ID A0A0N0ARG3_9PSEU Unreviewed; 470 AA.
AC A0A0N0ARG3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=ADK67_28155 {ECO:0000313|EMBL:KOX20934.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX20934.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX20934.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX20934.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-2015) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOX20934.1}.
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DR EMBL; LGED01000214; KOX20934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0ARG3; -.
DR STRING; 1415542.ADK67_28155; -.
DR PATRIC; fig|1415542.3.peg.6080; -.
DR OrthoDB; 4241492at2; -.
DR Proteomes; UP000037722; Unassembled WGS sequence.
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:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08987; GH62; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR PANTHER; PTHR40631:SF1; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..470
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039418979"
FT DOMAIN 30..139
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 140..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 49391 MW; F664A743DCACB008 CRC64;
MTRSRTATVG AAVASAALLA SAATLVALPA GAAAAGCSVN YAVASQWQGG FTGNVSITNL
GDPLTGWTLT WSFGAGQAVT QSWNTSLTQS GAAVTAKNVS YNGSIATGGS ASFGFNGSWT
GSNPIPTSFA LNGVACTGST TTTTTTSTTS TSTSTTTSTT TTTTTPVTCA LPSRYRWSSS
GALANPRSGW VSLKDFTYVP YNGKHLVYGT THDFGTSWGS MNFGLFSNWS EMASAPQQAM
NSGTVAPTLL YFAPKNIWVL AYQWGGTAFS YRTSTDPTNP NGWSAQQVLS TASITGSGTG
PIDQTLIGDG QNMYLFFAGD NGKIYRQVMP LGNFPSSFGS SYTTIMSDTT NNLFEAVEVY
KLQGQNQYLM IVEAIGANGR YFRSFTSSSL SGSWTPQAAT ESNPFAGKAN SGATWTNDIS
HGDLLRTNPD QTKTVDPCNL QLLYQGRDPR SDGVDYGLLP YRPGLLTLQR
//