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A5JTQ2

- XYL1_MEDSV

UniProt

A5JTQ2 - XYL1_MEDSV

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Protein
Beta-xylosidase/alpha-L-arabinofuranosidase 1
Gene
Xyl1
Organism
Medicago sativa subsp. varia (Alfalfa) (Medicago varia)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.59 mM for pNP-beta-D-xlyoside (at 37 degrees Celsius)1 Publication
  2. KM=0.94 mM for pNP-alpha-L-arabinofuranoside (at 37 degrees Celsius)1 Publication
  3. KM=1.20 mM for pNP-alpha-L-arabinopyranoside (at 37 degrees Celsius)

Sites

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

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC
  2. xylan 1,4-beta-xylosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-KW
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 1
Alternative name(s):
Xylan 1,4-beta-xylosidase/Alpha-L-arabinofuranosidase 1
Short name:
MsXyl1
Including the following 2 domains:
Alternative name(s):
1,4-beta-D-xylan xylohydrolase
Xylan 1,4-beta-xylosidase
Alpha-L-arabinofuranosidase (EC:3.2.1.55)
Short name:
Arabinosidase
Gene namesi
Name:Xyl1
OrganismiMedicago sativa subsp. varia (Alfalfa) (Medicago varia)
Taxonomic identifieri36902 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Subcellular locationi

Secretedextracellular spaceextracellular matrix By similarity By similarity

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 33›33 Reviewed prediction
Add
BLAST
Chaini34 – 774741Beta-xylosidase/alpha-L-arabinofuranosidase 1
PRO_0000392640Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi48 – 481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi136 – 1361N-linked (GlcNAc...) Reviewed prediction
Glycosylationi437 – 4371N-linked (GlcNAc...) Reviewed prediction
Glycosylationi530 – 5301N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Proteolytically cleaved in roots to form a 65 kDa protein.1 Publication

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA5JTQ2.

Family & Domainsi

Sequence similaritiesi

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: Fragment.

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

A5JTQ2-1 [UniParc]FASTAAdd to Basket

« Hide

ANTKNREPKV SSVFLCFSIF YVTVLLNCNH VYGQTSTVFA CDVAKNTNVS    50
SYGFCDNSLS VEDRVSDLVK RLTLQEKIGN LGNSAVEVSR LGIPKYEWWS 100
EALHGVSNIG PGTHFSSLVP GATNFPMPIL TAASFNTSLF QAIGSVVSNE 150
ARAMYNVGLA GLTYWSPNIN IFRDPRWGRG QETPGEDPLL SSKYAAGYVK 200
GLQQTDDGDS DKLKVAACCK HYTAYDVDNW KGVQRYTFDA VVSQQDLDDT 250
FQPPFKSCVI DGNVASVMCS YNKVNGKPTC ADPDLLKGVI RGKWKLNGYI 300
VSDCDSVEVL YKDQHYTKTP EEAAAKTILS GLDLDCGSYL GQYTGGAVKQ 350
GLVDEASITN AVSNNFATLM RLGFFDGDPS KQPYGNLGPK DVCTPENQEL 400
AREAARQGIV LLKNSPRSLP LSSKAIKSLA VIGPNANATR VMIGNYEGIP 450
CKYTSPLQGL TAFVPTSYAP GCPDVQCANA QIDDAAKIAA SADATIIVVG 500
ANLAIEAESL DRVNILLPGQ QQQLVNEVAN VSKGPVILVI MSGGGMDVSF 550
AKTNDKITSI LWVGYPGEAG GAAIADVIFG SYNPSGRLPM TWYPQSYVEK 600
VPMTNMNMRA DPATGYPGRT YRFYKGETVF SFGDGMSFGT VEHKIVKAPQ 650
LVSVPLAEDH ECRSLECKSL DVADKHCQNL AFDIHLSVKN MGKMSSSHSV 700
LLFFTPPNVH NAPQKHLLGF EKVQLAGKSE GMVRFKVDVC NDLSVVDELG 750
NRKVPLGDHM LHVGNLKHSL SVRI 774
Length:774
Mass (Da):83,727
Last modified:June 26, 2007 - v1
Checksum:i6C45493BA13ABF5F
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF569968 mRNA. Translation: ABQ45227.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF569968 mRNA. Translation: ABQ45227.1 .

3D structure databases

ProteinModelPortali A5JTQ2.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProi IPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR30620. PTHR30620. 1 hit.
Pfami PF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view ]
PRINTSi PR00133. GLHYDRLASE3.
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNeti Search...

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], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEOLYTIC PROCESSING.
    Strain: cv. A2.
    Tissue: Root nodule.

Entry informationi

Entry nameiXYL1_MEDSV
AccessioniPrimary (citable) accession number: A5JTQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: June 26, 2007
Last modified: May 14, 2014
This is version 26 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

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