XYL1_MEDSA
ID XYL1_MEDSA Reviewed; 45 AA.
AC P86450;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Beta-xylosidase/alpha-L-arabinofuranosidase 1 {ECO:0000303|PubMed:17615411};
DE AltName: Full=Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 1;
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: Fragments;
GN Name=Xyl1 {ECO:0000303|PubMed:17615411};
OS Medicago sativa (Alfalfa).
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=3879;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Sitel {ECO:0000269|PubMed:17615411};
RC TISSUE=Root nodule {ECO:0000269|PubMed:17615411};
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 -!- TISSUE SPECIFICITY: Strongly expressed in young roots, significantly
CC reduced expression in older roots. Highest expression levels seen in
CC root tips, some expression seen in root nodules and in the flowers, but
CC not seen in other aerial parts of the plant such as in the stems,
CC hypocotyls or leaves. {ECO:0000269|PubMed:17615411}.
CC -!- SIMILARITY: Belongs to the glycoside hydrolase 3 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P86450; -.
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.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Extracellular matrix;
KW Glycosidase; Hydrolase; Multifunctional enzyme; Polysaccharide degradation;
KW Secreted; Xylan degradation.
FT CHAIN <1..>45
FT /note="Beta-xylosidase/alpha-L-arabinofuranosidase 1"
FT /id="PRO_0000392639"
FT NON_CONS 15..16
FT /evidence="ECO:0000303|PubMed:17615411"
FT NON_CONS 30..31
FT /evidence="ECO:0000303|PubMed:17615411"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:17615411"
FT NON_TER 45
FT /evidence="ECO:0000303|PubMed:17615411"
SQ SEQUENCE 45 AA; 4785 MW; 83339885B81AEA45 CRC64;
GVQRYTFDAV VSQQDTILSG LDLDCGSYLG YTSPLQGLTA FVPTS
