ID   1FEH_HORVU              Reviewed;         599 AA.
AC   Q70AT7;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Fructan 1-exohydrolase {ECO:0000312|EMBL:CAE53426.1};
DE            EC=3.2.1.153;
DE   Flags: Precursor;
GN   Name=1-FEH {ECO:0000312|EMBL:CAE53426.1};
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAE53426.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nagaraj V.J.;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes inulin-type beta-(2,1)-fructans. May play a role
CC       as a beta-(2,1)-trimmer during graminan biosynthesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q84PN8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (2->1)-linked beta-D-
CC         fructofuranose residues in fructans.; EC=3.2.1.153;
CC         Evidence={ECO:0000250|UniProtKB:Q84PN8};
CC   -!- ACTIVITY REGULATION: Inhibited by sucrose.
CC       {ECO:0000250|UniProtKB:Q84PN8}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000255}.
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DR   EMBL; AJ605333; CAE53426.1; -; mRNA.
DR   AlphaFoldDB; Q70AT7; -.
DR   SMR; Q70AT7; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   ExpressionAtlas; Q70AT7; baseline and differential.
DR   GO; GO:0033948; F:fructan beta-(2,1)-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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..599
FT                   /note="Fructan 1-exohydrolase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395557"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        449..495
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
SQ   SEQUENCE   599 AA;  66628 MW;  7129F94ECA99C954 CRC64;
     MAQAWAFLLL PALALASYAS HLLLPAYITT PLCGGGDGAR SFFLCAQAPK DQDQDPSPAS
     TMYKTAFHFQ PAKNWMNDPS GPMYFNGIYH EFYQYNLNGP IFGDIVWGHS VSTDLVNWIG
     LEPALVRDTP SDIDGCWTGS VTILPGGKPV IIYTGGNIDQ HQTQNIAFPK NRSDPYLREW
     IKAANNPVLR PDEPGMNVIE FRDPTTGWIG PDGHWRMAVG GELNGYSAAL LYKSEDFLNW
     TKVDHPPYSH NGSNMWECPD FFAALPGNNG GLDLSAAIPQ GAKHALKMSV DSVDKYMIGV
     YDLQRDAFVP DNVVDDRRLW LRMDYGTFYA SKSFFDSKKG RRIVWGWSGE TDSPSDDLAK
     GWAGLHTIPR TIWLAADGKQ LLQWPVEEIE SLRTNEINHQ GLELNKGDLF EIKEVDAFQA
     DVEIDFELAS IDEAEPFDPS WLLDPEKHCG EAGASVPGGI GPFGLVILAS DNMDEHTEVY
     FRVYKSQEKY MVLMCSDLRR SSLRPGLEKP AYGGFFEFDL AKERKISLRT LIDRSAVESF
     GGGGRVCITS RVYPAVLANV GRAHIYAFNN GNAMVRVPQL SAWTMRKAQV NVEKGWSAI