1FEH2_WHEAT
ID 1FEH2_WHEAT Reviewed; 596 AA.
AC Q84LA1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Fructan 1-exohydrolase w2 {ECO:0000312|EMBL:ACI16117.1};
DE EC=3.2.1.153;
DE Flags: Precursor;
GN Name=1-FEHw2 {ECO:0000303|PubMed:12586886, ECO:0000303|Ref.2};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAD48199.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Pajero {ECO:0000269|PubMed:12586886};
RC TISSUE=Stem {ECO:0000269|PubMed:12586886};
RX PubMed=12586886; DOI=10.1104/pp.015305;
RA Van Den Ende W., Clerens S., Vergauwen R., Van Riet L., Van Laere A.,
RA Yoshida M., Kawakami A.;
RT "Fructan 1-exohydrolases. beta-(2,1)-trimmers during graminan biosynthesis
RT in stems of wheat? Purification, characterization, mass mapping, and
RT cloning of two fructan 1-exohydrolase isoforms.";
RL Plant Physiol. 131:621-631(2003).
RN [2] {ECO:0000312|EMBL:ACI16117.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chinese Spring {ECO:0000269|Ref.2};
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, but not beta-
CC (2,1)-linkages in branched fructans. Has low activity against beta-
CC (2,6)-linked fructans. May play a role as a beta-(2,1)-trimmer during
CC graminan biosynthesis. {ECO:0000269|PubMed:12586886}.
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:12586886};
CC -!- ACTIVITY REGULATION: Inhibited by sucrose.
CC {ECO:0000269|PubMed:12586886}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 mM for 1-kestose {ECO:0000269|PubMed:12586886};
CC pH dependence:
CC Optimum pH is 4.5-5.5. Inactive above pH 7.5.
CC {ECO:0000269|PubMed:12586886};
CC Temperature dependence:
CC Optimum temperature is 30-40 degrees Celsius.
CC {ECO:0000269|PubMed:12586886};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ508387; CAD48199.1; -; mRNA.
DR EMBL; FJ184991; ACI16117.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84LA1; -.
DR SMR; Q84LA1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PRIDE; Q84LA1; -.
DR EnsemblPlants; TraesCS6D02G064400.1; TraesCS6D02G064400.1; TraesCS6D02G064400.
DR Gramene; TraesCS6D02G064400.1; TraesCS6D02G064400.1; TraesCS6D02G064400.
DR KEGG; ag:CAD48199; -.
DR OMA; REWIKAP; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q84LA1; baseline and differential.
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; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..596
FT /note="Fructan 1-exohydrolase w2"
FT /evidence="ECO:0000255"
FT /id="PRO_5000068836"
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; 66603 MW; AA867C8888FD1CD6 CRC64;
MAQAWAFLLP VLVLGSYVTS LFFPSYISNP LCGGDGGRSL FLCAQAPKDQ DPSPAVSTMY
KTAFHFQPAK NWMNDPSGPM YFNGIYHEFY QYNLNGPIFG DIVWGHSVST DLVNWIGLEP
ALVRDTPSDI DGCWTGSVTI LPGGKPIIIY TGGDIDQHQA QNIAFPKNRS DPYLREWIKA
PNNPVLRPDE PGMNSIEFRD PTTGWIGPDG LWRMAVGGEL NGYSAALLYK SEDFLNWTKV
DHPLYSHNGS NMWECPDFFA VLPGNNAGLD LSAAIPQGAK HALKMSVDSV DKYMIGVYDL
QRDAFVPDNV VDDRRLWLRI DYGTFYASKS FFDSNKNRRI IWGWSRETDS PSDDLEKGWA
GLHTIPRTIW LAGDGKQLLQ WPVEEIESLR TNEISHQGIE LNKGDLFEIK EVDAFQADVE
IDFELASIDD ADPFDPSWLL DPEKHCGEAG ASVPGGIGPF GLVILASDNM DEHTEVYFRV
YKSQEKYMVL MCSDLRRSSL RPDLEKPAYG GFFEFDLEKE RKISLRTLID RSAVESFGGG
GRVCITSRVY PAVLADVGRA HIYAFNNGSA TVRVPQLSAW TMRKAQVNVE KGWSAI
