ID   D5EXR4_PRER2            Unreviewed;       868 AA.
AC   D5EXR4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
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=PRU_0525 {ECO:0000313|EMBL:ADE81175.1};
OS   Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Xylanibacter.
OX   NCBI_TaxID=264731 {ECO:0000313|EMBL:ADE81175.1, ECO:0000313|Proteomes:UP000000927};
RN   [1] {ECO:0000313|EMBL:ADE81175.1, ECO:0000313|Proteomes:UP000000927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19189 / JCM 8958 / 23 {ECO:0000313|Proteomes:UP000000927};
RX   PubMed=20585943; DOI=10.1007/s00248-010-9692-8;
RG   North American Consortium for Rumen Bacteria;
RA   Purushe J., Fouts D.E., Morrison M., White B.A., Mackie R.I.,
RA   Coutinho P.M., Henrissat B., Nelson K.E.;
RT   "Comparative genome analysis of Prevotella ruminicola and Prevotella
RT   bryantii: insights into their environmental niche.";
RL   Microb. Ecol. 60:721-729(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}.
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DR   EMBL; CP002006; ADE81175.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5EXR4; -.
DR   STRING; 264731.PRU_0525; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   KEGG; pru:PRU_0525; -.
DR   eggNOG; COG3534; Bacteria.
DR   HOGENOM; CLU_010060_2_0_10; -.
DR   Proteomes; UP000000927; Chromosome.
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   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; IPR013320; ConA-like_dom_sf.
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; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:ADE81175.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADE81175.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000927};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..868
FT                   /note="non-reducing end alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003071446"
FT   DOMAIN          478..820
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   868 AA;  97631 MW;  54088311A1A9C493 CRC64;
     MIITIFLKRY YFETIMNCKK SLFMGCWAAM AATAQAQITI DIDAQQRGPK VSPMLYGIFY
     EDINHAADGG IYAELIRNRS FEDGPRFGAP ADMQGWATVA AEPSVLAARL IQDSKKTPLL
     NSAQHHALQL DVKASPAAPV SLINEGYWGI NAVQGRTYRL SFWAKAPAYR GTVKAELRSA
     DGKQVYAQQQ VAVFAAAKKR GWTKYEATLT ALDNDAQAQF ALVFDGVGQV QLDMVSLFPP
     TFRNRENGMR PDLANMLWQL HPKFMRFPGG CFVEGQESPD NAFRWQRTIG PVEEREGHWN
     VNWGYRTTDG LGYHEYLQLA EDLVAKPLYV VNVGIWHGGQ TPYDSIQPWI DECLNALEYA
     NGPVSSKYGA MRAKNGHPEP FGIEYLEVGN ENNQPDPRQQ SDHYYERYEQ FYNAIKAKYP
     DMKIIGNVVA WGDDNPKWGS SLPVDLLDEH YYRSPDWFAD AFHKYDSYDR QGPKVYVGEY
     AVTNGYGTLG NMNAALGEAI YMMGMENNAD VVELASYAPI FVNENDARWR PDMIRFSSSR
     AMGTPSYYVQ QLMPQHLGTQ VLKVQLTNPY KDKVVKQITP KQSRVGYGTW NTRATFQCDK
     EVDCMYGDWQ IEGGMLHQTG HKDATRCIQK DVIDGDHYTC KFRCRKDEGA EGFIVIFNYV
     DDKNYCWVNL GGWTNSQHAI EQISNGGKLL TDSKRGRIEA GRWYDVTLQV AGDSVKVWLD
     NEQLFDTVLK RDHTKGIYSS ATINDATGEI IVKVVNNDDA ATTARISLKN FAPSEARVVR
     LAANDGMEEN TLQQPTTIHP VEQQLSTADD HVMLTVPPYS LNIVTIKTDD YLFSKGISTA
     NNETASTLIS GKGPLYRRKI VGQEATTF
//