6FEH_WHEAT
ID 6FEH_WHEAT Reviewed; 598 AA.
AC Q2UXF7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Fructan 6-exohydrolase {ECO:0000312|EMBL:CAJ28591.1};
DE EC=3.2.1.154;
DE Flags: Precursor;
GN Name=6-FEH {ECO:0000312|EMBL:CAJ28591.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAJ28591.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 151-163; 299-314 AND
RP 399-414, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Pajero {ECO:0000269|PubMed:16330524};
RC TISSUE=Spike {ECO:0000312|EMBL:CAJ28591.1};
RX PubMed=16330524; DOI=10.1093/jxb/erj031;
RA Van Riet L., Nagaraj V., Van den Ende W., Clerens S., Wiemken A.,
RA Van Laere A.;
RT "Purification, cloning and functional characterization of a fructan 6-
RT exohydrolase from wheat (Triticum aestivum L.).";
RL J. Exp. Bot. 57:213-223(2006).
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:16330524}.
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:16330524};
CC -!- ACTIVITY REGULATION: Not inhibited by sucrose.
CC {ECO:0000269|PubMed:16330524}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots and
CC inflorescences. Maximum expression is detected in stems, particularly
CC the penultimate internode. {ECO:0000269|PubMed:16330524}.
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; AM075205; CAJ28591.1; -; mRNA.
DR AlphaFoldDB; Q2UXF7; -.
DR SMR; Q2UXF7; -.
DR STRING; 4565.Traes_2BL_16B7CE123.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PRIDE; Q2UXF7; -.
DR eggNOG; KOG0228; Eukaryota.
DR BRENDA; 3.2.1.154; 6500.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q2UXF7; baseline and differential.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..598
FT /note="Fructan 6-exohydrolase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395873"
FT ACT_SITE 65
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 451..497
FT /evidence="ECO:0000250|UniProtKB:Q43866"
SQ SEQUENCE 598 AA; 66213 MW; A59B7355A68B53AB CRC64;
MAARLPLAAC VVAFHLCLLL SSLVRSPSTA LRRLSEAESS LVRHGHGVGI RPAYHFLPAK
NWQNDPNGPM YHNGVYHMFY QYNPLGAMWQ PGNLSWGHSV SRDLVNWDAL DTALDPTAPF
DYNGCWSGSA TILPGGIPAL LYTGRIDADK EVQVQNVAFP KNPADPLLRE WVKPAYNPVI
PLPADVPGDN FRDPTTAWVG RDGLWRIAVA AKVGGPNGIA STLIYRSKDF RHWKRNASPL
YTSRAAGMVE CPDLFPVAEP GVEEGRLGYA SGPASGAVRH VLKLSVMNTT QDYYAVGRYD
DVADTFVPEV DVERNADDCR TWRRFDYGHV YASKSFFDSS KNRRVLWAWA NESDSQDNDI
ARGWSGVQTV PRKVWLDEDG KQVRQWPIEE IETLRSKRVV GLLGAQVNAG GVNKITGVGA
QADVEAIFEI PSLEEAETFQ PNWLLDPQKL CEENGASVPG KVGPFGLLVM ASSNMQEHTA
IFFRVFRHNQ KYKVLMCTDL TRSTGRDNVY KPSYGGFVDI DIEQQGRTIS LRTLIDHSVV
ESFGGGGRTC ITARVYPEHA ENKNSHVFVF NNGTGLVKVS KLEAWRLAMA SVNVVHGR
