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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: -Experimental evidence at protein leveli

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

Catalytic activityi

(1-beta-D-fructofuranosyl-(2->1)-)(m+1) alpha-D-glucopyranoside + (1-beta-D-fructofuranosyl-(2->1)-)(n+1) alpha-D-glucopyranoside = (1-beta-D-fructofuranosyl-(2->1)-)(m) alpha-D-glucopyranoside + (1-beta-D-fructofuranosyl-(2->1)-)(n+1) beta-D-fructofuranosyl-(2->6)-alpha-D-glucopyranoside (m > 0; n > = 0).
(Beta-D-fructosyl-(2->1)-)(m) + (beta-D-fructosyl-(2->1)-)(n) = (beta-D-fructosyl-(2->1)-)(m-1) + (beta-D-fructosyl-(2->1)-)(n+1).

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
Active sitei85By similarity1
Binding sitei101SubstrateBy similarity1
Binding sitei109SubstrateBy similarity1
Binding sitei267SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.243 248

Protein family/group databases

CAZyiGH32 Glycoside Hydrolase Family 32

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional 6(G)-fructosyltransferase/2,1-fructan:2,1-fructan 1-fructosyltransferase (EC:2.4.1.100, EC:2.4.1.243)
Short name:
1-FFT
Short name:
6G-FFT
Short name:
6GFT
Short name:
FFT
OrganismiAllium cepa (Onion)
Taxonomic identifieri4679 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 24CytoplasmicSequence analysisAdd BLAST24
Transmembranei25 – 45Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini46 – 612VacuolarSequence analysisAdd BLAST567

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003107331 – 612Bifunctional 6(G)-fructosyltransferase/2,1-fructan:2,1-fructan 1-fructosyltransferaseAdd BLAST612

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi111N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi216N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi230N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi465N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi466 ↔ 514By similarity
Glycosylationi586N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi603N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP92916

Expressioni

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

Structurei

3D structure databases

ProteinModelPortaliP92916
SMRiP92916
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni82 – 85Substrate bindingBy similarity4
Regioni144 – 145Substrate bindingBy similarity2
Regioni208 – 209Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 32 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

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

Sequencei

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
Checksum:i6BE93637A9EAA7EA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
EMBLi
GenBanki
DDBJi
Links Updated
Y07838 mRNA Translation: CAA69170.1

Similar proteinsi

Entry informationi

Entry nameiGFT_ALLCE
AccessioniPrimary (citable) accession number: P92916
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 1997
Last modified: May 23, 2018
This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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