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Entry version 85 (11 Dec 2019)
Sequence version 1 (01 May 1997)
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Protein

Bifunctional 6(G)-fructosyltransferase/2,1-fructan:2,1-fructan 1-fructosyltransferase

Gene
N/A
Organism
Allium cepa (Onion)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the synthesis of fructan of the inulin neoseries. Catalyzes a self-transfer between identical oligosaccharides of the 1-kestose series.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=88 mM for 1-kestose (3a) (for 6G-FFT activity)1 Publication
  2. KM=18 mM for 1-kestose (3a) (for 1-FFT activity)1 Publication
  3. KM=310 mM for nystose (4a) (for 6G-FFT activity)1 Publication
  4. KM=440 mM for nystose (4a) (for 1-FFT activity)1 Publication
  1. Vmax=10.5 mmol/min/mg enzyme toward 1-kestose (3a) for 6G-FFT activity1 Publication
  2. Vmax=7.51 mmol/min/mg enzyme toward 1-kestose (3a) for 1-FFT activity1 Publication
  3. Vmax=34.9 mmol/min/mg enzyme toward nystose (4a) for 6G-FFT activity1 Publication
  4. Vmax=3.66 mmol/min/mg enzyme toward nystose (4a) for 1-FFT activity1 Publication

pH dependencei

Optimum pH is 5.68 for both catalytic activities. Stable between pH 5.0-6.3.1 Publication

Temperature dependencei

Stable up to 40 degrees Celsius for both catalytic activities.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei85By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei101SubstrateBy similarity1
Binding sitei109SubstrateBy similarity1
Binding sitei267SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase, Transferase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.243 248

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH32 Glycoside Hydrolase Family 32

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bifunctional 6(G)-fructosyltransferase/2,1-fructan:2,1-fructan 1-fructosyltransferase (EC:2.4.1.1001 Publication, EC:2.4.1.2431 Publication)
Short name:
1-FFT
Short name:
6G-FFT
Short name:
6GFT
Short name:
FFT
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAllium cepa (Onion)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri4679 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 24CytoplasmicSequence analysisAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei25 – 45Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini46 – 612VacuolarSequence analysisAdd BLAST567

Keywords - Cellular componenti

Membrane, Vacuole

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003107331 – 612Bifunctional 6(G)-fructosyltransferase/2,1-fructan:2,1-fructan 1-fructosyltransferaseAdd BLAST612

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi111N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi216N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi230N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi465N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi466 ↔ 514By similarity
Glycosylationi586N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi603N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Might be processed in two N-terminal and C-terminal proteolytic fragments.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P92916

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

6G-FFT activity is induced by high sucrose under continuous light. Both 6G-fFFT and 1-FFT activities are strongly inhibited by HgCl2, AgNO3, p-chloromercuribenzoate and SDS, partially inhibited by CaCl2, MgCl2, MnCl2, FeCl2, CoCl2, ZnCl2, SnCl2, CuSO4 and EDTA, and activated by sodium deoxycholate, triton X-100 and tween-80.1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P92916

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni82 – 85Substrate bindingBy similarity4
Regioni144 – 145Substrate bindingBy similarity2
Regioni208 – 209Substrate bindingBy similarity2

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.115.10.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013320 ConA-like_dom_sf
IPR001362 Glyco_hydro_32
IPR013189 Glyco_hydro_32_C
IPR013148 Glyco_hydro_32_N
IPR023296 Glyco_hydro_beta-prop_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08244 Glyco_hydro_32C, 1 hit
PF00251 Glyco_hydro_32N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00640 Glyco_32, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49899 SSF49899, 1 hit
SSF75005 SSF75005, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P92916-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDAQDIESRH PLIGARPRRR ALRSLSILLA AALLLGLVLF YANGTGSGTA
60 70 80 90 100
VDPVRVDNEF PWTNDMLAWQ RCGFHFRTVR NYMNDPSGPM YYKGWYHLFY
110 120 130 140 150
QHNKDFAYWG NITWGHAVSR DLINWQHLPV AVGPDHWYDI SGVWTGSIIV
160 170 180 190 200
VSEDRVVMLF TGGTKSFDQS INLAEAADPS DPLLLKWIKY DNNPILWPPP
210 220 230 240 250
GIVRDDFRDP NPIWYNASES TYHIVVGSKN DSLQHTGIAL VYLTKDFKKF
260 270 280 290 300
DLLPTVLHSV DKVGMWECVE VYPVATTGPL LHKAIDNFDV DRVLDRSTVK
310 320 330 340 350
HVLKASMNDE WHDYYAIGTF DPIGNKWTPD DETVDVGIGL RYDWGKFYAS
360 370 380 390 400
RTFFDPLKQR RIIWGYIGEV DSQKADIAKG WASLQGIPRS VLYDVKTGTN
410 420 430 440 450
VLTWPIEEME GLRMARKDFS GIKIKKGSTV ELSDFGDAFQ IDIEAEFTIS
460 470 480 490 500
KEALEATIEA DVGYNCSSSG GAAIRGTLGP FGLLVLANQD LTENTATYFY
510 520 530 540 550
VSKGIDGSLI THFCQDETRS SKANDIVKRV VGGTVPVLDG ETFAVRILVD
560 570 580 590 600
HSVIESFAMG GRTSATSRAY PTEAINSAAR VFLFNNATGV DVIAESVKIW
610
QMNSTYNDFY HF
Length:612
Mass (Da):68,631
Last modified:May 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6BE93637A9EAA7EA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti56V → A AA sequence (PubMed:15720662).Curated1
Sequence conflicti468S → T AA sequence (PubMed:15720662).Curated1
Sequence conflicti474I → T AA sequence (PubMed:15720662).Curated1
Sequence conflicti505I → T AA sequence (PubMed:15720662).Curated1
Sequence conflicti508S → A AA sequence (PubMed:15720662).Curated1
Sequence conflicti510I → R AA sequence (PubMed:15720662).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y07838 mRNA Translation: CAA69170.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07838 mRNA Translation: CAA69170.1

3D structure databases

SMRiP92916
ModBaseiSearch...

Protein family/group databases

CAZyiGH32 Glycoside Hydrolase Family 32

Proteomic databases

PRIDEiP92916

Enzyme and pathway databases

BRENDAi2.4.1.243 248

Family and domain databases

Gene3Di2.115.10.20, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR001362 Glyco_hydro_32
IPR013189 Glyco_hydro_32_C
IPR013148 Glyco_hydro_32_N
IPR023296 Glyco_hydro_beta-prop_sf
PfamiView protein in Pfam
PF08244 Glyco_hydro_32C, 1 hit
PF00251 Glyco_hydro_32N, 1 hit
SMARTiView protein in SMART
SM00640 Glyco_32, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
SSF75005 SSF75005, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGFT_ALLCE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P92916
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 1997
Last modified: December 11, 2019
This is version 85 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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