ID   XYNB_PRUPE              Reviewed;         461 AA.
AC   P83344;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Putative beta-D-xylosidase;
DE            EC=3.2.1.-;
DE   AltName: Full=PpAz152;
DE   Flags: Fragment;
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000312|EMBL:AAM00218.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RC   STRAIN=cv. Springcrest; TISSUE=Abscission zone;
RX   PubMed=11847241; DOI=10.1093/jexbot/53.368.429;
RA   Ruperti B., Cattivelli L., Pagni S., Ramina A.;
RT   "Ethylene-responsive genes are differentially regulated during abscission,
RT   organ senescence and wounding in peach (Prunus persica).";
RL   J. Exp. Bot. 53:429-437(2002).
CC   -!- FUNCTION: May be involved in cell wall metabolism, related to
CC       senescence. {ECO:0000303|PubMed:11847241}.
CC   -!- TISSUE SPECIFICITY: Equally expressed in the abscission zone and
CC       surrounding tissues of both fruitlets and leaves.
CC       {ECO:0000269|PubMed:11847241}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during both the early and late stages of
CC       fruit ripening and during leaf senescence.
CC       {ECO:0000269|PubMed:11847241}.
CC   -!- INDUCTION: Up-regulated in both the abscission zone and surrounding
CC       tissues after wounding due to embryoctomy.
CC       {ECO:0000269|PubMed:11847241}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; AF362990; AAM00218.1; -; mRNA.
DR   AlphaFoldDB; P83344; -.
DR   SMR; P83344; -.
DR   STRING; 3760.EMJ26867; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   eggNOG; ENOG502QQ55; Eukaryota.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; TAS:UniProtKB.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR044993; BXL.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42721; PTHR42721; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase.
FT   CHAIN           <1..461
FT                   /note="Putative beta-D-xylosidase"
FT                   /id="PRO_0000210807"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAM00218.1"
SQ   SEQUENCE   461 AA;  49516 MW;  E051FF8C275D9921 CRC64;
     ADAIKAGLDL DCGPFLAIHT EAAVRRGLVS QLEINWALAN TMTVQMRLGM FDGEPSAHQY
     GNLGPRDVCT PAHQQLALEA ARQGIVLLEN RGRSLPLSTR RHRTVAVIGP NSDVTVTMIG
     NYAGVACGYT TPLQGIGRYT RTIHQAGCTD VHCNGNQLFG AAEAAARQAD ATVLVMGLDQ
     SIEAEFVDRA GLLLPGHQQE LVSRVARASR GPTILVLMSG GPIDVTFAKN DPRISAIIWV
     GYPGQAGGTA IANVLFGTAN PGGKLPMTWY PQNYVTHLPM TDMAMRADPA RGYPGRTYRF
     YIGPVVFPFG LGLSYTTFAH NLAHGPTLVS VPLTSLKATA NSTMLSKTVR VSHPDCNALS
     PLDVHVDVKN TGSMDGTHTL LVFTSPPDGK WASSKQLMGF HKIHIATGSE KRVRIAVHVC
     KHLSVVDRFG IRRIPLGEHK LQIGDLSHHV SLQTNLGEIK V