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Database: UniProt
Entry: A0A089I030_9BACL
LinkDB: A0A089I030_9BACL
Original site: A0A089I030_9BACL 
ID   A0A089I030_9BACL        Unreviewed;       793 AA.
AC   A0A089I030;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=H70357_13905 {ECO:0000313|EMBL:AIQ17631.1};
OS   Paenibacillus sp. FSL H7-0357.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536774 {ECO:0000313|EMBL:AIQ17631.1, ECO:0000313|Proteomes:UP000029508};
RN   [1] {ECO:0000313|EMBL:AIQ17631.1, ECO:0000313|Proteomes:UP000029508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0357 {ECO:0000313|EMBL:AIQ17631.1,
RC   ECO:0000313|Proteomes:UP000029508};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP009241; AIQ17631.1; -; Genomic_DNA.
DR   RefSeq; WP_038590033.1; NZ_CP009241.1.
DR   AlphaFoldDB; A0A089I030; -.
DR   STRING; 1536774.H70357_13905; -.
DR   KEGG; paeh:H70357_13905; -.
DR   eggNOG; COG3534; Bacteria.
DR   HOGENOM; CLU_010060_2_0_9; -.
DR   Proteomes; UP000029508; 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; 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}.
FT   DOMAIN          441..786
FT                   /note="Alpha-L-arabinofuranosidase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00813"
SQ   SEQUENCE   793 AA;  88317 MW;  D9B24E45DDB25D09 CRC64;
     MKTEGTLTVH TGRRGAELSD LFGIFFEDLN HAADGGLYAE LVQNRSFEFD PIDKADYHAL
     TAWEPVIRGD GQAVITVEDK EPLNPRNLHY AVIDIVSEGG GVGIMNLGFN SGIPVKEGDN
     YKFSMYARRD NSWDTPLTVT IEAVDGTVYG AAKITVNSSE WTRYEAVIQA NSTDNSSRLV
     ILAGGSGKVC LDMVSLFPEK TFLNRPGGLR EDLSMLLADM KPKFMRFPGG CLIHDGSLNP
     DDRNSMYRWK NTIGDIAQRP PRRNNWSYNQ TLGLGYLEYF QFCEDIGAKP IPVLPGGYDP
     HHKRIVPLDE LQPWIDDALD LIEFANGDSS TEWGGIRAGL GHTEPFGLEY IGIGNEEVGE
     PFFERYPFFH EAIKAKYPEI KVINSSGPFS AGKEYERGWA SARANGSDLV DEHYYAAPEW
     FLANHHRYDE FKAGEPKVFL GEYASWGNTY YNALVEAAFM TGLQNNAHAV GLACYAPMLC
     NVDYVNWKPD MIWFNNHQAY GTANYYVQKL FMNHQGDQLL EMRSCGFAPA QAQEDQPITG
     AITLAVDASA ARFSEITLVN NLTGEVKAYA DLSGEVADLP DPALNGAAKR TLELGPTHWT
     NYTLSLKAVR TGGAKGFVLY FGKADEQNHL FWEIGGWQNQ DSIVASIAQG RNSVLTHTLF
     TVESDVEYYL TLEVSGRQIR TYIDGELINE AEDKLPVIEP LYYTASVEHS TGDMILKTVN
     MQEVSVTAEI VLEGLADKRL SIEVYEMSGH QPEDENSFEQ PMLVSPKQKA LQTEGSSFAY
     EFPKQSVTVM RLR
//
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