ID D6CYP9_9BACE Unreviewed; 329 AA.
AC D6CYP9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:CBK67301.1};
GN ORFNames=BXY_22280 {ECO:0000313|EMBL:CBK67301.1};
OS Bacteroides xylanisolvens XB1A.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=657309 {ECO:0000313|EMBL:CBK67301.1, ECO:0000313|Proteomes:UP000008795};
RN [1] {ECO:0000313|EMBL:CBK67301.1, ECO:0000313|Proteomes:UP000008795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XB1A {ECO:0000313|EMBL:CBK67301.1,
RC ECO:0000313|Proteomes:UP000008795};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Bernalier A.;
RT "The genome sequence of Bacteriodes xylanisolvens XB1A.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK67301.1, ECO:0000313|Proteomes:UP000008795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XB1A {ECO:0000313|EMBL:CBK67301.1,
RC ECO:0000313|Proteomes:UP000008795};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929033; CBK67301.1; -; Genomic_DNA.
DR AlphaFoldDB; D6CYP9; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; bxy:BXY_22280; -.
DR PATRIC; fig|657309.4.peg.1026; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_0_10; -.
DR Proteomes; UP000008795; 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 Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..329
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003082234"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
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 329 AA; 37778 MW; 4DC930423EAABDFA CRC64;
MKKYKMTKRL ILALGIIGLS VTGVRADSVN EKEITYADPT IYVENGKYYL TGTRNQEPQG
FAILESTDLE HWTVPDGTSL QLILRKGDRT YGEKGFWAPQ YFKDKRTYYF TYTANEQTVI
ASSKSVFGPF RQKEVKPIDA SAKNIDSFLF KDDDGKYYLY HVRFNKGNYL WVAEFDIKKG
SIKPETLKQC MDCTESWEKT PNYKSAPVME GPTVMKWDGV YYLFYSANHF MNIDYSVGYA
TASSPFGPWK KHPNSPIIHR SLVGENGSGH GDVFKGLDGK YYYVYHVHRS DSTVSPRKTR
IVPLILKKGN DGIYNITVDK EHVIKPMWK
//
