GFT_ASPOF
ID GFT_ASPOF Reviewed; 610 AA.
AC Q5FC15;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=6(G)-fructosyltransferase;
DE EC=2.4.1.243 {ECO:0000269|PubMed:15720693};
DE AltName: Full=6G-FFT;
DE Short=6GFT;
DE AltName: Full=6G-fructosyltransferase;
DE AltName: Full=AoFT1;
GN Name=FT1;
OS Asparagus officinalis (Garden asparagus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC Asparagoideae; Asparagus.
OX NCBI_TaxID=4686;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=cv. Zuiyuu;
RX PubMed=15720693; DOI=10.1111/j.1469-8137.2004.01294.x;
RA Ueno K., Onodera S., Kawakami A., Yoshida M., Shiomi N.;
RT "Molecular characterization and expression of a cDNA encoding
RT fructan:fructan 6G-fructosyltransferase from asparagus (Asparagus
RT officinalis).";
RL New Phytol. 165:813-824(2005).
RN [2]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITION.
RA Shiomi N.;
RT "Purification and characterisation of 6G-fructosyltransferase from the
RT roots of asparagus (Asparagus officinalis L.).";
RL Carbohydr. Res. 96:281-292(1981).
CC -!- FUNCTION: Involved in the synthesis of fructan of the inulin neoseries.
CC Has no 1-FFT activity. {ECO:0000269|PubMed:15720693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[1-beta-D-fructofuranosyl-(2->1)-]m+1 alpha-D-glucopyranoside
CC + [1-beta-D-fructofuranosyl-(2->1)-]n+1 alpha-D-glucopyranoside = [1-
CC beta-D-fructofuranosyl-(2->1)-]m alpha-D-glucopyranoside + [1-beta-D-
CC fructofuranosyl-(2->1)-]n+1 beta-D-fructofuranosyl-(2->6)-alpha-D-
CC glucopyranoside (m > 0, n >= 0).; EC=2.4.1.243;
CC Evidence={ECO:0000269|PubMed:15720693};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. Stable between pH 5.0-6.0.
CC {ECO:0000269|PubMed:15720693, ECO:0000269|Ref.2};
CC Temperature dependence:
CC Stable up to 37 degrees Celsius. {ECO:0000269|PubMed:15720693,
CC ECO:0000269|Ref.2};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Single-pass type
CC II membrane protein {ECO:0000305}.
CC -!- INDUCTION: Inhibited by Hg(2+), p-chloromercuribenzoate and Ag(+).
CC -!- PTM: Might be processed in two N-terminal and C-terminal proteolytic
CC fragments. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB084283; BAD89564.1; -; mRNA.
DR AlphaFoldDB; Q5FC15; -.
DR SMR; Q5FC15; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR KEGG; ag:BAD89564; -.
DR BRENDA; 2.4.1.243; 486.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033841; F:6G-fructosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..610
FT /note="6(G)-fructosyltransferase"
FT /id="PRO_0000310732"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..610
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT ACT_SITE 82
FT /evidence="ECO:0000250"
FT BINDING 79..82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141..142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207..208
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 460..508
FT /evidence="ECO:0000250"
SQ SEQUENCE 610 AA; 68315 MW; B65C60F475CE9DAC CRC64;
MATSLQAPIL GSRPPRRTLR FLSFALFSAL VLVVASFSSR KSESGSGLRS GSVEPEYAWT
NQMLTWQRAG FHFRTVKNYM NDPSGPMYYK GWYHLFYQHN PNYAYWGDIS WGHAVSRDLL
NWFHLPVAVK PDRWYDIYGV WTGSITVMPD DGRVVMLYTG GTKEKYQIMS VAMAADPSDP
LLVEWVKYDE VNPVLRPPPG IGLTDFRDPN PIWYNTTDST WQLVIGSKND SLQHTGIAMV
YTTKDFINLT LLPGVLHSVD HVGMWECVDL FPVASSGPLI GRGLDRSMML ADNVKHVLKA
SMNDEWHDYY AIGSYDVATH RWVPDDESVD VGIGMRIDWG KFYASRTFYD PVKERRVMWG
YVGETDSGDA DVAKGWASFQ GIPRTVLFDV KTGTNVLTWP IEEVESLRMT RKDFSDIVVN
KGSTVELHVG DANQLDIEAE FEMDKDALET AIEADIGYNC SSSGGAVSRG VLGPFGLFVL
ANQDLTELTA TYFYVSRATD GSLHTHLCHD EMRSSKANDI VKRVVGGTFT VLDGELLSLR
ILVDHSIVES FAQGGRTSAT SRVYPTEAIY ERARVFLFNN ATGATITAKA VKVWQMNSTS
NQYYPFTSSN
