XYL1_MEDSV
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 25-MAY-2022, entry version 46.
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=1.20 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 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; 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 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
