ID A0A0E4HC61_9BACL Unreviewed; 320 AA.
AC A0A0E4HC61;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Alpha-N-arabinofuranosidase 2 {ECO:0000313|EMBL:CQR54304.1};
DE EC=3.2.1.55 {ECO:0000313|EMBL:CQR54304.1};
GN ORFNames=PRIO_1894 {ECO:0000313|EMBL:CQR54304.1};
OS Paenibacillus riograndensis SBR5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus;
OC Paenibacillus sonchi group.
OX NCBI_TaxID=1073571 {ECO:0000313|EMBL:CQR54304.1, ECO:0000313|Proteomes:UP000033163};
RN [1] {ECO:0000313|Proteomes:UP000033163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; LN831776; CQR54304.1; -; Genomic_DNA.
DR RefSeq; WP_046502010.1; NZ_LN831776.1.
DR AlphaFoldDB; A0A0E4HC61; -.
DR STRING; 483937.AMQ84_15330; -.
DR KEGG; pri:PRIO_1894; -.
DR PATRIC; fig|1073571.4.peg.1989; -.
DR HOGENOM; CLU_009397_2_1_9; -.
DR Proteomes; UP000033163; Chromosome I.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18817; GH43f_LbAraf43-like; 1.
DR InterPro; IPR016828; Alpha-L-arabinofuranosidase.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF025414; Alpha-L-arabinofuranosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:CQR54304.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:CQR54304.1}.
FT SITE 136
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 320 AA; 36497 MW; C756EFAECC881418 CRC64;
MSRKKEYSNP LVEQRADPWV YKHTDGYYYF TASVPEYDRI EVRRAATIEG LRGAEPVVAW
RKYETGPLSA NIWAPEIHYI HGKWYIYFAA ARTTETKEGL FDHRMYALEN ESANPLEGRW
VEKGQVKTAW ESFALDATAF QHKGVLYYVW AQKDPDIPGN SNLYISEMEN PWTLTGPQTM
IAKPEHPWEI IGFSVNEGAA VLKRNGKIFM SFSASATDHN YCMGLLTADE DSDLLDAASW
SKHPEPVFQT SEANGQFGPG HNSFTVNENG EDVLIYHCRN YKEITGDPLY DPNRHTRAQV
LEWNEDGTPN FGVPVKDGRE
//
