Skip Header

Contribute Send feedback
Read comments (?) or add your own

P80065 (INVB_DAUCA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Beta-fructofuranosidase, soluble isoenzyme I

EC=3.2.1.26
Alternative name(s):
Invertase
Saccharase
Sucrose hydrolase
Gene names
Name:INV*DC4
OrganismDaucus carota (Carrot)
Taxonomic identifier4039 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridscampanulidsApialesApiaceaeApioideaeScandiceaeDaucinaeDaucus

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May participate in the regulation of the hexose level in mature tissues and in the utilization of sucrose stored in vacuoles.

Catalytic activity

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

Subunit structure

Monomer.

Subcellular location

Vacuole.

Post-translational modification

N-glycosylated; high-mannose and high-xylose complex glycans.

Miscellaneous

There are at least three isozymes of beta-fructofuranosidase in carrot: one insoluble and two soluble ones.

Sequence similarities

Belongs to the glycosyl hydrolase 32 family.

Ontologies

Keywords
   Cellular componentVacuole
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionsucrose alpha-glucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5757 Potential
Propeptide58 – 11558
PRO_0000033372
Chain116 – 661546Beta-fructofuranosidase, soluble isoenzyme I
PRO_0000033373

Amino acid modifications

Glycosylation1711N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation5121N-linked (GlcNAc...) Potential
Glycosylation6331N-linked (GlcNAc...) Potential

Natural variations

Natural variant211R → L in class 3.
Natural variant521S → A in class 3.
Natural variant561L → F in class 3.
Natural variant851R → H in class 3.
Natural variant2101V → I in class 2 and class 3.
Natural variant2771R → P in class 2 and class 3.
Natural variant3341G → V in class 2.
Natural variant418 – 4236TDSESA → SDNEST in class 2 and class 3.
Natural variant4681D → N in class 2 and class 3.
Natural variant5031G → R in class 2.
Natural variant5861H → P in class 2 and class 3.

Experimental info

Sequence conflict4221S → P AA sequence Ref.3
Sequence conflict4251L → V AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P80065 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: ED534C08D61745EA

FASTA66173,864
        10         20         30         40         50         60 
MDTYHFLPSR DLEHASSYTP RPDSPETRHE PDPDRSKTNR RPIKIVSSVL LSTLILSFVI 

        70         80         90        100        110        120 
FLLVNPNVQQ VVRKKVSKNS NGEDRNKASK SPEMLGPPSR GVSQGVSEKS FRQATAEPSY 

       130        140        150        160        170        180 
PWTNDMLSWQ RTSFHFQPQE NWMNDPNGPL FHMGWYHLFY QYNPDSAIWG NITWGHAISR 

       190        200        210        220        230        240 
DLINWLHLPF AMQPDQWYDI NGVWTGSATV LPDGKIVMLY TGDTDDLVQV QNLAYPANLS 

       250        260        270        280        290        300 
DPLLLDWIKY PDNPVMFPPP GIGSTDFRDP TTAWIGRDGK WRITIGSKVN KTGISLMYKT 

       310        320        330        340        350        360 
TDFITYELLD NLLHAVPGTG MWECVDFYPV SVTGSNGLDT SVNGPGVKHV LKSSLDDDRH 

       370        380        390        400        410        420 
DYYALGTYDP INDKWTPDNP ELDVGIGLRL DYGKYYASKT FYDQDKERRL LWGWIGETDS 

       430        440        450        460        470        480 
ESADLLKGWA SVQSIPRTVV FDKKTGTNIL QWPVKEVESL RSRSYEIDDV ELKPGSLVPL 

       490        500        510        520        530        540 
KISSAAQLDI VASFEVDEEA FKGTYEADAS YNCTASEGAA GRGILGPFGI LVLADDPLSE 

       550        560        570        580        590        600 
LTPVYFYIAK GVDGNAKTYF CADQSRSSTA SDVDKEVYGS DVPVLHGESL SMRLLVDHSI 

       610        620        630        640        650        660 
VESFAQGGRT VITSRVYPTR AIYSAARVFL FNNATGVSVT ASVKAWQMAS ATLKPFPFDQ 


L 

« Hide

References

[1]"cDNA cloning of carrot (Daucus carota) soluble acid beta-fructofuranosidases and comparison with the cell wall isoenzyme."
Unger C., Hardegger M., Lienhard S., Sturm A.
Plant Physiol. 104:1351-1357(1994) [PubMed: 8016265] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Nantaise.
Tissue: Flower bud.
[2]Sturm A.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Nantaise.
[3]"Purification and characterization of a soluble beta-fructofuranosidase from Daucus carota."
Unger C., Hofstenge J., Sturm A.
Eur. J. Biochem. 204:915-921(1992) [PubMed: 1541302] [Abstract]
Cited for: PROTEIN SEQUENCE OF 116-121; 269-280; 410-437 AND 507-511.
Strain: cv. Nantaise.
Tissue: Seed.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75351 mRNA. Translation: CAA53097.1.
X75352 mRNA. Translation: CAA53098.1.
X75353 mRNA. Translation: CAA53099.1.
Y18707 Genomic DNA. Translation: CAA77267.1.
PIRS37590.
S37591.
S37592.

3D structure databases

ProteinModelPortalP80065.
ModBaseSearch...

Protein family/group databases

CAZyGH32. Glycoside Hydrolase Family 32.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR021792. Beta-fructofuranosidase.
IPR008985. 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]
PfamPF11837. DUF3357. 1 hit.
PF08244. 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 nameINVB_DAUCA
AccessionPrimary (citable) accession number: P80065
Secondary accession number(s): Q42719, Q42720, Q42721
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 11, 2001
Last modified: September 21, 2011
This is version 74 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families