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Q9LXD6 (BXL3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-D-xylosidase 3
Short name=AtBXL3
EC=3.2.1.-
Alternative name(s):
Alpha-L-arabinofuranosidase
EC=3.2.1.55
Gene names
Name:BXL3
Synonyms:XYL3
Ordered Locus Names:At5g09730
ORF Names:F17I14.80
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length773 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the hydrolysis of arabinan. Can hydrolyze (1,3)-alpha-, (1,2)-alpha-linked side group residues and non-reducing terminal L-arabinofuranose residues of debranched (1,5)-alpha-L-arabinan backbone. Acts also as a beta-D-xylosidase, releasing D-xylose from arabinoxylan and xylan. Ref.5

Catalytic activity

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Ref.5

Subcellular location

Secreted › extracellular space › extracellular matrix Potential.

Tissue specificity

Expressed in flowers and siliques, in the early stage of seed formation and not at seed maturation. Detected exclusively in the endosperm of very young seeds when the embryo is at the globular stage. Ref.5

Disruption phenotype

Reduced seeds size and delayed germination. Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.26 mM for p-nitrophenyl-beta-D-xylopyranoside (at 37 degrees Celsius) Ref.5

KM=3.52 mM for p-nitrophenyl-alpha-L-arabinofuranoside (at 37 degrees Celsius)

KM=5.5 mM for (1,5)-alpha-L-arabinobiose (at 37 degrees Celsius)

pH dependence:

Optimum pH is 4.7.

Temperature dependence:

Optimum temperature is 65 degrees Celsius.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarabinan catabolic process

Inferred from direct assay Ref.5. Source: TAIR

   Cellular_componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-N-arabinofuranosidase activity

Inferred from direct assay Ref.5. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.5
Chain24 – 773750Beta-D-xylosidase 3
PRO_0000384058

Sites

Active site2981 By similarity

Amino acid modifications

Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential
Glycosylation4321N-linked (GlcNAc...) Potential
Glycosylation7701N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict4881A → S in BAD94522. Ref.6
Sequence conflict5691A → P in BAD94522. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9LXD6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3C98ED6D3876621C

FASTA77383,222
        10         20         30         40         50         60 
MASRNRALFS VSTLFLCFIV CISEQSNNQS SPVFACDVTG NPSLAGLRFC NAGLSIKARV 

        70         80         90        100        110        120 
TDLVGRLTLE EKIGFLTSKA IGVSRLGIPS YKWWSEALHG VSNVGGGSRF TGQVPGATSF 

       130        140        150        160        170        180 
PQVILTAASF NVSLFQAIGK VVSTEARAMY NVGSAGLTFW SPNVNIFRDP RWGRGQETPG 

       190        200        210        220        230        240 
EDPTLSSKYA VAYVKGLQET DGGDPNRLKV AACCKHYTAY DIDNWRNVNR LTFNAVVNQQ 

       250        260        270        280        290        300 
DLADTFQPPF KSCVVDGHVA SVMCSYNQVN GKPTCADPDL LSGVIRGQWQ LNGYIVSDCD 

       310        320        330        340        350        360 
SVDVLFRKQH YAKTPEEAVA KSLLAGLDLN CDHFNGQHAM GAVKAGLVNE TAIDKAISNN 

       370        380        390        400        410        420 
FATLMRLGFF DGDPKKQLYG GLGPKDVCTA DNQELARDGA RQGIVLLKNS AGSLPLSPSA 

       430        440        450        460        470        480 
IKTLAVIGPN ANATETMIGN YHGVPCKYTT PLQGLAETVS STYQLGCNVA CVDADIGSAV 

       490        500        510        520        530        540 
DLAASADAVV LVVGADQSIE REGHDRVDLY LPGKQQELVT RVAMAARGPV VLVIMSGGGF 

       550        560        570        580        590        600 
DITFAKNDKK ITSIMWVGYP GEAGGLAIAD VIFGRHNPSG NLPMTWYPQS YVEKVPMSNM 

       610        620        630        640        650        660 
NMRPDKSKGY PGRSYRFYTG ETVYAFADAL TYTKFDHQLI KAPRLVSLSL DENHPCRSSE 

       670        680        690        700        710        720 
CQSLDAIGPH CENAVEGGSD FEVHLNVKNT GDRAGSHTVF LFTTSPQVHG SPIKQLLGFE 

       730        740        750        760        770 
KIRLGKSEEA VVRFNVNVCK DLSVVDETGK RKIALGHHLL HVGSLKHSLN ISV

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S.
DNA Res. 6:183-195(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Purification, functional characterization, cloning, and identification of mutants of a seed-specific arabinan hydrolase in Arabidopsis."
Minic Z., Do C.-T., Rihouey C., Morin H., Lerouge P., Jouanin L.
J. Exp. Bot. 57:2339-2351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-31, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[6]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 487-773.
Strain: cv. Columbia.
[7]"AtBXL1, a novel higher plant (Arabidopsis thaliana) putative beta-xylosidase gene, is involved in secondary cell wall metabolism and plant development."
Goujon T., Minic Z., El Amrani A., Lerouxel O., Aletti E., Lapierre C., Joseleau J.-P., Jouanin L.
Plant J. 33:677-690(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB020752 Genomic DNA. Translation: BAB09531.1.
AL353994 Genomic DNA. Translation: CAB89357.1.
CP002688 Genomic DNA. Translation: AED91439.1.
AY053409 mRNA. Translation: AAK96639.1.
AK221979 mRNA. Translation: BAD94522.1.
IPIIPI00530124.
PIRT49925.
RefSeqNP_196535.1. NM_121010.2.
UniGeneAt.47498.

3D structure databases

ProteinModelPortalQ9LXD6.
SMRQ9LXD6. Positions 439-764.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT5G09730.1-P.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Proteomic databases

PaxDbQ9LXD6.
PRIDEQ9LXD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G09730.1; AT5G09730.1; AT5G09730.
GeneID830833.
KEGGath:AT5G09730.

Organism-specific databases

TAIRAt5g09730.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000031216.
InParanoidQ9LXD6.
OMASHADDRE.
PhylomeDBQ9LXD6.
ProtClustDBCLSN2686278.

Gene expression databases

GenevestigatorQ9LXD6.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR30620. PTHR30620. 1 hit.
PfamPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
PRINTSPR00133. GLHYDRLASE3.
SUPFAMSSF52279. Glyco_hydro_3_C. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBXL3_ARATH
AccessionPrimary (citable) accession number: Q9LXD6
Secondary accession number(s): Q56WQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents