEQRKK MINTHWGGVV EASFGTDEFM ELCRQLECEP
     YINGNLGSGT VKEMQDWIEY LTFDGISPMS ELRAKNGRKE PYRLKYFCIG NENWGCGGNM
     RPEFYADMYR RYQTYVRNYG NNKIYKIACG PNSDDYNWTE TVVKIAGRFM DAISLHYYTV
     PGTWHSKGSS TKFTEEEWYI TLFKTLKMDE LITKHTAIIR RYDPDNRIGL VVDEWGTWYD
     VEPGTNPGFL YQQNTMRDAL VAGINLNIFN KHSDKVVMAN LAQTINVLQA VILTEGEKML
     LTPTYHVFDM YKEHQGAELV EKLLLKTEKK SAQTKYTVPN LHESASVNAD GKLHITLCNL
     SLSESYRVET EIIGKKAENV TGRILTGKMN DHNTFDAPET VKPQTFDKIS VRQNGLVIEI
     PPVSVVSITV D
//