ID   IABF_BACOV              Reviewed;         514 AA.
AC   Q59219;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Intracellular exo-alpha-L-arabinofuranosidase;
DE            Short=ABF;
DE            EC=3.2.1.55;
DE   AltName: Full=Intracellular arabinan exo-alpha-L-arabinosidase;
DE            Short=Arabinosidase;
GN   Name=asdII;
OS   Bacteroides ovatus.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=28116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=V975;
RA   Whitehead T.R.;
RL   Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the degradation of arabinan and is a key enzyme
CC       in the complete degradation of the plant cell wall. Catalyzes the
CC       cleavage of terminal alpha-L-arabinofuranosyl residues in different
CC       hemicellulosic homopolysaccharides (branched and debranched arabinans)
CC       and heteropolysaccharides (arabinoxylans) (By similarity).
CC       {ECO:0000250}.
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   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR   EMBL; U15179; AAA50393.1; -; Genomic_DNA.
DR   RefSeq; WP_004297450.1; NZ_UAQF01000004.1.
DR   AlphaFoldDB; Q59219; -.
DR   SMR; Q59219; -.
DR   STRING; 28116.Bovatus_00205; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   GeneID; 29454855; -.
DR   OrthoDB; 620389at2; -.
DR   UniPathway; UPA00667; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Disulfide bond; Glycosidase; Hydrolase.
FT   CHAIN           1..514
FT                   /note="Intracellular exo-alpha-L-arabinofuranosidase"
FT                   /id="PRO_0000057703"
FT   ACT_SITE        195
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        317
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            321
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
FT   SITE            366
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
FT   DISULFID        93..199
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   514 AA;  57979 MW;  C8E1023A2E098884 CRC64;
     MKAKLLVSTA FLAASVSLSA QKSATITVHA DQGKEIIPKE IYGQFAEHLG SCIYGGLWVG
     ENSDIPNIKG YRTDVFNALK DLSVPVLRWP GGCFADEYHW MDGIGPKENR PKMVNNNWGG
     TIEDNSFGTH EFLNLCEMLG CEPYVSGNVG SGTVEELAKW VEYMTSDGDS PMANLRRKNG
     RDKAWKLKYL GVGNESWGCG GSMRPEYYAD LYRRYSTYCR NYDGNRLFKI ASGASDYDYK
     WTDVLMNRVG HRMDGLSLHY YTVTGWSGSK GSATQFNKDD YYWTMGKCLE VEDVLKKHCT
     IMDKYDKDKK IALLLDEWGT WWDEEPGTIK GHLYQQNTLR DAFVASLSLD VFHKYTDRLK
     MANIAQIVNV LQSMILTKDK EMVLTPTYYV FKMYKVHQDA TYLPIDLTCE KMSVRDNRTV
     PMVSATASKN KDGVIHISLS NVDADEAQEI TINLGDTKAK KAIGEILTAS KLTDYNSFEK
     PNIVKPAPFK EVKINKGTMK VKLPAKSIVT LELQ