ID   A0A1I0T6K5_9SPHI        Unreviewed;       341 AA.
AC   A0A1I0T6K5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Beta-xylosidase, GH43 family {ECO:0000313|EMBL:SFA46666.1};
GN   ORFNames=SAMN04488511_10635 {ECO:0000313|EMBL:SFA46666.1};
OS   Pedobacter suwonensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=332999 {ECO:0000313|EMBL:SFA46666.1, ECO:0000313|Proteomes:UP000198836};
RN   [1] {ECO:0000313|Proteomes:UP000198836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18130 {ECO:0000313|Proteomes:UP000198836};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOJM01000006; SFA46666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0T6K5; -.
DR   STRING; 332999.SAMN04488511_10635; -.
DR   OrthoDB; 177947at2; -.
DR   Proteomes; UP000198836; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18820; GH43_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};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..341
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011658051"
FT   SITE            146
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   341 AA;  38432 MW;  BEFBC52C0030057A CRC64;
     MNKLKIKLWF ALCLLVIGGL NAQTFTNPLL PSGADPYSYY KDGYYYYTHT TGNRIDLWKT
     KTLAGLKDAE RKTIWKAPAE TMYSKEIWAP EVMFLRGKWY AYFAADDGRN ENHRMYVLEN
     ASADPMKGEW IFKGKISDPT DKWAIDGDVI DFKGQLYMIW SGWEGDKNGK QEIFIARLKN
     PWTVDGQRVK ISTPKFDWEK NGDLGGGEHV DVNEGPQFLV HGGKVFIIYS ASGCWTDFYA
     LGMLSASAKS NLLDPASWTK FTKPVFQQSP KDGVYAPGHN SFFKSPDGKE DWILYHANDK
     PGQGCGGFRS PRAQKFYWNS DGTPNFGTPV KAGARLASPS N
//