1FEH1_WHEAT
ID 1FEH1_WHEAT Reviewed; 597 AA.
AC Q84PN8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Fructan 1-exohydrolase w1 {ECO:0000312|EMBL:CAD56806.1};
DE EC=3.2.1.153;
DE Flags: Precursor;
GN Name=1-FEHw1 {ECO:0000312|EMBL:CAD56806.1};
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:CAD56806.1}
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:ACI16115.1}
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 and beta-(2,1)-
CC linkages in branched fructans. Has low activity against beta-(2,6)-
CC 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}.
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DR EMBL; AJ516025; CAD56806.1; -; mRNA.
DR EMBL; FJ184989; ACI16115.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84PN8; -.
DR SMR; Q84PN8; -.
DR STRING; 4565.Traes_6AS_1A94E971B.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PRIDE; Q84PN8; -.
DR EnsemblPlants; TraesCS6A02G060700.1; TraesCS6A02G060700.1; TraesCS6A02G060700.
DR Gramene; TraesCS6A02G060700.1; TraesCS6A02G060700.1; TraesCS6A02G060700.
DR KEGG; ag:CAD56806; -.
DR eggNOG; KOG0228; Eukaryota.
DR OMA; EWVKSPY; -.
DR BRENDA; 3.2.1.153; 6500.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q84PN8; baseline and differential.
DR GO; GO:0033948; F:fructan beta-(2,1)-fructosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IDA:CACAO.
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..597
FT /note="Fructan 1-exohydrolase w1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395552"
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; 66645 MW; 7C2DDDC7CBE02CB1 CRC64;
MAQAWAFLLP VLVFGSYVTS LFFPSYISGP LCGGDGGGRS LFLCAQAPKD QDPSPAVSTM
YKTAFHFQPA KNWMNDPSGP MYFNGFYHEF YQYNLNGPIF 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 WLADNGKQLL QWPVEEIESL RTNEISHQGI ELNKGDLFEI KEVDAFQADV
EIGFELASID DADPFDPSWL LDPEKHCGEA GASVPGGIGP FGLVILASDN MDEHTEVYFR
VYKSQEKYMV LMCSDLRRSS LRPDLEKPAY GGFFEFDLEK ERKISLRTLI DRSAVESFGG
GGRVCITSRV YPAVLADVGR AHIYAFNNGS ATVRVPQLSA WTMRKAQVNV EKGWSAI
