ID   XYL1_MEDSV              Reviewed;         774 AA.
AC   A5JTQ2;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   22-FEB-2023, entry version 48.
DE   RecName: Full=Beta-xylosidase/alpha-L-arabinofuranosidase 1 {ECO:0000303|PubMed:17615411, ECO:0000312|EMBL:ABQ45227.1};
DE   AltName: Full=Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 1;
DE            Short=MsXyl1 {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; Fragment;
GN   Name=Xyl1 {ECO:0000312|EMBL:ABQ45227.1};
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:ABQ45227.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND PROTEOLYTIC PROCESSING.
RC   STRAIN=cv. A2 {ECO:0000269|PubMed:17615411};
RC   TISSUE=Root nodule {ECO:0000312|EMBL:ABQ45227.1};
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. Does not cleave xylan from oat spelts
CC       although xylan from oat spelts was degraded to xylose when this enzyme
CC       was used in combination with xylanase. Also releases xylose and
CC       arabinose from aryl glycosides, xylo-oligosaccharides, arabinan from
CC       sugar beet and arabino-oligosaccharides, arabinan from sugar beet and
CC       arabinoxylan from wheat. {ECO:0000269|PubMed:17615411}.
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:0000269|PubMed:17615411};
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:0000269|PubMed:17615411};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.59 mM for pNP-beta-D-xlyoside (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:17615411};
CC         KM=0.94 mM for pNP-alpha-L-arabinofuranoside (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:17615411};
CC         KM=1.2 mM for pNP-alpha-L-arabinopyranoside (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:17615411};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250|UniProtKB:Q9FLG1}.
CC   -!- PTM: Proteolytically cleaved in roots to form a 65 kDa protein.
CC       {ECO:0000269|PubMed:17615411}.
CC   -!- SIMILARITY: Belongs to the glycoside hydrolase 3 family. {ECO:0000255}.
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DR   EMBL; EF569968; ABQ45227.1; -; mRNA.
DR   AlphaFoldDB; A5JTQ2; -.
DR   SMR; A5JTQ2; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   GlyCosmos; A5JTQ2; 4 sites, No reported glycans.
DR   SABIO-RK; A5JTQ2; -.
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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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:SF14; BETA-D-XYLOSIDASE 4-RELATED; 1.
DR   PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 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; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE   1: Evidence at protein 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 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000392640"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000250|UniProtKB:Q9FGY1"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ABQ45227.1"
SQ   SEQUENCE   774 AA;  83727 MW;  6C45493BA13ABF5F CRC64;
     ANTKNREPKV SSVFLCFSIF YVTVLLNCNH VYGQTSTVFA CDVAKNTNVS SYGFCDNSLS
     VEDRVSDLVK RLTLQEKIGN LGNSAVEVSR LGIPKYEWWS EALHGVSNIG PGTHFSSLVP
     GATNFPMPIL TAASFNTSLF QAIGSVVSNE ARAMYNVGLA GLTYWSPNIN IFRDPRWGRG
     QETPGEDPLL SSKYAAGYVK GLQQTDDGDS DKLKVAACCK HYTAYDVDNW KGVQRYTFDA
     VVSQQDLDDT FQPPFKSCVI DGNVASVMCS YNKVNGKPTC ADPDLLKGVI RGKWKLNGYI
     VSDCDSVEVL YKDQHYTKTP EEAAAKTILS GLDLDCGSYL GQYTGGAVKQ GLVDEASITN
     AVSNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTPENQEL AREAARQGIV LLKNSPRSLP
     LSSKAIKSLA VIGPNANATR VMIGNYEGIP CKYTSPLQGL TAFVPTSYAP GCPDVQCANA
     QIDDAAKIAA SADATIIVVG ANLAIEAESL DRVNILLPGQ QQQLVNEVAN VSKGPVILVI
     MSGGGMDVSF AKTNDKITSI LWVGYPGEAG GAAIADVIFG SYNPSGRLPM TWYPQSYVEK
     VPMTNMNMRA DPATGYPGRT YRFYKGETVF SFGDGMSFGT VEHKIVKAPQ LVSVPLAEDH
     ECRSLECKSL DVADKHCQNL AFDIHLSVKN MGKMSSSHSV LLFFTPPNVH NAPQKHLLGF
     EKVQLAGKSE GMVRFKVDVC NDLSVVDELG NRKVPLGDHM LHVGNLKHSL SVRI
//