ID   EABF_STRCX              Reviewed;         825 AA.
AC   P82593;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Extracellular exo-alpha-L-arabinofuranosidase;
DE            Short=ABF;
DE            EC=3.2.1.55;
DE   AltName: Full=Alpha-L-AFase;
DE   AltName: Full=Extracellular arabinan exo-alpha-L-arabinosidase;
DE            Short=Arabinosidase;
DE   Flags: Precursor;
OS   Streptomyces chartreusis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-75, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=GS901;
RX   PubMed=10657233; DOI=10.1042/bj3460009;
RA   Matsuo N., Kaneko S., Kuno A., Kobayashi H., Kusakabe I.;
RT   "Purification, characterization and gene cloning of two alpha-L-
RT   arabinofuranosidases from Streptomyces chartreusis GS901.";
RL   Biochem. J. 346:9-15(2000).
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 of arabinan
CC       present in the arabinofuranosyl polysaccharides or oligosaccharides. It
CC       cannot act on other arabinose-containing polysaccharides and
CC       arabinoxylo-oligosaccharides. It leaves most of the polymer intact,
CC       including most of the main-chain residues and the arabinose side
CC       chains. It acts preferentially on the linear alpha-(1->2)-linked
CC       arabinofuranobiosides and alpha-(1->3)-linked arabinofuranobiosides,
CC       and is much less effective on alpha-(1->5)-linked
CC       arabinofuranobiosides. It also hydrolyzes the terminal alpha-(1->3)-
CC       linked arabinofuranotriosides in preference to the alpha-(1->5)-linked
CC       arabinofuranotriosides. {ECO:0000269|PubMed:10657233}.
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:0000269|PubMed:10657233};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5. The enzyme is slowly inactivated above pH 8.5 and
CC         below pH 5.5. {ECO:0000269|PubMed:10657233};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius. The enzyme is inactivated
CC         at temperatures above 45 degrees Celsius.
CC         {ECO:0000269|PubMed:10657233};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR   EMBL; AB023625; BAA90771.1; -; Genomic_DNA.
DR   PIR; A59296; A59296.
DR   AlphaFoldDB; P82593; -.
DR   SMR; P82593; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   BRENDA; 3.2.1.55; 5991.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; IPR003305; CenC_carb-bd.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31776; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR   PANTHER; PTHR31776:SF0; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:10657233"
FT   CHAIN           30..825
FT                   /note="Extracellular exo-alpha-L-arabinofuranosidase"
FT                   /id="PRO_0000012217"
FT   DOMAIN          70..215
FT                   /note="CBM-cenC"
FT   ACT_SITE        380
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="alpha-L-arabinofuranose"
FT                   /ligand_id="ChEBI:CHEBI:28772"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="alpha-L-arabinofuranose"
FT                   /ligand_id="ChEBI:CHEBI:28772"
FT                   /evidence="ECO:0000250"
FT   BINDING         379..380
FT                   /ligand="alpha-L-arabinofuranose"
FT                   /ligand_id="ChEBI:CHEBI:28772"
FT                   /evidence="ECO:0000250"
FT   SITE            607
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   825 AA;  90184 MW;  9FF4EE99BE0C696E CRC64;
     MSRIRWRYGT AATALLVAAG LVPTATAHAE DVTDYSITVD PAAKGAAIDD TMYGVFFEDI
     NRAADGGLYA ELVQNRSFEY STDDNRSYTP LTSWIVDGTG EVVNDAGRLN ERNRNYLSLG
     AGSSVTNAGY NTGIRVEQGK RYDFSVWARA GSASTLTVAL KDAAGTLATA RQVAVEGGWA
     KYRATFTATR TSNRGRLAVA ANDAAALDMV SLFPRDTYRN QQNGLRKDLA EKIAALHPGF
     VRFPGGCLVN TGSMEDYSAA SGWQRKRSYQ WKDTVGPVEE RATNANFWGY NQSYGLGYYE
     YFRFSEDIGA MPLPVVPALV TGCGQNKAVD DEALLKRHIQ DTLDLIEFAN GPATSKWGKV
     RAEMGHPRPF RLTHLEVGNE ENLPDEFFDR FKQFRAAIEA EYPDITVVSN SGPDDAGTTF
     DTAWKLNREA NVEMVDEHYY NSPNWFLQNN DRYDSYDRGG PKVFLGEYAS QGNAWKNGLS
     EAAFMTGLER NADVVKLASY APLLANEDYV QWRPDLVWFN NRASWNSANY EVQKLFMNNV
     GDRVVPSKAT TTPDVSGPIT GAVGLSTWAT GTAYDDVKVT AADGATLLSD DFSGDASKWT
     HTGAGSWSVQ DGQYVQTDAA AENTMVQAGD PSWHDYDLHV KATKKSGKEG FLVAFGVKDT
     GNYYWWNLGG WNNTQSAVEQ AVDGGKGTLL TKAGSIETGR AYDIDVKVRG RQVTLYLDGQ
     EWGGFTDDKP AEPFRQVVTK DARTGDLIVK VVNAQPAEAR TAIDLGGARV ASTARVTTLA
     ADQDAVNTET DAPVTPATST FSGVTDRFTY TFPANSVTFL RLKQR
//