ID   1FEH_BROPI              Reviewed;         602 AA.
AC   D2IGW7;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Fructan 1-exohydrolase {ECO:0000312|EMBL:ACZ65470.1};
DE            EC=3.2.1.153;
DE   Flags: Precursor;
GN   Name=1-FEHa {ECO:0000303|PubMed:19789892};
OS   Bromus pictus (Patagonian grass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Bromeae; Bromus.
OX   NCBI_TaxID=629273;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ACZ65470.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   TISSUE=Leaf {ECO:0000269|PubMed:19789892};
RX   PubMed=19789892; DOI=10.1007/s00425-009-1020-5;
RA   Del Viso F., Puebla A.F., Hopp H.E., Heinz R.A.;
RT   "Cloning and functional characterization of a fructan 1-exohydrolase (1-
RT   FEH) in the cold tolerant Patagonian species Bromus pictus.";
RL   Planta 231:13-25(2009).
CC   -!- FUNCTION: Hydrolyzes inulin-type beta-(2,1)-fructans. Has low activity
CC       against beta-(2,6)-linked fructans. May play a role as a beta-(2,1)-
CC       trimmer during graminan biosynthesis. {ECO:0000250|UniProtKB:Q84PN8,
CC       ECO:0000269|PubMed:19789892}.
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:0000269|PubMed:19789892};
CC   -!- ACTIVITY REGULATION: Inhibited by sucrose.
CC       {ECO:0000250|UniProtKB:Q84PN8}.
CC   -!- TISSUE SPECIFICITY: Detected in leaves, with maximum levels at the leaf
CC       tip. {ECO:0000269|PubMed:19789892}.
CC   -!- INDUCTION: In the first section of the leaf sheath expression decreases
CC       after 7 days of cold treatment. In the second section of the leaf
CC       sheath expression increases upon cold treatment. In the thrid section
CC       of the leaf sheath and the first section from the leaf blade expression
CC       increases in the first 4 days of cold treatment before returning to its
CC       original levels. In the leaf tip expression decreases after 2 days of
CC       cold treatment. {ECO:0000269|PubMed:19789892}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000255}.
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DR   EMBL; GQ247882; ACZ65470.1; -; mRNA.
DR   AlphaFoldDB; D2IGW7; -.
DR   SMR; D2IGW7; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   BRENDA; 3.2.1.153; 993.
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   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..602
FT                   /note="Fructan 1-exohydrolase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395556"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        452..498
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
SQ   SEQUENCE   602 AA;  67078 MW;  5CBA2E8D1A9B1D89 CRC64;
     MAQAWAFLLL PVLLLSSYAS HRLFPSYITG PLCGSTTTSS SSSSGVRSFL CSQQDSQTPS
     PASTMYKTAF HFQPAKNWIN DPSGPMYFNG FYHEFYQYNL NGPTFGDIVW GHSVSTDLVN
     WIGLEPALVR DTPSDIDGCW TGSVTILPGG QPVIIYTGGD IEKHQAQNIA FPKNRSDPYL
     REWTKVINNP VLLPNEPGMN SIEFRDPTTG WIGPDGHWRM AVGAEWHGYS AALLYKSEDF
     LNWTMVDHPL YSHNGTNMWE CPDFYAVLPG NNGGLDLSAA IPQGAKHALK MSVDSVDKYM
     IGVYDLERDA FVPDVVLDDH RLWLRIDYGT FYASKSFYDS KKGRRVIWGW SRETDSPSDD
     LEKGWAGLHT IPRTIWLDGD GKQLLQWPVD EIESLRTNEI NHQGLELNKG DLFEIKGVDT
     FQADVEIDFE LPSLDDAEPF DPSWLLDPEM HCGEAGASVQ GGIGPFGLVI LASNDMNEHT
     EVYFRVYKSQ EKGMVLMCSD LRRSSLRPGL ETPAYGGFFE LDLAKEKKIS LRTLIDRSAV
     ESFGGGGRVC ITSRVYPAVL ADGGSAHMYA FNNGNAIVKV PQLRAWTMRK AQVNVEMGWS
     AI