ID   SST_FESAR               Reviewed;         654 AA.
AC   Q9FSV7;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Sucrose:sucrose 1-fructosyltransferase;
DE            EC=2.4.1.99;
DE   AltName: Full=Sucrose 1(F)-fructosyltransferase;
DE   AltName: Full=Sucrose:sucrose 1(F)-beta-D-fructosyltransferase;
DE   Flags: Precursor;
GN   Name=1-SST;
OS   Festuca arundinacea (Tall fescue) (Schedonorus arundinaceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type); Loliinae;
OC   Lolium.
OX   NCBI_TaxID=4606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 107-116, FUNCTION,
RP   CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Hyt;
RX   PubMed=11080298; DOI=10.1104/pp.124.3.1217;
RA   Luescher M., Hochstrasser U., Vogel G., Aeschbacher R., Galati V.,
RA   Nelson C.J., Boller T., Wiemken A.;
RT   "Cloning and functional analysis of sucrose:sucrose 1-fructosyltransferase
RT   from tall fescue.";
RL   Plant Physiol. 124:1217-1228(2000).
CC   -!- FUNCTION: Transferase involved in fructan biosynthesis that catalyzes
CC       the production of 1-kestose (fructose and nystose to a lower extent)
CC       from sucrose. Exhibits also some hydrolase activity toward 1-kestose,
CC       thus producing fructose and sucrose. A weak fructosyltransferase
CC       activity leads to the formation of nystose from 1-kestose.
CC       {ECO:0000269|PubMed:11080298}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 sucrose = 1(F)-beta-D-fructosylsucrose + D-glucose;
CC         Xref=Rhea:RHEA:23312, ChEBI:CHEBI:4167, ChEBI:CHEBI:16885,
CC         ChEBI:CHEBI:17992; EC=2.4.1.99;
CC         Evidence={ECO:0000269|PubMed:11080298};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Accumulates at the base of growing leaves.
CC       {ECO:0000269|PubMed:11080298}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; AJ297369; CAC05261.1; -; mRNA.
DR   AlphaFoldDB; Q9FSV7; -.
DR   SMR; Q9FSV7; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   KEGG; ag:CAC05261; -.
DR   BRENDA; 2.4.1.99; 2244.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:InterPro.
DR   GO; GO:0050306; F:sucrose 1F-fructosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR021792; Beta-fructofuranosidase_N.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001362; Glyco_hydro_32.
DR   InterPro; IPR018053; Glyco_hydro_32_AS.
DR   InterPro; IPR013189; Glyco_hydro_32_C.
DR   InterPro; IPR013148; Glyco_hydro_32_N.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF11837; DUF3357; 1.
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.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Glycosyltransferase;
KW   Hydrolase; Transferase; Vacuole.
FT   PROPEP          1..106
FT                   /evidence="ECO:0000269|PubMed:11080298"
FT                   /id="PRO_0000419020"
FT   CHAIN           107..654
FT                   /note="Sucrose:sucrose 1-fructosyltransferase"
FT                   /id="PRO_0000419021"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   654 AA;  71382 MW;  6FF0A96F95D5BE52 CRC64;
     MESSAVVPGT TAPLLPYAYA PLPSSADDAR ENQSSGGVRW RVCAAVLAAS ALAVLIVVGL
     LAGGRVDRGP AGGDVASAAV PAVPMEIPRS RGKDFGVSEK ASGAYSADGG FPWSNAMLQW
     QRTGFHFQPE KHYMNDPNGP VYYGGWYHLF YQYNPKGDSW GNIAWAHAVS KDMVNWRHLP
     LAMVPDQWYD SNGVLTGSIT VLPDGQVILL YTGNTDTLAQ VQCLATPADP SDPLLREWIK
     HPANPILYPP PGIGLKDFRD PLTAWFDHSD NTWRTVIGSK DDDGHAGIIL SYKTKDFVNY
     ELMPGNMHRG PDGTGMYECI DLYPVGGNSS EMLGGDDSPD VLFVLKESSD DERHDYYALG
     RFDAAANIWT PIDQELDLGI GLRYDWGKYY ASKSFYDQKK NRRIVWAYIG ETDSEQADIT
     KGWANLMTIP RTVELDKKTR TNLIQWPVEE LDTLRRNSTD LSGITVDAGS VIRLPLHQGA
     QIDIEASFQL NSSDVDALTE ADVSYNCSTS GAAVRGALGP FGLLVLANGR TEQTAVYFYV
     SKGVDGALQT HFCHDESRST QAKDVVNRMI GSIVPVLDGE TFSVRVLVDH SIVQSFAMGG
     RITATSRAYP TEAIYAAAGV YLFNNATGAT VTAERLVVYE MASADNHIFT NDDL