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Database: UniProt
Entry: W0LLC6_STRTL
LinkDB: W0LLC6_STRTL
Original site: W0LLC6_STRTL 
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}.
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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
//
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