A5JTQ3 (XYL2_MEDSV) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-xylosidase/alpha-L-arabinofuranosidase 2

Alternative name(s):
Xylan 1,4-beta-xylosidase/Alpha-N-arabinofuranosidase 2
Short name=MsXyl2

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:

Xyl2

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	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity. UniProtKB A5JTQ2
Catalytic activity	Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini. UniProtKB A5JTQ2 Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. UniProtKB A5JTQ2
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity UniProtKB Q9FLG1.
Sequence similarities	Belongs to the glycoside hydrolase 3 family.

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 2		PRO_0000392641
Sites
	Active site	303	1	By similarity UniProtKB Q9FGY1
Amino acid modifications
	Glycosylation	136	1	N-linked (GlcNAc...) Potential
	Glycosylation	437	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	A5JTQ3 [UniParc]. Last modified June 26, 2007. Version 1. Checksum: A709EB1AA6B3EF42	FASTA	774	83,383
	10 20 30 40 50 60 MASVENRTPN VSVFLCFFVL FATLLLSGGR VSSQTSAVFA CDVAKNPALA NYGFCNKKLS 70 80 90 100 110 120 VDARVKDLVR RLTLQEKVGN LVNSAVDVSR LGIPKYEWWS EALHGVSNIG PGTHFSNVIP 130 140 150 160 170 180 GATSFPMPIL IAASFNASLF QTIGKVVSTE ARAMHNVGLA GLTYWSPNIN IFRDPRWGRG 190 200 210 220 230 240 QETPGEDPLL ASKYAAGYVK GLQQTDDGDS NKLKVAACCK HYTAYDVDDW KGVQRYTFNA 250 260 270 280 290 300 VVTQQDLDDT YQPPFKSCVI DGNVASVMCS YNQVNGKPTC ADPDLLKGVI RGKWKLNGYI 310 320 330 340 350 360 VSDCDSVDVL FKNQHYTKTP EEAAAKSILA GLDLNCGSFL GRYTEGAVKQ GLIGEASINN 370 380 390 400 410 420 AVYNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTSANQEL AREAARQGIV LLKNCAGSLP 430 440 450 460 470 480 LNAKAIKSLA VIGPNANATR AMIGNYEGIP CKYTSPLQGL TALVPTSFAA GCPDVQCTNA 490 500 510 520 530 540 ALDDAKKIAA SADATVIVVG ANLAIEAESH DRINILLPGQ QQQLVTEVAN VAKGPVILAI 550 560 570 580 590 600 MSGGGMDVSF AKTNKKITSI LWVGYPGEAG GAAIADVIFG YHNPSGRLPM TWYPQSYVDK 610 620 630 640 650 660 VPMTNMNMRP DPATGYPGRT YRFYKGETVF SFGDGISYST FEHKLVKAPQ LVSVPLAEDH 670 680 690 700 710 720 VCRSSKCKSL DVVGEHCQNL AFDIHLRIKN KGKMSSSQTV FLFSTPPAVH NAPQKHLLAF 730 740 750 760 770 EKVLLTGKSE ALVSFKVDVC KDLGLVDELG NRKVALGKHM LHVGDLKHPL SVMI

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]. Strain: cv. A2. Tissue: Root nodule.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EF569969 mRNA. Translation: ABQ45228.1.
3D structure databases
ProteinModelPortal	A5JTQ3.
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

XYL2_MEDSV

Accession

Primary (citable) accession number: A5JTQ3

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