ID   V9G3H5_9BACL            Unreviewed;       420 AA.
AC   V9G3H5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:GAE04106.1};
GN   ORFNames=JCM10914_135 {ECO:0000313|EMBL:GAE04106.1};
OS   Paenibacillus sp. JCM 10914.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE04106.1, ECO:0000313|Proteomes:UP000018028};
RN   [1] {ECO:0000313|EMBL:GAE04106.1, ECO:0000313|Proteomes:UP000018028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE04106.1,
RC   ECO:0000313|Proteomes:UP000018028};
RA   Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA   Hattori M.;
RT   "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT   sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL   Genome Announc. 2:e01144-13(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAE04106.1}.
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DR   EMBL; BAUO01000001; GAE04106.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9G3H5; -.
DR   STRING; 1236974.GCA_001315105_00139; -.
DR   Proteomes; UP000018028; 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; cd09002; GH43_XYL-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR   PANTHER; PTHR42812:SF2; XYLOSIDASE_ARABINOSIDASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 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   Reference proteome {ECO:0000313|Proteomes:UP000018028}.
FT   ACT_SITE        16
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        165
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            110
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   420 AA;  47013 MW;  BF2418D9A28250CC CRC64;
     MTTGTEMLII GGNFADPSVI RVGEDYYMTH SSYKLTPGLI IWHSRDLLHW NRFSAALMTY
     VGDVWAPDFV HHEGKFYIYF PAGRSNWVVT AQNPAGPWSE PIDLGIKGID PGHTVGPDGK
     RYLHMSGGGF VELTDDGLAV AGEVSQVYEG WKYPQEWVVE AYSLEGPKVT YHEGYYYLTV
     AVGGTAGPPT SHMAVSSRSR TPWGPWEHSP YNPIIHTRSS AEPWWSKGHA SLIDTPAGEW
     WIVYHAYAGG YHTLGRQTLL ERVEWTADGW FRISDGLAMN SVDTPLLTSF HDDFESTALG
     FEWQCEGMNP AERFRYDSGQ LSVEGTAENE LHSPLFFMPM HERYEVEVEV RVKGNAEGRL
     LLYYNESAYL GIGLHAKGVS HFRSFKGYGT MNHDGGHAYL RIVNDAISYP SIIASMVDHG
//