A5JTQ2 (XYL1_MEDSV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-xylosidase/alpha-L-arabinofuranosidase 1

Alternative name(s):
Xylan 1,4-beta-xylosidase/Alpha-N-arabinofuranosidase 1
Short name=MsXyl1

Including the following 2 domains:

1. Beta-xylosidase
   EC=3.2.1.37
   Alternative name(s):
   1,4-beta-D-xylan xylohydrolase
   Xylan 1,4-beta-xylosidase
2. Alpha-N-arabinofuranosidase
   EC=3.2.1.55
   Alternative name(s):
   Alpha-L-arabinofuranosidase
   Short name=Arabinosidase

Gene names

Name:

Xyl1

Organism

Medicago sativa subsp. varia (Alfalfa) (Medicago varia)

Taxonomic identifier

36902 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago › Medicago sativa

Protein attributes

Sequence length	774 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls. Does not cleave xylan from oat spelts although xylan from oat spelts was degraded to xylose when this enzyme was used in combination with xylanase. Also releases xylose and arabinose from aryl glycosides, xylo-oligosaccharides, arabinan from sugar beet and arabino-oligosaccharides, arabinan from sugar beet and arabinoxylan from wheat. Ref.1
Catalytic activity	Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini. Ref.1 Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Ref.1
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity UniProtKB Q9FLG1.
Post-translational modification	Proteolytically cleaved in roots to form a 65 kDa protein. Ref.1
Sequence similarities	Belongs to the glycoside hydrolase 3 family.
Biophysicochemical properties	Kinetic parameters: KM=0.59 mM for pNP-beta-D-xlyoside (at 37 degrees Celsius) Ref.1 KM=0.94 mM for pNP-alpha-L-arabinofuranoside (at 37 degrees Celsius) Ref.1 KM=1.20 mM for pNP-alpha-L-arabinopyranoside (at 37 degrees Celsius)

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Extracellular matrix Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological_process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alpha-N-arabinofuranosidase activity Inferred from electronic annotation. Source: EC xylan 1,4-beta-xylosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	‹1 – 33	›33	Potential
	Chain	34 – 774	741	Beta-xylosidase/alpha-L-arabinofuranosidase 1		PRO_0000392640
Sites
	Active site	303	1	By similarity UniProtKB Q9FGY1
Amino acid modifications
	Glycosylation	48	1	N-linked (GlcNAc...) Potential
	Glycosylation	136	1	N-linked (GlcNAc...) Potential
	Glycosylation	437	1	N-linked (GlcNAc...) Potential
	Glycosylation	530	1	N-linked (GlcNAc...) Potential
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	A5JTQ2 [UniParc]. Last modified June 26, 2007. Version 1. Checksum: 6C45493BA13ABF5F	FASTA	774	83,727
	10 20 30 40 50 60 ANTKNREPKV SSVFLCFSIF YVTVLLNCNH VYGQTSTVFA CDVAKNTNVS SYGFCDNSLS 70 80 90 100 110 120 VEDRVSDLVK RLTLQEKIGN LGNSAVEVSR LGIPKYEWWS EALHGVSNIG PGTHFSSLVP 130 140 150 160 170 180 GATNFPMPIL TAASFNTSLF QAIGSVVSNE ARAMYNVGLA GLTYWSPNIN IFRDPRWGRG 190 200 210 220 230 240 QETPGEDPLL SSKYAAGYVK GLQQTDDGDS DKLKVAACCK HYTAYDVDNW KGVQRYTFDA 250 260 270 280 290 300 VVSQQDLDDT FQPPFKSCVI DGNVASVMCS YNKVNGKPTC ADPDLLKGVI RGKWKLNGYI 310 320 330 340 350 360 VSDCDSVEVL YKDQHYTKTP EEAAAKTILS GLDLDCGSYL GQYTGGAVKQ GLVDEASITN 370 380 390 400 410 420 AVSNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTPENQEL AREAARQGIV LLKNSPRSLP 430 440 450 460 470 480 LSSKAIKSLA VIGPNANATR VMIGNYEGIP CKYTSPLQGL TAFVPTSYAP GCPDVQCANA 490 500 510 520 530 540 QIDDAAKIAA SADATIIVVG ANLAIEAESL DRVNILLPGQ QQQLVNEVAN VSKGPVILVI 550 560 570 580 590 600 MSGGGMDVSF AKTNDKITSI LWVGYPGEAG GAAIADVIFG SYNPSGRLPM TWYPQSYVEK 610 620 630 640 650 660 VPMTNMNMRA DPATGYPGRT YRFYKGETVF SFGDGMSFGT VEHKIVKAPQ LVSVPLAEDH 670 680 690 700 710 720 ECRSLECKSL DVADKHCQNL AFDIHLSVKN MGKMSSSHSV LLFFTPPNVH NAPQKHLLGF 730 740 750 760 770 EKVQLAGKSE GMVRFKVDVC NDLSVVDELG NRKVPLGDHM LHVGNLKHSL SVRI

References

[1]

"Molecular cloning of a bifunctional beta-xylosidase/alpha-L-arabinosidase from alfalfa roots: heterologous expression in Medicago truncatula and substrate specificity of the purified enzyme." Xiong J.S., Balland-Vanney M., Xie Z.P., Schultze M., Kondorosi A., Kondorosi E., Staehelin C. J. Exp. Bot. 58:2799-2810(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEOLYTIC PROCESSING. Strain: cv. A2. Tissue: Root nodule.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EF569968 mRNA. Translation: ABQ45227.1.
3D structure databases
ProteinModelPortal	A5JTQ2.
ModBase	Search...
Protein family/group databases
CAZy	GH3. Glycoside Hydrolase Family 3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.20.20.300. 1 hit. 3.40.50.1700. 1 hit.
InterPro	IPR026891. Fn3-like. IPR026892. Glyco_hydro_3. IPR002772. Glyco_hydro_3_C. IPR001764. Glyco_hydro_3_N. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR30620. PTHR30620. 1 hit.
Pfam	PF14310. Fn3-like. 1 hit. PF00933. Glyco_hydro_3. 1 hit. PF01915. Glyco_hydro_3_C. 1 hit. [Graphical view]
PRINTS	PR00133. GLHYDRLASE3.
SUPFAM	SSF52279. Glyco_hydro_3_C. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00775. GLYCOSYL_HYDROL_F3. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYL1_MEDSV

Accession

Primary (citable) accession number: A5JTQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 23, 2010
Last sequence update:	June 26, 2007
Last modified:	March 6, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program