ID A0A1H4PJV3_9ACTN Unreviewed; 825 AA.
AC A0A1H4PJV3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN ORFNames=SAMN05216482_2008 {ECO:0000313|EMBL:SEC07382.1};
OS Streptomyces sp. PAN_FS17.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855351 {ECO:0000313|EMBL:SEC07382.1, ECO:0000313|Proteomes:UP000199275};
RN [1] {ECO:0000313|Proteomes:UP000199275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAN_FS17 {ECO:0000313|Proteomes:UP000199275};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 Evidence={ECO:0000256|ARBA:ARBA00001462};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family.
CC {ECO:0000256|ARBA:ARBA00007186}.
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DR EMBL; FNTN01000001; SEC07382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4PJV3; -.
DR STRING; 1855351.SAMN05216482_2008; -.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000199275; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000199275};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..825
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011650814"
FT DOMAIN 466..816
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
SQ SEQUENCE 825 AA; 90053 MW; 7BF3B73E851D38A0 CRC64;
MPRIRWRDGA AATALLVAVG LVPTATAHAE DVTDYSITVD PAARGASIDD TMYGVFFEDI
NRAADGGLYA ELVQNRSFEY STADNGSYTP LTSWTVAGAG QVVNDAGRLN ERNRNYLSLG
AGSSVTNAGY NTGIRIEQGK RYDFSVWARA DSGTTLTVAL KDAAGALATA RQMAVKGGWA
KYRATFTSTR TSNRGRLAVA ATDAAALDMV SLFPRDTYRN QQNGLRKDLA EKIAALHPGF
VRFPGGCLVN TGSMEDYSAA SGWQRKRSYQ WKDTVGPVEE RATNANFWGY NQSYGIGYYE
YFRFSEDIGA MPLPVVPALV TGCGQNRAVD DEALLKRHIQ DTLDLIEFAN GPATSKWGKV
RAEMGHPRPF RLTHLEVGNE ENLPDEFFDR FKQFRAAIEA RYPDITVVSN SGPDDAGTTF
DTAWKLNREA NVEMVDEHYY NSPNWFLQNN DRYDSYDRSG PKVFLGEYAS QGNAWKNGLS
EAAFMTGLER NADVVKLASY APLLANEDYV QWRPDLVWFN NRASWNSANY EVQKLFMNNV
GDRVVPSKAT TTPDVSGPIA GAVGLSTWAT SAAYDDVKVT AADGATLLSD DFSGDASKWT
QTGAGSWSVQ DGQYVQTDEA AENTMVQAGD PSWHDYDLHV KATKKSGKEG FLVAFGVKGT
GNYYWWNLGG WNNTQSAVEQ AVDGGKGTLL TKAGSIETGR AYDIDVKVRG RQVTLYLDGQ
EWGGFTDDKP AEPFRQVVTR DTATGELIVK VVNAQPAEAR TGIDLGGARV ASTARVTTLA
ADQDAVNTET DAPVTPATST FSGVTDRFTY TFPANSVTFL RLKQR
//