ID F0C095_9XANT Unreviewed; 528 AA.
AC F0C095;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:EGD21057.1};
GN ORFNames=XGA_0251 {ECO:0000313|EMBL:EGD21057.1};
OS Xanthomonas hortorum ATCC 19865.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas; Xanthomonas hortorum pv. gardneri.
OX NCBI_TaxID=925777 {ECO:0000313|EMBL:EGD21057.1, ECO:0000313|Proteomes:UP000005023};
RN [1] {ECO:0000313|EMBL:EGD21057.1, ECO:0000313|Proteomes:UP000005023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19865 {ECO:0000313|EMBL:EGD21057.1,
RC ECO:0000313|Proteomes:UP000005023};
RX PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA Jones J.B.;
RT "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT and pepper.";
RL BMC Genomics 12:146-146(2011).
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:EGD21057.1}.
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DR EMBL; AEQX01000020; EGD21057.1; -; Genomic_DNA.
DR RefSeq; WP_006448577.1; NZ_AEQX01000020.1.
DR AlphaFoldDB; F0C095; -.
DR GeneID; 55512204; -.
DR PATRIC; fig|925777.8.peg.5607; -.
DR Proteomes; UP000005023; 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; cd08990; GH43_AXH_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..528
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003248877"
FT REGION 343..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 183
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 528 AA; 57915 MW; 1D598BC6D8B2F4EE CRC64;
MMRPFSRLLV LACGLLLASA PACAVQPPQG TQLHSPGNPI LADGSAYSAD PAPLVADGKL
YIIAGRDTAA PNLNAFVMPG WQMFVGSDPG SGEWTHYRDF LRPQQVFAWA DKRYAYASQI
VQGPDGRYYL YAPVQQRDSP NADPFAIGVA VADSPLGPWT DAHPQGPVIS QSVPGYNDIQ
NIDPTVMVDD DGRVYLYWGT FGALYGVELQ RDMVTFQGKP VLVDTLDGYF EAPWLFKRNG
TYYLAYAANN AGRLSPCTPT LYHACIAYAS APTPLGPWTY RGIVLPPVSS TTSHPGIVEF
QRRWYLVYHT ADAQGGGNFR RSVAIDRLDW DDSTQPASIR TVVPTRRPMP PAPPTRNQAP
SAYATASNDP DMPVQYWIAA LNDGIVKANP LPPEMWASWT DNNPPQQWLQ YSWAQPITVD
RTRIVFWADH PAGADVGVAP PARWHLEYRH AGRWQPVQPS DGYGTRTDHY EAVSFAPVTT
RCVRVVMDAS GNAASYAALA VQEWEVLAPQ PQRLPAATAA DSKRCDAP
//
