ID A0A087A1K7_9BIFI Unreviewed; 800 AA.
AC A0A087A1K7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-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};
GN ORFNames=BBIA_0338 {ECO:0000313|EMBL:KFI52657.1};
OS Bifidobacterium biavatii DSM 23969.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI52657.1, ECO:0000313|Proteomes:UP000029108};
RN [1] {ECO:0000313|EMBL:KFI52657.1, ECO:0000313|Proteomes:UP000029108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI52657.1,
RC ECO:0000313|Proteomes:UP000029108};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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}.
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:KFI52657.1}.
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DR EMBL; JGYN01000004; KFI52657.1; -; Genomic_DNA.
DR RefSeq; WP_033493356.1; NZ_JGYN01000004.1.
DR AlphaFoldDB; A0A087A1K7; -.
DR STRING; 1437608.GCA_000771645_02521; -.
DR eggNOG; COG3534; Bacteria.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000029108; Unassembled WGS sequence.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
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 InterPro; IPR010720; Alpha-L-AF_C.
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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000313|EMBL:KFI52657.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KFI52657.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029108}.
FT DOMAIN 461..793
FT /note="Alpha-L-arabinofuranosidase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00813"
FT REGION 758..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 86904 MW; 08EAB4E69C55D086 CRC64;
MTDKLVATLD KAGVRKVSTD LWGIFFEDIS YSGDGGLNSE LVQNGAFEYN RADKGDWSNY
TAWRKIVPAG SFAAFGVREA APVATENPHY AVVEVGSVDG GPVALENIGF DGMVFRAGET
YDFTVWARAH DRELPLTVAL VGDDGKPLAT AELTAPASYA GGDWSWLHAE LTVPAGDGET
AGDAGTADGK PVVASQGMLR VAFDQPGVID VDFVSCEPRT TYKGLEHFRP DLVKALDELH
PRFMRFPGGC ITHGLGMSNM YHWDTTIGDV EHRPHNFNVW GYHQSFRIGF YEYFRLCETI
GAKPLPVLPA GVSCQNTSQG PVPVAQEDMP AYIDEVLGLI DFCNADPATN KWAAKRAAMG
HPEPFGLEYL GIGNEDLIDD VFKSRFQQIF DAVKAAHPEI TVVGTVGPAP SGQDYEQGWA
YAREAQVPIV DEHSYQAPSW WFHNLDHYDD ADRQGPKVYL GEYGSWGTGL INGLSEAAFM
GRMELNGDVV HMASYAPLFC KNGHDSWNPN LIYFDNEHVY HPYSYWVQQM YATTTADTAW
PVALDGTTTF RRELPDTIGV KIDGGAHADF ADFSIETADG QRVDLPDVSY RGNGPIDLGV
NLHADAYTIR AKVTYHEGMW GVNIVSGDLA GKNHNRTSLG RGFGLGLIRD GAGYNIAGTE
VSMDAVRPGT VWDVRVDVTD RGEAMKLTIN GEVVAEGHEV PDEPRRTVSV SRDEVAGVDY
IRIVNALPEA ADVDLTQVLD ALGVSETARA NATANVLTGD DPYAGDKGAE SPTQPTAHEA
NLASGTYTAP AWSFTTLVIR
//
