EABF_STRCX
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 03-AUG-2022, entry version 78.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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; 2.60.40.1180; -; 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 Pfam; PF06964; Alpha-L-AF_C; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF51445; SSF51445; 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
