ID   1FEH_TRIUA              Reviewed;         597 AA.
AC   B6DZD0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Fructan 1-exohydrolase;
DE            EC=3.2.1.153;
DE   Flags: Precursor;
GN   Name=1-FEH {ECO:0000250|UniProtKB:Q84PN8};
OS   Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4572;
RN   [1] {ECO:0000312|EMBL:ACI16118.1}
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; FJ184992; ACI16118.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6DZD0; -.
DR   SMR; B6DZD0; -.
DR   STRING; 4572.TRIUR3_08289-P1; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   eggNOG; KOG0228; Eukaryota.
DR   Proteomes; UP000015106; Unassembled WGS sequence.
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; Reference proteome;
KW   Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..597
FT                   /note="Fructan 1-exohydrolase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395559"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   CARBOHYD        169
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        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        447..493
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
SQ   SEQUENCE   597 AA;  66677 MW;  6454498F9BD88649 CRC64;
     MAQAWAFLLP VLVFGSYMTS LFFPTYISGP LCGGDGGGRS LFLCAQAPKD QDPSPAVSTM
     YKTAFHFQPA KNWMNDPSGP MYFNGFYHEF YQYNPNGPIF GDIVWGHSVS TDLVNWIGLE
     PALVRDTPSD IDGCWTGSVT ILPGGKPVII YTGGDKDQHQ AQNIAFPKNR SDPYLREWIK
     AANNPVLRPD EPGMNSIEFR DPTTGWIGPD GLWRMAVGGE LNGYSAALLY KSEDFLNWTK
     VDHPLYSHNG SNMWECPDFF AVLPGNNAGL DLSAAIPQGA KHALKMSVDS VDKYMIGVYD
     LQRDAFVPDN VVDDRRLWLR IDYGTFYASK SFFDSNKNRR IIWGWSRETD SPSDDLEKGW
     AGLHTIPRTI WLADDGKQLL QWPVEEIESL RTNEISHQGI ELNKGDLFEI KEVDAFQADV
     EIGFELASID DADPFDPSWL LDPEKHCGEA GASVPGGIGP FGLVILASDN MDEHTEVYFR
     VYKSEEKYMV LMCSDLRRSS LRPDLEKPAY GGFFEFDLEK ERKISLRTLI DRSAVESFGG
     GGRVCITSRV YPAVLADVGR AHIYAFNNGS ATVRVPQLSA WTMRKAQVNV EKGWSAI