ID   1FEH_LEYCH              Reviewed;         600 AA.
AC   B6DXP5;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Fructan 1-exohydrolase {ECO:0000312|EMBL:ACI24008.1};
DE            EC=3.2.1.153;
DE   Flags: Precursor;
GN   Name=1-FEH {ECO:0000312|EMBL:ACI24008.1};
OS   Leymus chinensis (Chinese lyme grass) (Elymus chinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Leymus.
OX   NCBI_TaxID=52714;
RN   [1] {ECO:0000312|EMBL:ACI24008.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang L., Li X., Zhang J., Peng X., Su M., Chen Z., Liu G.;
RT   "Cloning and functional analysis of fructan 1-exohydrolase (1-FEH) from
RT   Leymus chinensis.";
RL   Submitted (SEP-2008) 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; FJ178114; ACI24008.1; -; mRNA.
DR   AlphaFoldDB; B6DXP5; -.
DR   SMR; B6DXP5; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..600
FT                   /note="Fructan 1-exohydrolase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395558"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        444..490
FT                   /evidence="ECO:0000250|UniProtKB:Q43866"
SQ   SEQUENCE   600 AA;  67194 MW;  9897E6C820C26E38 CRC64;
     MAQAWAFLLP VLFFGSYVTN LFLPTYASSP LCSGDGGRSF LCAQAPKDKD PSPASTMYKT
     AFHFQSAKNW MNDPSGPMYF NGIYHEFYQY NLNGPIFGDI VWGHSVSTDL INWIGLGPAL
     VRDTSSDIDG CWTGSVTILP GGKPVIIYTG GDIDQHQVQN IAFPKNRSDP YLREWIKAAN
     NPVLRPDEPG MNSIEFRDPT TGWIGPDGLW RMAVGGELNG YSAALLYKSE DFLNWTKVDH
     PLYSHNGSNM WECPDFFAVL PGNNGGLDLS AAIPQGAKHA LKMSVDSVDK YLIGVYDLKR
     DAFVPDNVID DRRLWLRIDY GTFYASKSFF DSNKGRRIIW GWSRETDSPS DDLEKGWAGL
     HTIPRRIWLA DDGKQLLQWP VDEIEFLRTN EINHQGLELN KGDLFEIKEV DTFQADVEID
     FELASIDDAD PFDPSWLLDP EKHCGEVGAS VPGGIGPFGL VILASDNMEE HTEVYFRVYK
     LQEKYMVLMC SDLRRSSMRP DLEKPAYGGF FEFDLAKERK ISLRTLIDRS AVESFGGGGR
     VCITSRVYPA VLADVGRAHM YAFNNGSATV RVPQLSAWTM RKAQVNVEKG WSAIQNRGSI