ID   1FEH_AEGSP              Reviewed;         595 AA.
AC   B6DZD1;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Fructan 1-exohydrolase {ECO:0000312|EMBL:ACI16119.1};
DE            EC=3.2.1.153;
DE   Flags: Precursor;
GN   Name=1-FEH {ECO:0000250|UniProtKB:Q84PN8};
OS   Aegilops speltoides (Goatgrass) (Triticum speltoides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=4573;
RN   [1] {ECO:0000312|EMBL:ACI16119.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND44093987;
RA   Zhang J., Huang S., Fosu-Nyarko J., Dell B., McNeil M., Waters I.,
RA   Moolhuijzen P., Conocono E., Appels R.;
RT   "The genome structure of the 1-FEH genes in wheat (Triticum aestivum L.):
RT   new markers to track stem carbohydrates and grain filling QTLs in
RT   breeding.";
RL   Mol. Breed. 22:339-351(2008).
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; FJ184993; ACI16119.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6DZD1; -.
DR   SMR; B6DZD1; -.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..595
FT                   /note="Fructan 1-exohydrolase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395554"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        445..491
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
SQ   SEQUENCE   595 AA;  66492 MW;  32B3378BFFE12FD2 CRC64;
     MAQAWAFLLP LLVLGSYVTS LFFPTYISNP LCGGDGGRSF HLCAQAPKDP DPPAVSTMYK
     TAFHFQPAKN WMNDPSGPMY FNGIYHEFYQ YNLNGPIFGD IVWGHSVSTD LVNWIGLEPA
     LVRDTPSDID GCWTGSVTIL PGGKPIIIYT GGDIDQNQAQ NIAFPKNRSD PYLREWIKAD
     NNPVLRPDEP GMNSIEFRDP TTGWIGPDGL WRMAVGGELN GYSAALLYKS EDFLNWTKVD
     HPLYSHNGSN MWECPDFFAV LPGNNAGLDL SAAIPQGAKH ALKMSVDSVD KYMIGVYDLQ
     RDAFVPDNVV DDRRLWLRID YGTFYASKSF FDSNKNRRII WGWSRETDSP SDDLAKGWAG
     LHTIPRTIWL AGDGKQLLQW PVEEIESLRT NEINHQGLEL NKGDLFEIKE VDAFQADVEI
     DFELASIDDA DRFDPSWLLD PEKHCGEAGA SVPGGIGPFG LVILASDNMD EHTEVYFRVY
     KSEEKYMVLM CSDLRRSSLR PDLEKPAYGG FFEFDLEKER KISLRTLIDR SAVESFGGGG
     RVCITSRVYP AVLADVGRAH IYAFNNGSAT VSVPQLSAWT MRKAQVNVEK GWSAI