ID   A0A0Q8XKT5_9SPHN        Unreviewed;       615 AA.
AC   A0A0Q8XKT5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Xylosidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASE13_18605 {ECO:0000313|EMBL:KRC78327.1};
OS   Sphingomonas sp. Root241.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC78327.1, ECO:0000313|Proteomes:UP000051629};
RN   [1] {ECO:0000313|EMBL:KRC78327.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC78327.1,
RC   ECO:0000313|Proteomes:UP000051629};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC78327.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC78327.1,
RC   ECO:0000313|Proteomes:UP000051629};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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:KRC78327.1}.
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DR   EMBL; LMIV01000004; KRC78327.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8XKT5; -.
DR   STRING; 1736501.ASE13_18605; -.
DR   Proteomes; UP000051629; 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:UniProtKB-KW.
DR   CDD; cd08986; GH43-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:SF5; ENDO-ARABINASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 2.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
PE   3: Inferred from homology;
FT   ACT_SITE        344
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        510
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            463
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   615 AA;  66581 MW;  79ACBE3EEADB1F5D CRC64;
     MAPPVLAQDL KKAVADDIFA DHPSMDRNAV VMPAPDAKPV APFFSERAIG DASVARTADG
     GWILTGTTLR SGVRHGIELW TSKDGKTWKG WGPAKVSGNG IVLDDVSERY LAPSVTVAGE
     RLHLAFSDKT GCARVATGLA ANPGGSFAAS PCLVEDASDV SLFVDRDGTG YLLWGGGNIA
     KLQPGFAQLA EAPRFLKPDQ ALFARHPPVG KDWPVRTRIG RSGATMFRDG DRYVLAASEV
     TGRMRTATED LFMAEGPTPY GPFGMRMLAV PHAGRGSIVR IEGGLAAAYN PKCDDGFALF
     CEQVGLVPLE RAPDGRLRQA ASVITEDSAV AARKPLITSE TMRDPSVTLG GDGFYYLVGT
     LDGYGYHKPD GGVKLWRSAD LKKWDEVGFI WRWEGMGYDF GKNIAELWAP EIKWVARDRT
     YYLAFSVMER SVGGKTWLYR STSGQAEGPY ANVTKSYLVK GIDGFPFEDD DGLYFLWGGG
     SIGRLNAARN GFEGSVRQLV DVDGDHVGYE GNGLIKVNGV YFLTGAEWHG PLRTHGTYDM
     MYGTSKSLFG PYSQRRMGAP HGGHGTAFAD KQGRYWYTMF GNDPTAPWRM KFGLVPIDIG
     DPASIGVPRI GTARE
//