ID A0A1X9Z092_9SPHI Unreviewed; 325 AA.
AC A0A1X9Z092;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:ARS38431.1};
GN ORFNames=CA265_01505 {ECO:0000313|EMBL:ARS38431.1};
OS Sphingobacteriaceae bacterium GW460-11-11-14-LB5.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae.
OX NCBI_TaxID=1986952 {ECO:0000313|EMBL:ARS38431.1, ECO:0000313|Proteomes:UP000194429};
RN [1] {ECO:0000313|Proteomes:UP000194429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ray J., Price M., Deutschbauer A.;
RL Submitted (MAY-2017) 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; CP021237; ARS38431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9Z092; -.
DR KEGG; sbx:CA265_01505; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000194429; Chromosome.
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; cd08991; GH43_HoAraf43-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000194429};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..325
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012801583"
FT ACT_SITE 33
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 138
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 325 AA; 36759 MW; 32448E8D04CBB6F5 CRC64;
MKYLFAFFLY CFVFSIGKNA FAKQLNDTIY LADPTIFLDK GIYYLYGTSG DEGFMVYASR
DLKNWTKPAG KNKGFALKKG DAFGTKGFWA PQVFKKGKTY FMAYTADEQI AIAHSNSPTG
PFVQKELKAI SGIGKQIDPF VFTDTDGKNY LYHVKLDQGN RIFVAELKHD FSDVIPETTK
FCLSGTEPWE NTAKTDWPVT EGPTVLKKNN LYYLFYSAND FRNPDYAVGY ATSGSATGPW
LKYTGNPIIS KKTLQLNGTG HGDFFTDKSG QLQYVFHTHY TNHKVSPRAT AVVKAAFVKD
KNDRYHMQID AESFRFLRQS VAKTF
//
