1FEH_AEGTA
ID 1FEH_AEGTA Reviewed; 596 AA.
AC B6DZD2;
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;
DE EC=3.2.1.153;
DE Flags: Precursor;
GN Name=1-FEH {ECO:0000250|UniProtKB:Q84PN8};
OS Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=37682;
RN [1] {ECO:0000312|EMBL:ACI16120.1}
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; FJ184994; ACI16120.1; -; Genomic_DNA.
DR AlphaFoldDB; B6DZD2; -.
DR SMR; B6DZD2; -.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..596
FT /note="Fructan 1-exohydrolase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395555"
FT ACT_SITE 75
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 446..492
FT /evidence="ECO:0000250|UniProtKB:Q43866"
SQ SEQUENCE 596 AA; 66505 MW; 728C8ABBEF21B998 CRC64;
MAQAWAFLLP VLVLGSYVTS LFFPSYISNP LCGGDGGRSL FLCAQAPKDQ DPSPAVSTMY
KTAFHFQPAK NWMNDPSGPM YFNGIYHEFY QYNLNGPIFG DIVWGHSVST DLVNWIGLEP
ALVRDTPSDI DGCWTGSVTI LPGGKPIIIY TGGDIDQHQA QNIAFPKNRS DPYLREWIKA
PNNPVLRPDG PGMNSIEFRD PTTGWIGPDG LWRMAVGGEL NGYSAALLYK SEDFLNWTKV
DHPLYSHNGS NMWECPDFFA VLPGNNAGLD LSAAIPQGAK HALKMSVDSV DKYMIGVYDL
QRDAFVPDNV VDDRRLWLRI DYGTFYASKS FFDSNKNRRI IWGWSRETDS PSDDLEKGWA
GLHTIPRTIW LAGDGKQLLQ WPVEEIESLR TNEISHQGIE LNKGDLFEIK EVDAFQADVE
IVFELASIDD ADSFDPSWLL DPEKHCGEAG ASVPGGIGPF GLVILASDNM DEHTEVYFRV
YKSQEKYMVL MCSDLRRSSL RPDLEKPAYG GFFEFDLEKE RKISLRTLID RSAVESFGGG
GRVCITSRVY PAVLADVGRA HIYAFNNGSA TVRVPQLSAW TMRKAQVNVE KGWSAI
