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Database: UniProt
Entry: A0A255T0S6_9BACT
LinkDB: A0A255T0S6_9BACT
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ID   A0A255T0S6_9BACT        Unreviewed;       658 AA.
AC   A0A255T0S6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
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=CIK99_03980 {ECO:0000313|EMBL:OYP58597.1};
OS   Prevotella sp. P5-92.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2024222 {ECO:0000313|EMBL:OYP58597.1, ECO:0000313|Proteomes:UP000216769};
RN   [1] {ECO:0000313|EMBL:OYP58597.1, ECO:0000313|Proteomes:UP000216769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P5-92 {ECO:0000313|EMBL:OYP58597.1,
RC   ECO:0000313|Proteomes:UP000216769};
RA   Accetto T., Nograsek B., Avgustin G.;
RT   "Comparative genomics of non-oral Prevotella species.";
RL   Submitted (AUG-2017) 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:OYP58597.1}.
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DR   EMBL; NPJG01000038; OYP58597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255T0S6; -.
DR   OrthoDB; 9758333at2; -.
DR   Proteomes; UP000216769; Unassembled WGS sequence.
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; IPR003305; CenC_carb-bd.
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   Pfam; PF02018; CBM_4_9; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216769};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..658
FT                   /note="non-reducing end alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012400510"
FT   DOMAIN          460..650
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   658 AA;  75034 MW;  D7FD536E8197F813 CRC64;
     MKLKTLGCAI ALASALAAQA QTNVMDINTK KVGAPVQNTM YGLFFEDINY AADGGLYGEL
     VKNRSFEFPQ SFMGWQVFGD VKLKNDGPFE RCPHYVTLSD PGHKERRTGI QNEGYFGIGV
     EKGESYRFTV WARAPKGKTT IRVQLIDQNT MEEHQEFTEN KLEIASADWK KYEVVVKSPR
     TFNHANLRIF LAGANPVDLE HVSLFPVNTF KNRQNGMRRD IAQALADIHP GLLRFPGGCI
     VEGVDLATRY QWKNTIGPVE NRPLNQNRWE HTFDYRYFPD YYQSYGLGFF EFFQLSEDIG
     AEPLPVLNVG MACQFQNWNQ ECAHAKMDEL EPFIQDCLDL IEFANGDENT EWGKKRIEMG
     HPAPFNMKYL GVGNEQWDEL YFKRLKPFVE RIRAKYPEIK IVGTSGPDSE GKMFDLGWEA
     MKSQKADLVD EHFYRPESWF LSHGLRYESY DRKGPKVFAG EYACHGKGKK WNHYETSLYE
     AAFMTDLERN ADVVYMTAYA PLLAHVDGWQ WRPDLIWFDN TKMFKTVSYY VQQMYAQNKG
     TNVLPLTMNK QFVAGQEGQN GLFASSVLDA KANTVIVKII NTGKTAQPVS VNLLGLKGEK
     SVKTITLSHN GLDDENSIDN PDKIRPVDGA MKCEAGKKNT ILNDVLQPMT FKLYIIEK
//
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