ID   XYL2_MEDSV              Reviewed;         774 AA.
AC   A5JTQ3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Beta-xylosidase/alpha-L-arabinofuranosidase 2 {ECO:0000303|PubMed:17615411, ECO:0000312|EMBL:ABQ45228.1};
DE   AltName: Full=Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 2;
DE            Short=MsXyl2 {ECO:0000303|PubMed:17615411};
DE   Includes:
DE     RecName: Full=Beta-xylosidase;
DE              EC=3.2.1.37;
DE     AltName: Full=1,4-beta-D-xylan xylohydrolase {ECO:0000250|UniProtKB:P48792};
DE     AltName: Full=Xylan 1,4-beta-xylosidase;
DE   Includes:
DE     RecName: Full=Alpha-L-arabinofuranosidase;
DE              Short=Arabinosidase {ECO:0000250|UniProtKB:P48792};
DE              EC=3.2.1.55;
DE   Flags: Precursor;
GN   Name=Xyl2 {ECO:0000312|EMBL:ABQ45228.1};
OS   Medicago sativa subsp. varia (Alfalfa) (Medicago varia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=36902;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABQ45228.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. A2 {ECO:0000269|PubMed:17615411};
RC   TISSUE=Root nodule {ECO:0000312|EMBL:ABQ45228.1};
RX   PubMed=17615411; DOI=10.1093/jxb/erm133;
RA   Xiong J.S., Balland-Vanney M., Xie Z.P., Schultze M., Kondorosi A.,
RA   Kondorosi E., Staehelin C.;
RT   "Molecular cloning of a bifunctional beta-xylosidase/alpha-L-arabinosidase
RT   from alfalfa roots: heterologous expression in Medicago truncatula and
RT   substrate specificity of the purified enzyme.";
RL   J. Exp. Bot. 58:2799-2810(2007).
CC   -!- FUNCTION: A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-
CC       enzyme that acts synergistically with endohydrolases. Releases xylose
CC       and arabinose from cell walls (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-
CC         xylose residues from the non-reducing termini.; EC=3.2.1.37;
CC         Evidence={ECO:0000250|UniProtKB:A5JTQ2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC         residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC         Evidence={ECO:0000250|UniProtKB:A5JTQ2};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q9FLG1}.
CC   -!- SIMILARITY: Belongs to the glycoside hydrolase 3 family. {ECO:0000255}.
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DR   EMBL; EF569969; ABQ45228.1; -; mRNA.
DR   AlphaFoldDB; A5JTQ3; -.
DR   SMR; A5JTQ3; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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; IPR001764; Glyco_hydro_3_N.
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; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52279; SSF52279; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Extracellular matrix; Glycoprotein; Glycosidase;
KW   Hydrolase; Multifunctional enzyme; Polysaccharide degradation; Secreted;
KW   Signal; Xylan degradation.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..774
FT                   /note="Beta-xylosidase/alpha-L-arabinofuranosidase 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000392641"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000250|UniProtKB:Q9FGY1"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   774 AA;  83383 MW;  A709EB1AA6B3EF42 CRC64;
     MASVENRTPN VSVFLCFFVL FATLLLSGGR VSSQTSAVFA CDVAKNPALA NYGFCNKKLS
     VDARVKDLVR RLTLQEKVGN LVNSAVDVSR LGIPKYEWWS EALHGVSNIG PGTHFSNVIP
     GATSFPMPIL IAASFNASLF QTIGKVVSTE ARAMHNVGLA GLTYWSPNIN IFRDPRWGRG
     QETPGEDPLL ASKYAAGYVK GLQQTDDGDS NKLKVAACCK HYTAYDVDDW KGVQRYTFNA
     VVTQQDLDDT YQPPFKSCVI DGNVASVMCS YNQVNGKPTC ADPDLLKGVI RGKWKLNGYI
     VSDCDSVDVL FKNQHYTKTP EEAAAKSILA GLDLNCGSFL GRYTEGAVKQ GLIGEASINN
     AVYNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTSANQEL AREAARQGIV LLKNCAGSLP
     LNAKAIKSLA VIGPNANATR AMIGNYEGIP CKYTSPLQGL TALVPTSFAA GCPDVQCTNA
     ALDDAKKIAA SADATVIVVG ANLAIEAESH DRINILLPGQ QQQLVTEVAN VAKGPVILAI
     MSGGGMDVSF AKTNKKITSI LWVGYPGEAG GAAIADVIFG YHNPSGRLPM TWYPQSYVDK
     VPMTNMNMRP DPATGYPGRT YRFYKGETVF SFGDGISYST FEHKLVKAPQ LVSVPLAEDH
     VCRSSKCKSL DVVGEHCQNL AFDIHLRIKN KGKMSSSQTV FLFSTPPAVH NAPQKHLLAF
     EKVLLTGKSE ALVSFKVDVC KDLGLVDELG NRKVALGKHM LHVGDLKHPL SVMI