1FEH3_WHEAT
ID 1FEH3_WHEAT Reviewed; 596 AA.
AC B6DZC8; Q70LR2;
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 w3 {ECO:0000312|EMBL:ACI16116.1};
DE EC=3.2.1.153;
DE Flags: Precursor;
GN Name=1-FEHw3 {ECO:0000303|PubMed:18346083, ECO:0000303|Ref.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:0000312|EMBL:ACI16116.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chinese Spring {ECO:0000269|Ref.1};
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).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAD92365.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Pajero {ECO:0000269|PubMed:18346083};
RC TISSUE=Stem {ECO:0000269|PubMed:18346083};
RX PubMed=18346083; DOI=10.1111/j.1399-3054.2008.01070.x;
RA Van Riet L., Altenbach D., Vergauwen R., Clerens S., Kawakami A.,
RA Yoshida M., Van den Ende W., Wiemken A., Van Laere A.;
RT "Purification, cloning and functional differences of a third fructan 1-
RT exohydrolase (1-FEHw3) from wheat (Triticum aestivum).";
RL Physiol. Plantarum 133:242-253(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:0000250|UniProtKB:Q84PN8,
CC ECO:0000269|PubMed:18346083}.
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:18346083};
CC -!- ACTIVITY REGULATION: Inhibited by sucrose.
CC {ECO:0000269|PubMed:18346083}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5-6. {ECO:0000269|PubMed:18346083};
CC Temperature dependence:
CC Optimum temperature is 25-40 degrees Celsius.
CC {ECO:0000269|PubMed:18346083};
CC -!- TISSUE SPECIFICITY: Expressed in the stem, particularly the penultimate
CC internode. Little expression is detected in roots and in the peduncle
CC part of the stem. {ECO:0000269|PubMed:18346083}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000255}.
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DR EMBL; FJ184990; ACI16116.1; -; Genomic_DNA.
DR EMBL; AJ564996; CAD92365.1; -; mRNA.
DR AlphaFoldDB; B6DZC8; -.
DR SMR; B6DZC8; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PRIDE; B6DZC8; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; B6DZC8; 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 w3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395553"
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 DISULFID 446..492
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CONFLICT 113
FT /note="A -> V (in Ref. 2; CAD92365)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="P -> S (in Ref. 2; CAD92365)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="G -> S (in Ref. 2; CAD92365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 66296 MW; 0D635F0F06EA4CF2 CRC64;
MAQAWAFLLP VLVLGSYVTS LFLPTYITGP LCGGDGGGRS LFLCAQAPKD QDPSPASTMY
KTAFHFQPAK NWMNDPSGPM YFNGIYHEFY QYNLNGPIFG DIVWGHSVST DLANWIGLEP
ALVRDTPSDI DGCWTGSVTI LPGGKPIIIY TGGDIDQNQA QNIAFPKNRS DPYLREWIKA
DNNPVLRPDE PGMNSIEFRD PTTGWIGPDG LWRMAVGGEL NGYSAALLYK SEDFLNWTKV
DHPLYSHNGS NMWECPDFFA VLPGNNAGLD LSAAIPQGAK HALKMSVDSV DKYMIGVYDL
HRDAFVPDNV VDDRRLWLRI DYGTFYASKS FFDPNKNRRI IWGWSRETDS PSDDLAKGWA
GLHTIPRTIW LAGDGKQLLQ WPVEEIESLR TNEINHQGLE LNKGDLFEIK EVDAFQADVE
IGFELASIDD ADPFDPSWLL DPEKHCGEAG ASVPGGIGPF GLVILASDNM DEHTEVYFRV
YKSQEKYMVL MCSDLRRSSL RPDLEKPAYG GFFEFDLEKE RKISLRTLID RSAVESFGGG
GRVCITSRVY PAVLADVGSA HIYAFNNGGA TVRVPQLSAW TMRKAQVNVE KGWSAI
