ID D6ZWS7_BIFLJ Unreviewed; 786 AA.
AC D6ZWS7;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN OrderedLocusNames=BLJ_1910 {ECO:0000313|EMBL:ADH01333.1};
OS Bifidobacterium longum subsp. longum (strain JDM301).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=759350 {ECO:0000313|EMBL:ADH01333.1, ECO:0000313|Proteomes:UP000006740};
RN [1] {ECO:0000313|EMBL:ADH01333.1, ECO:0000313|Proteomes:UP000006740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM301 {ECO:0000313|EMBL:ADH01333.1,
RC ECO:0000313|Proteomes:UP000006740};
RX PubMed=20525832; DOI=10.1128/JB.00538-10;
RA Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P.,
RA Wang S., Guo X.K.;
RT "Complete genome sequence of Bifidobacterium longum JDM301.";
RL J. Bacteriol. 192:4076-4077(2010).
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}.
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; CP002010; ADH01333.1; -; Genomic_DNA.
DR RefSeq; WP_013141420.1; NC_014169.1.
DR AlphaFoldDB; D6ZWS7; -.
DR CAZy; GH51; Glycoside Hydrolase Family 51.
DR KEGG; bll:BLJ_1910; -.
DR HOGENOM; CLU_010060_2_0_11; -.
DR Proteomes; UP000006740; Chromosome.
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; 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 SMART; SM00813; Alpha-L-AF_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 448..779
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
SQ SEQUENCE 786 AA; 86099 MW; 433661D11D6E6860 CRC64;
MTDKLIATLD KAGVRAISTD LWGIFFEDIS YSGDGGLNAD LVQNGAFEYN RADSAEWSNY
SFWRKIVPDG SFAAFCIHDI DPVAVENPHY ATVEIEQAPA ALDNTGWDGM VFHAGETYDF
TAWMRVRSGS AMPVTVSLHG DDGSIISETT ITVTASAWTT YQASLTVPES GEEDGKAGAS
VSTQGTLRLT FGGEGVIDLD FITLEPRTTY HGLKHFRPDL VKALADLKPR FMRFPGGCIT
HGLGMDNMYH WDRTIGPVEH RPHNFNLWGY HQSFRIGYYE YLCLCETIGA KPLPVLPAGV
SCQNTSQGPV PVAQEDMPAY IDEVLHLIEF CNGGTDTEWG AKRAAMGHPE PFGLEYLGIG
NEDLIDDVFK NRFQQIFDAV KAAYPDIVVV GTVGPSPSGK DYEEGWKHAR EAGLPIVDEH
SYQSSSWWFH NLDHYDHTDR KGPKVYLGEY GSWNTQLING LSEAAFMGRM ELNGDVVAMA
SYAPLFAKNS HHSWNPDLIY FDNERAYHPY SYWVQQMYAT TTADTAWPVA VEGPSTLRRT
LPDTVRLRIA GNAKADFNNL TVTTASGETV NLGDVSYDGR TIDTPLDLHT DAYSIDATVV
YYEGKWGMDL ICGDIDGKNH NIVSFGRGHS VRVVRDGTAY ALAGTEVSMN EVLPGTTWQV
HADVTGRGQA MKLYIDGTLI ADGTEVKDEP RRTVTVSRNA KAGETYVRVV NAMDEPVDVD
LSQILAGLDV SAQSAATATA TILAGNDPYA GQVGEESPTK PVNTPLDLMD GTYAAPAWSF
TVIALK
//
