ID   A0A1H7PN17_9BURK        Unreviewed;       326 AA.
AC   A0A1H7PN17;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Beta-xylosidase, GH43 family {ECO:0000313|EMBL:SEL37173.1};
GN   ORFNames=SAMN05216359_10869 {ECO:0000313|EMBL:SEL37173.1};
OS   Roseateles sp. YR242.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1855305 {ECO:0000313|EMBL:SEL37173.1, ECO:0000313|Proteomes:UP000198631};
RN   [1] {ECO:0000313|EMBL:SEL37173.1, ECO:0000313|Proteomes:UP000198631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR242 {ECO:0000313|EMBL:SEL37173.1,
RC   ECO:0000313|Proteomes:UP000198631};
RA   de Groot N.N.;
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; FOAV01000008; SEL37173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7PN17; -.
DR   STRING; 1855305.SAMN05216359_10869; -.
DR   OrthoDB; 177947at2; -.
DR   Proteomes; UP000198631; 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; 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};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187}.
FT   REGION          249..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        24
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            143
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   326 AA;  36360 MW;  DF6D365AC5F844A2 CRC64;
     MNPSPALAPA APTVLAPLIP QRADPHLTRH TDGWYYFTAS VPAYDRIELR RARRWQDLAQ
     AETVTAWQKP DTGAWSELVW APELHHHDGA WYVYFAAAPS RAIVGGLFQH RMYALRNPSP
     NPLEGEWTFL GQVATGLDSF SLDATTFSHR GQLYYLWAQK DPAIAGNSNL YIAPMSNPWT
     LAGPPVLLSR PEYDWECRGF LVNEGPSVLK RNGKVFISYS ASATDQNYAM GLLWADEQAD
     PLDPASWHKS PTPVLTTSPT QPIFGPGHNS FSLDEDGQTV LLVYHARTYT EIEGDPLWNP
     DRHTFVKRLC WDAQGMPVFG DAGLAD
//