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Q43866 (INV1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-fructofuranosidase, insoluble isoenzyme CWINV1

EC=3.2.1.26
Alternative name(s):
Cell wall beta-fructosidase 1
Short name=AtbetaFRUCT1
Cell wall invertase 1
Short name=AtcwINV1
Sucrose hydrolase 1
Gene names
Name:CWINV1
Synonyms:BFRUCT1
Ordered Locus Names:At3g13790
ORF Names:MMM17.26
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length584 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Beta-fructofuranosidase that can use sucrose and 1-kestose, and, to a lower extent, neokestose and levan, as substrates, but not inuline. Ref.7 Ref.9

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.

Subcellular location

Secretedextracellular spaceapoplast Probable. Secretedcell wall Probable. Note: Associated to the cell wall Probable.

Tissue specificity

Expressed in seedlings, leaves, flowers, and seeds. Ref.5 Ref.6 Ref.8

Induction

By wounding, aeroponic growth condition, darkness, sucrose, glucose and mannitol. Ref.5 Ref.8

Sequence similarities

Belongs to the glycosyl hydrolase 32 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.35 mM for sucrose (at pH 5 and 30 degrees Celsius) Ref.9

KM=1 mM for 1-kestose (at pH 5 and 30 degrees Celsius)

Sequence caution

The sequence BAB01930.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentApoplast
Cell wall
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processresponse to karrikin

Inferred from expression pattern. Source: TAIR

response to wounding

Inferred from mutant phenotype Ref.8. Source: TAIR

   Cellular componentapoplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell wall

Inferred from direct assay. Source: TAIR

   Molecular functionsucrose alpha-glucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q43866-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 584556Beta-fructofuranosidase, insoluble isoenzyme CWINV1
PRO_0000348347

Regions

Region63 – 664Substrate binding
Region125 – 1262Substrate binding
Region191 – 1922Substrate binding

Sites

Active site661
Binding site821Substrate
Binding site901Substrate
Binding site2461Substrate
Binding site2821Substrate

Amino acid modifications

Glycosylation1591N-linked (GlcNAc...)
Glycosylation1861N-linked (GlcNAc...)
Glycosylation3421N-linked (GlcNAc...)
Glycosylation4461N-linked (GlcNAc...) Potential
Disulfide bond442 ↔ 491

Experimental info

Mutagenesis631W → L: Loss of activity. Ref.9
Mutagenesis661D → A: Loss of activity. Ref.9 Ref.12
Mutagenesis901W → L: Loss of activity. Ref.9
Mutagenesis1251W → L: Loss of activity. Ref.9
Mutagenesis2461E → A or Q: Loss of activity. Ref.9 Ref.12 Ref.13
Mutagenesis2821D → A: Impaired beta-fructofuranosidase activity but enhanced 1-fructan exohydrolase activity. Ref.9 Ref.12
Mutagenesis2821D → F: Loss of activity. Ref.9 Ref.12
Mutagenesis2821D → N: Normal activity. Ref.9 Ref.12
Mutagenesis2851K → L: Slightly reduced activity. Ref.9
Mutagenesis3421N → D: Reduced activity and glycosylation. Ref.10 Ref.11

Secondary structure

........................................................................................... 584
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C571359FB1825E36

FASTA58466,280
        10         20         30         40         50         60 
MTKEVCSNIG LWLLLTLLIG NYVVNLEASH HVYKRLTQST NTKSPSVNQP YRTGFHFQPP 

        70         80         90        100        110        120 
KNWMNDPNGP MIYKGIYHLF YQWNPKGAVW GNIVWAHSTS TDLINWDPHP PAIFPSAPFD 

       130        140        150        160        170        180 
INGCWSGSAT ILPNGKPVIL YTGIDPKNQQ VQNIAEPKNL SDPYLREWKK SPLNPLMAPD 

       190        200        210        220        230        240 
AVNGINASSF RDPTTAWLGQ DKKWRVIIGS KIHRRGLAIT YTSKDFLKWE KSPEPLHYDD 

       250        260        270        280        290        300 
GSGMWECPDF FPVTRFGSNG VETSSFGEPN EILKHVLKIS LDDTKHDYYT IGTYDRVKDK 

       310        320        330        340        350        360 
FVPDNGFKMD GTAPRYDYGK YYASKTFFDS AKNRRILWGW TNESSSVEDD VEKGWSGIQT 

       370        380        390        400        410        420 
IPRKIWLDRS GKQLIQWPVR EVERLRTKQV KNLRNKVLKS GSRLEVYGVT AAQADVEVLF 

       430        440        450        460        470        480 
KVRDLEKADV IEPSWTDPQL ICSKMNVSVK SGLGPFGLMV LASKNLEEYT SVYFRIFKAR 

       490        500        510        520        530        540 
QNSNKYVVLM CSDQSRSSLK EDNDKTTYGA FVDINPHQPL SLRALIDHSV VESFGGKGRA 

       550        560        570        580 
CITSRVYPKL AIGKSSHLFA FNYGYQSVDV LNLNAWSMNS AQIS 

« Hide

References

« Hide 'large scale' references
[1]"Arabidopsis gene and cDNA encoding cell-wall invertase."
Schwebel-Dugue N., el Mtili N., Krivitzky M., Jean-Jacques I., Williams J.H., Thomas M., Kreis M., Lecharny A.
Plant Physiol. 104:809-810(1994) [PubMed: 8159800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
Tissue: Leaf.
[2]"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
DNA Res. 7:217-221(2000) [PubMed: 10907853] [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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Expression of the Arabidopsis thaliana invertase gene family."
Tymowska-Lalanne Z., Kreis M.
Planta 207:259-265(1998) [PubMed: 9951726] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[6]"Roles of cell-wall invertases and monosaccharide transporters in the growth and development of Arabidopsis."
Sherson S.M., Alford H.L., Forbes S.M., Wallace G., Smith S.M.
J. Exp. Bot. 54:525-531(2003) [PubMed: 12508063] [Abstract]
Cited for: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[7]"Arabidopsis AtcwINV3 and 6 are not invertases but are fructan exohydrolases (FEHs) with different substrate specificities."
de Coninck B., Le Roy K., Francis I., Clerens S., Vergauwen R., Halliday A.M., Smith S.M., Van Laere A., Van Den Ende W.
Plant Cell Environ. 28:432-443(2005)
Cited for: FUNCTION.
[8]"Imaging photosynthesis in wounded leaves of Arabidopsis thaliana."
Quilliam R.S., Swarbrick P.J., Scholes J.D., Rolfe S.A.
J. Exp. Bot. 57:55-69(2006) [PubMed: 16339783] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION BY WOUNDING.
[9]"Unraveling the difference between invertases and fructan exohydrolases: a single amino acid (Asp-239) substitution transforms Arabidopsis cell wall invertase1 into a fructan 1-exohydrolase."
Le Roy K., Lammens W., Verhaest M., De Coninck B., Rabijns A., Van Laere A., Van den Ende W.
Plant Physiol. 145:616-625(2007) [PubMed: 17873089] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TRP-63; ASP-66; TRP-90; TRP-125; GLU-246; ASP-282 AND LYS-285, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE BINDING.
[10]"N-glycosylation affects substrate specificity of chicory fructan 1-exohydrolase: evidence for the presence of an inulin binding cleft."
Le Roy K., Verhaest M., Rabijns A., Clerens S., Van Laere A., Van den Ende W.
New Phytol. 176:317-324(2007) [PubMed: 17888113] [Abstract]
Cited for: MUTAGENESIS OF ASN-342.
[11]"X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana."
Verhaest M., Lammens W., Le Roy K., De Coninck B., De Ranter C.J., Van Laere A., Van den Ende W., Rabijns A.
Acta Crystallogr. D 62:1555-1563(2006) [PubMed: 17139091] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 44-584 IN COMPLEX WITH SUBSTRATES, MUTAGENESIS OF ASN-342, GLYCOSYLATION.
[12]"Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose."
Lammens W., Le Roy K., Van Laere A., Rabijns A., Van den Ende W.
J. Mol. Biol. 377:378-385(2008) [PubMed: 18258263] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 48-584 IN COMPLEX WITH SUBSTRATES, MUTAGENESIS OF ASP-66; GLU-246 AND ASP-282, GLYCOSYLATION.
[13]"An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: an X-ray crystallography and docking study."
Matrai J., Lammens W., Jonckheer A., Le Roy K., Rabijns A., Van den Ende W., De Maeyer M.
Proteins 71:552-564(2008) [PubMed: 17963237] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 48-584 IN COMPLEX WITH SUBSTRATES, MUTAGENESIS OF GLU-246, GLYCOSYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74514 mRNA. Translation: CAA52619.1.
X74515 mRNA. Translation: CAA52620.1.
AP001307 Genomic DNA. Translation: BAB01930.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE75414.1.
AY045776 mRNA. Translation: AAK76450.1.
AY079422 mRNA. Translation: AAL85153.1.
IPIIPI00518427.
PIRS37212.
RefSeqNP_001189881.1. NM_001202952.1.
NP_566464.1. NM_112232.3.
UniGeneAt.24308.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AC1X-ray2.15A44-584[»]
2OXBX-ray2.60A48-584[»]
2QQUX-ray2.84A48-582[»]
2QQVX-ray3.01A48-584[»]
2QQWX-ray2.80A48-584[»]
2XQRX-ray2.58A/C/E/G/I/K48-584[»]
ProteinModelPortalQ43866.
SMRQ43866. Positions 48-584.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ43866.

Protein family/group databases

CAZyGH32. Glycoside Hydrolase Family 32.

Proteomic databases

PRIDEQ43866.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G13790.1; AT3G13790.1; AT3G13790.
GeneID820591.
GenomeReviewsGene locus AT3G13790 in contig BA000014_GR.
KEGGath:AT3G13790.
NMPDRfig|3702.1.peg.13499.

Organism-specific databases

TAIRAt3g13790.

Phylogenomic databases

eggNOGKOG0228.
GeneTreeEPGT00050000007871.
HOGENOMHBG317462.
InParanoidQ43866.
OMACIANPPK.
PhylomeDBQ43866.
ProtClustDBCLSN2914992.

Gene expression databases

ArrayExpressQ43866.
GenevestigatorQ43866.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_43_beta-prop.
[Graphical view]
Gene3DG3DSA:2.115.10.20. Glyco_hydro_43_beta-prop. 1 hit.
KOK01193.
PfamPF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
SSF75005. Glyco_hydro_43_beta-prop. 1 hit.
PROSITEPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameINV1_ARATH
AccessionPrimary (citable) accession number: Q43866
Secondary accession number(s): Q9LIB8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 79 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families