ID W0LLC6_STRTL Unreviewed; 328 AA.
AC W0LLC6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
DE Flags: Fragment;
GN Name=araf62A {ECO:0000313|EMBL:AHG24944.1};
OS Streptomyces thermoviolaceus subsp. apingens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66859 {ECO:0000313|EMBL:AHG24944.1};
RN [1] {ECO:0000313|EMBL:AHG24944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 19283 {ECO:0000313|EMBL:AHG24944.1};
RX PubMed=24951792; DOI=10.1128/AEM.00685-14;
RA Wang W., Mai-Gisondi G., Stogios P.J., Kaur A., Xu X., Cui H., Turunen O.,
RA Savchenko A., Master E.R.;
RT "Elucidation of the molecular basis for arabinoxylan-debranching activity
RT of a thermostable family GH62 alpha-l-arabinofuranosidase from Streptomyces
RT thermoviolaceus.";
RL Appl. Environ. Microbiol. 80:5317-5329(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KF958299; AHG24944.1; -; Genomic_DNA.
DR AlphaFoldDB; W0LLC6; -.
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 GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08987; GH62; 1.
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; PF03664; Glyco_hydro_62; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000313|EMBL:AHG24944.1};
KW Hydrolase {ECO:0000313|EMBL:AHG24944.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AHG24944.1"
SQ SEQUENCE 328 AA; 35914 MW; F5950C2410533C96 CRC64;
TVVPSDDVQG TGRQSQLTDG FGTRASCELP STYRWTSTGA LAQPRSGWVS LKDFTVVPYN
GQHLVYATTH DTGTRWGSMN FEPFGDWSQM ATARQNAMNS PTVAPTLFYF APKDIWVLAY
QWGGSAFSYR TSHDPTDPNG WSSEQVLFSG SIADSATGPI DQTLIGDDTH MYLFFAGDNG
KIYRASMPIG DFPGSFGSTA TVVMSDTRNN LFEAPQVYKL QGQNRYLMIV EAIGAQGQRY
FRSFTATSLD GEWTPQATSE SNPFAGKANS GATWTDDISH GELIRTTADQ TMTVDPCNLQ
LLYQGRDPGS GGTYDLLPYR PGLLTLQR
//