Reviewed, UniProtKB/Swiss-Prot Q43866 (INV1_ARATH)

Names and origin

Protein names

Recommended name:
    Beta-fructofuranosidase, insoluble isoenzyme CWINV1
    EC=3.2.1.26
Alternative name(s):
    Cell wall invertase 1
      Short name=AtcwINV1
    Sucrose hydrolase 1
    Cell wall beta-fructosidase 1
      Short name=AtbetaFRUCT1

Gene names

Name:	CWINV1
Synonyms:	BFRUCT1
Ordered Locus Names:	At3g13790
ORF Names:	MMM17.26

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	584 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.6 Ref.8
Catalytic activity	Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
Subcellular location	Secreted › extracellular space › apoplast Probable. Secreted › cell wall Probable. Note: Associated to the cell wall Probable.
Tissue specificity	Expressed in seedlings, leaves, flowers, and seeds. Ref.4 Ref.5 Ref.7
Induction	By wounding, aeroponic growth condition, darkness, sucrose, glucose and mannitol. Ref.4 Ref.7
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) 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 component	Apoplast Cell wall Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro response to wounding Ref.7 Inferred from mutant phenotype. Source: TAIR
Cellular component	apoplast Inferred from electronic annotation. Source: UniProtKB-SubCell cell wall Inferred from direct assay. Source: TAIR
Molecular function	beta-fructofuranosidase activity Ref.7 Inferred from mutant phenotype. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Chain

29 – 584

556

Beta-fructofuranosidase, insoluble isoenzyme CWINV1

PRO_0000348347

Regions

Region

63 – 66

4

Substrate binding

Region

125 – 126

2

Substrate binding

Region

191 – 192

2

Substrate binding

Sites

Active site

66

1

Binding site

82

1

Substrate

Binding site

90

1

Substrate

Binding site

246

1

Substrate

Binding site

282

1

Substrate

Amino acid modifications

Glycosylation

159

1

N-linked (GlcNAc...)

Glycosylation

186

1

N-linked (GlcNAc...)

Glycosylation

342

1

N-linked (GlcNAc...)

Glycosylation

446

1

N-linked (GlcNAc...) Potential

Disulfide bond

442 ↔ 491

Experimental info

Mutagenesis

63

1

W → L: Loss of activity. Ref.8

Mutagenesis

66

1

D → A: Loss of activity. Ref.8 Ref.11

Mutagenesis

90

1

W → L: Loss of activity. Ref.8

Mutagenesis

125

1

W → L: Loss of activity. Ref.8

Mutagenesis

246

1

E → A or Q: Loss of activity. Ref.8 Ref.11 Ref.12

Mutagenesis

282

1

D → A: Impaired beta-fructofuranosidase activity but enhanced 1-fructan exohydrolase activity. Ref.8 Ref.11

Mutagenesis

282

1

D → F: Loss of activity. Ref.8 Ref.11

Mutagenesis

282

1

D → N: Normal activity. Ref.8 Ref.11

Mutagenesis

285

1

K → L: Slightly reduced activity. Ref.8

Mutagenesis

342

1

N → D: Reduced activity and glycosylation. Ref.9 Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

584

Helix Strand Turn

Details...

Beta strand

54 – 56

3

Beta strand

60 – 73

14

Beta strand

76 – 83

8

Beta strand

88 – 90

3

Beta strand

94 – 113

20

Helix

118 – 120

3

Beta strand

124 – 131

8

Beta strand

137 – 144

8

Beta strand

150 – 158

9

Beta strand

168 – 170

3

Turn

181 – 183

3

Beta strand

189 – 191

3

Beta strand

204 – 212

9

Beta strand

215 – 228

14

Beta strand

236 – 240

5

Beta strand

245 – 256

12

Beta strand

273 – 281

9

Turn

282 – 284

3

Beta strand

287 – 295

9

Turn

296 – 299

4

Beta strand

300 – 303

4

Beta strand

318 – 320

3

Beta strand

322 – 329

8

Turn

330 – 333

4

Beta strand

334 – 341

8

Helix

347 – 353

7

Beta strand

363 – 367

5

Beta strand

371 – 378

8

Helix

380 – 385

6

Beta strand

391 – 398

8

Beta strand

402 – 405

4

Beta strand

413 – 421

9

Helix

425 – 427

3

Beta strand

428 – 430

3

Helix

438 – 444

7

Beta strand

452 – 462

11

Beta strand

466 – 468

3

Beta strand

470 – 480

11

Beta strand

486 – 493

8

Beta strand

508 – 512

5

Beta strand

520 – 527

8

Beta strand

530 – 535

6

Turn

536 – 539

4

Beta strand

540 – 545

6

Beta strand

549 – 551

3

Helix

553 – 555

3

Beta strand

557 – 562

6

Beta strand

564 – 566

3

Beta strand

568 – 578

11

Sequences

	Sequence		Length	Mass (Da)
	Q43866-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C571359FB1825E36	FASTA	584	66,280
	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

References

	« Hide 'large scale' referencesShow '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]	"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. , 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.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
AY045776 mRNA. Translation: AAK76450.1.
AY079422 mRNA. Translation: AAL85153.1.

IPI

IPI00518427.

PIR

S37212.

RefSeq

NP_566464.1.

UniGene

At.24308

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AC1	X-ray	2.15	A	44-584	[»]
2OXB	X-ray	2.60	A	48-584	[»]
2QQU	X-ray	2.84	A	48-582	[»]
2QQV	X-ray	3.01	A	48-584	[»]
2QQW	X-ray	2.80	A	48-584	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q43866.

Protein family/group databases

CAZy

GH32. Glycoside Hydrolase Family 32.

Proteomic databases

PRIDE

Q43866.

Genome annotation databases

GeneID

820591.

GenomeReviews

Gene locus AT3G13790 in contig BA000014_GR.

KEGG

ath:AT3G13790.

NMPDR

fig|3702.1.peg.13499.

Organism-specific databases

TAIR

At3g13790.

Phylogenomic databases

eggNOG

KOG0228.

HOGENOM

HBG317462.

InParanoid

Q43866.

OMA

INASSFR.

PhylomeDB

Q43866.

Gene expression databases

ArrayExpress

Q43866.

Genevestigator

Q43866.

Family and domain databases

InterPro

IPR008985. ConA-like_lec_gl.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013189. Glyco_hydro_32_C.
IPR013148. Glyco_hydro_32_N.
[Graphical view]

Pfam

PF08244. Glyco_hydro_32C. 1 hit.
PF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]

SMART

SM00640. Glyco_32. 1 hit.
[Graphical view]

PROSITE

PS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

INV1_ARATH

Accession

Primary (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:	February 9, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)