ID A0A1H1ECR0_9ACTN Unreviewed; 680 AA.
AC A0A1H1ECR0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN04489718_2476 {ECO:0000313|EMBL:SDQ86414.1};
OS Actinopolyspora saharensis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=995062 {ECO:0000313|EMBL:SDQ86414.1, ECO:0000313|Proteomes:UP000199301};
RN [1] {ECO:0000313|EMBL:SDQ86414.1, ECO:0000313|Proteomes:UP000199301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45459 {ECO:0000313|EMBL:SDQ86414.1,
RC ECO:0000313|Proteomes:UP000199301};
RA de Groot N.N.;
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; FNKO01000002; SDQ86414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1ECR0; -.
DR STRING; 995062.SAMN04489718_2476; -.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000199301; 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; 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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..680
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011478914"
FT DOMAIN 485..663
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 75252 MW; A7C3CC91F5E33DE7 CRC64;
MSRLQPAFGL ITAALLGATL APAAAGASES PAPEHSLRIN TSGETTSIPE TMHGVFYEDI
NDAADGGLYA EKVRNRSFEY DEVDNPSYTP MTAWEPTSTG GASGTTEVLD DSERLNENNR
RYLRLELNGD GRRDSAYGVT NAGYHSGMAL KRGEKYDFSI WARSDQPGGT PLSVTATDGS
GSPVGRTMRL QVRGDEWTEY TGTFAAHSDT DTGGLRVLAH GSGTVRMDMV SLFPRETFKG
EPNGLRKDLA SKIEALDPGF LRFPGGCLVN TGSHESYQAP DWERRRSYQW KDTVGPVEQR
PTNANFWGYN QSYGLGFYEY FRFAENIGAM PLPVVPALVT GCGEDKATHD PQLLQRHIQD
TLDLIQFANG SVDTEWGAKR AAMGHPEPFS LTHLAVGNEE NLPEDFYEHF EKFRDAIEQR
YPGITVVANS GPDDSGATFD RAWELAREQN AEMVDEHYYN NPQWFLENTE RYDSYDRSGP
KVSLTEFASE GNRFENALAE AAYMTGLERN ADVVRMSSYA PLLAHEDSPQ WTPDMIWFDN
DESWGSTSYE AQKLFANNVG DEVVPSELAR SDEKNGVKPV YQVVTRDDRT GELIVKVVNA
RDDAARVRLN IEGADEVAPA AELTTLHGDP DAVNTKGSQP IRPEHSTVQG VSQQFEHTFP
AHSISFMRIK TPGDRPRTDS
//
