Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Beta-xylosidase/alpha-L-arabinofuranosidase 2

Gene

Xyl2

Organism
Medicago sativa subsp. varia (Alfalfa) (Medicago varia)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo-enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls (By similarity).By similarity

Catalytic activityi

Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.By similarity
Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei303 – 3031By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-xylosidase/alpha-L-arabinofuranosidase 21 PublicationImported
Alternative name(s):
Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 2
Short name:
MsXyl21 Publication
Including the following 2 domains:
Alternative name(s):
1,4-beta-D-xylan xylohydrolaseBy similarity
Xylan 1,4-beta-xylosidase
Alpha-L-arabinofuranosidase (EC:3.2.1.55)
Short name:
ArabinosidaseBy similarity
Gene namesi
Name:Xyl2Imported
OrganismiMedicago sativa subsp. varia (Alfalfa) (Medicago varia)
Taxonomic identifieri36902 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 774741Beta-xylosidase/alpha-L-arabinofuranosidase 2Sequence AnalysisPRO_0000392641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA5JTQ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycoside hydrolase 3 family.Sequence Analysis

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A5JTQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVENRTPN VSVFLCFFVL FATLLLSGGR VSSQTSAVFA CDVAKNPALA
60 70 80 90 100
NYGFCNKKLS VDARVKDLVR RLTLQEKVGN LVNSAVDVSR LGIPKYEWWS
110 120 130 140 150
EALHGVSNIG PGTHFSNVIP GATSFPMPIL IAASFNASLF QTIGKVVSTE
160 170 180 190 200
ARAMHNVGLA GLTYWSPNIN IFRDPRWGRG QETPGEDPLL ASKYAAGYVK
210 220 230 240 250
GLQQTDDGDS NKLKVAACCK HYTAYDVDDW KGVQRYTFNA VVTQQDLDDT
260 270 280 290 300
YQPPFKSCVI DGNVASVMCS YNQVNGKPTC ADPDLLKGVI RGKWKLNGYI
310 320 330 340 350
VSDCDSVDVL FKNQHYTKTP EEAAAKSILA GLDLNCGSFL GRYTEGAVKQ
360 370 380 390 400
GLIGEASINN AVYNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTSANQEL
410 420 430 440 450
AREAARQGIV LLKNCAGSLP LNAKAIKSLA VIGPNANATR AMIGNYEGIP
460 470 480 490 500
CKYTSPLQGL TALVPTSFAA GCPDVQCTNA ALDDAKKIAA SADATVIVVG
510 520 530 540 550
ANLAIEAESH DRINILLPGQ QQQLVTEVAN VAKGPVILAI MSGGGMDVSF
560 570 580 590 600
AKTNKKITSI LWVGYPGEAG GAAIADVIFG YHNPSGRLPM TWYPQSYVDK
610 620 630 640 650
VPMTNMNMRP DPATGYPGRT YRFYKGETVF SFGDGISYST FEHKLVKAPQ
660 670 680 690 700
LVSVPLAEDH VCRSSKCKSL DVVGEHCQNL AFDIHLRIKN KGKMSSSQTV
710 720 730 740 750
FLFSTPPAVH NAPQKHLLAF EKVLLTGKSE ALVSFKVDVC KDLGLVDELG
760 770
NRKVALGKHM LHVGDLKHPL SVMI
Length:774
Mass (Da):83,383
Last modified:June 26, 2007 - v1
Checksum:iA709EB1AA6B3EF42
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF569969 mRNA. Translation: ABQ45228.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF569969 mRNA. Translation: ABQ45228.1.

3D structure databases

ProteinModelPortaliA5JTQ3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSiPR00133. GLHYDRLASE3.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNetiSearch...

Publicationsi

  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. A21 Publication.
    Tissue: Root noduleImported.

Entry informationi

Entry nameiXYL2_MEDSV
AccessioniPrimary (citable) accession number: A5JTQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: June 26, 2007
Last modified: January 7, 2015
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.