ID   6FEH_BETVU              Reviewed;         606 AA.
AC   Q70XE6;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Fructan 6-exohydrolase {ECO:0000312|EMBL:CAD48404.1};
DE            EC=3.2.1.154;
DE   Flags: Precursor;
GN   Name=6-FEH {ECO:0000312|EMBL:CAD48404.1};
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAD48404.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Root {ECO:0000269|PubMed:14617070};
RX   PubMed=14617070; DOI=10.1046/j.1365-313x.2003.01912.x;
RA   Van den Ende W., De Coninck B., Clerens S., Vergauwen R., Van Laere A.;
RT   "Unexpected presence of fructan 6-exohydrolases (6-FEHs) in non-fructan
RT   plants: characterization, cloning, mass mapping and functional analysis of
RT   a novel 'cell-wall invertase-like' specific 6-FEH from sugar beet (Beta
RT   vulgaris L.).";
RL   Plant J. 36:697-710(2003).
CC   -!- FUNCTION: Hydrolyzes levan-type beta-(2->6)-linked fructans to
CC       fructose, but not inulin-type beta-(2->1)-linked fructans.
CC       {ECO:0000269|PubMed:14617070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (2->6)-linked beta-D-
CC         fructofuranose residues in fructans.; EC=3.2.1.154;
CC         Evidence={ECO:0000269|PubMed:14617070};
CC   -!- ACTIVITY REGULATION: Not inhibited by sucrose.
CC       {ECO:0000269|PubMed:14617070}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=77 mM for 6-kestose {ECO:0000269|PubMed:14617070};
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|PubMed:14617070};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:14617070};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000255}.
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; AJ508534; CAD48404.1; -; mRNA.
DR   AlphaFoldDB; Q70XE6; -.
DR   SMR; Q70XE6; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   PRIDE; Q70XE6; -.
DR   EnsemblPlants; KMT04889; KMT04889; BVRB_7g170560.
DR   Gramene; KMT04889; KMT04889; BVRB_7g170560.
DR   KEGG; ag:CAD48404; -.
DR   PhylomeDB; Q70XE6; -.
DR   BRENDA; 3.2.1.154; 836.
DR   GO; GO:0033949; F:fructan beta-(2,6)-fructosidase activity; IEA:UniProtKB-EC.
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; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..606
FT                   /note="Fructan 6-exohydrolase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395865"
FT   ACT_SITE        70
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        564
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        585
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        590
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        593
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        445..491
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
SQ   SEQUENCE   606 AA;  68496 MW;  CD19CB6816AA5E92 CRC64;
     MAPNNGSWLV LSISMMLLSH GMIIIAKDQA IHHHDDDHDD MLINDHQMIN DDDPYRTAYH
     FQSPKNWMND PNGPMIYKGI YHLFYQYYPY DPVWHTEIVW GHSTSTDLIN WTQQPIALSP
     SEPYDINGCW SGSITILPQN KPVILYTGIN NKNYQVQNLA LPKNLSDPYL KEWIKLPQNP
     LMAGTPTNNN NINASSFRDP STAWQLSDGK WRVIVGTQQG KRGLAVLFTS DDFVKWNNTG
     NPLHSTEGNG IWECPDFFPV YVGKSLGADT SIIGDDVKHV LKLSLFDTQY EYYTIGRYDI
     EKDIYVPDEG SIESDLGLRY DYGKFYASKS FFDDETNRRI LWGWVNESSI QADDIKKGWS
     GVQAIPRTVV LDKSGKQLVQ WPLAEVDMLR ENDVELPSQV IKGGSLVEIS QITASQADVE
     ISFKIPESNY VEELDSTCTN PQILCSQKGA SIKGRFGPFG LLTLASMGLE EYTAVFFRIF
     KGPNKYVVLM CSDQTRSSLN PTTDKLSFGI FVDVDPINED LSLRILIDHS IVESFSAKGK
     SCITARVYPT MAINDKAKLY VFNNGTEDVK ITKLSAWSMK KAQINLSTDN TSNMSYNSNK
     VEKEEF