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Database: UniProt
Entry: A0A1G7J495_9BACT
LinkDB: A0A1G7J495_9BACT
Original site: A0A1G7J495_9BACT 
ID   A0A1G7J495_9BACT        Unreviewed;       655 AA.
AC   A0A1G7J495;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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=SAMN05216518_10433 {ECO:0000313|EMBL:SDF19614.1};
OS   Bacteroidales bacterium KHT7.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1855373 {ECO:0000313|EMBL:SDF19614.1, ECO:0000313|Proteomes:UP000198526};
RN   [1] {ECO:0000313|EMBL:SDF19614.1, ECO:0000313|Proteomes:UP000198526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KHT7 {ECO:0000313|EMBL:SDF19614.1,
RC   ECO:0000313|Proteomes:UP000198526};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNBQ01000004; SDF19614.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7J495; -.
DR   STRING; 1855373.SAMN05216518_10433; -.
DR   OrthoDB; 9758333at2; -.
DR   Proteomes; UP000198526; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198526};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..655
FT                   /note="non-reducing end alpha-L-arabinofuranosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011523326"
FT   DOMAIN          459..648
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   655 AA;  74093 MW;  8E4EA40C7193E3CA CRC64;
     MKSLLTTLAF ATAISASAQN NITVNAQKLG APIPKTMYGI FFEDINFAAD GGLYAELVKN
     RSFEFPNHLQ GWTAFGKFEV RNDNPAYDRN PNYVRLIPVG HRHKRTGLEN SGFFGIGLKK
     GEEYRITFTA RRTDDKDATI RIQLIDPSNM GEVQFIQEKE AKIAIDSKEW KKYTAIIKSK
     ATIDKAHLRV LHAGASAVDI DHISLFPVDT WKGHENGMRK DLAQALADLK PGVFRFPGGC
     IVEGTEEGDR YNWKNSVGAV ENRPLNLNRW QYTFEHRFYP DYYQSYGLGF YEYFLLSEEI
     GAEPLPILSC GLVCQYQNND KVHTPVEELK PYIQDALDLI EFANGATTTT WGKLRAEMGH
     PEPFNLKYIG IGNEQWGDIY PAHLKPFIDA LRKAHPEVKI VGSSGPDSEG KKFDYLWPEM
     KKLKADLVDE HFYRPADWFL KSGNRYDNYD RKGPKVFAGE YACHIKGKKY NQFYASLLEA
     AFMTGLERNA DVVEMATYAP LFAHVEGWQW RPDLIWFDNL RSFRSCSYLV QQLYSHYKGS
     NVVSLTMDNK PVAGNEGQNG LFASAVFDKA SSSYIVKVAN TSKEPQPLKV NFKLKNKKQK
     LAGAHVITLQ SDNLEAENTL DEPNKISTKE SNMTISGNCL DTTIAPETFA VYIVK
//
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