ID   INV3_DAUCA              Reviewed;         583 AA.
AC   Q39693;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme 3;
DE            EC=3.2.1.26;
DE   AltName: Full=Cell wall beta-fructosidase 3;
DE   AltName: Full=Invertase 3;
DE   AltName: Full=Sucrose hydrolase 3;
DE   Flags: Precursor;
GN   Name=INV3;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Queen Anne's Lace;
RX   PubMed=7787183; DOI=10.1007/bf00042049;
RA   Lorenz K., Lienhard S., Sturm A.;
RT   "Structural organization and differential expression of carrot beta-
RT   fructofuranosidase genes: identification of a gene coding for a flower bud-
RT   specific isozyme.";
RL   Plant Mol. Biol. 28:189-194(1995).
CC   -!- FUNCTION: May play an important role in phloem unloading and in stress
CC       response.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC         residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10067};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Note=Ionically bound to the
CC       cell wall.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; X78423; CAA55188.1; -; Genomic_DNA.
DR   PIR; S56680; S56680.
DR   AlphaFoldDB; Q39693; -.
DR   SMR; Q39693; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004564; F:beta-fructofuranosidase 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; IPR018053; Glyco_hydro_32_AS.
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.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE   3: Inferred from homology;
KW   Cell wall; Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal; Zymogen.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   PROPEP          34..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033370"
FT   CHAIN           ?..583
FT                   /note="Beta-fructofuranosidase, insoluble isoenzyme 3"
FT                   /id="PRO_0000033371"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        561
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   583 AA;  66381 MW;  1DBF591CD94749AF CRC64;
     MARTKILVFS SDSSLFLLSI FSFIFLNING VDSTHRVFPE LQSISAVDVK LVHRTGYHFQ
     PQKHWINDPN GPMFYKGYYH LFYQYNPKGS VWGNIVWAHS VSKDLINWIA LEPAIFPSKP
     FDQYGCWSGS ATILPGNKPV ILYTGIVSPD PENAQVQNYA VPANYSDPFL REWVKPDNNP
     LVGVHTENPS AFRDPTTAWF DGGHWKMLVG SSRKHRGIAY LYRSKDFKKW KRSPHPIHTK
     AETGMWECPD FYPVSPRSED GLDNSKMGRG IKHVLKVSLN STRYEYYTIG RYNRVRDFYV
     PDNTSVDGWA GLRYDYGNFY ASKTFYDPIK KRRILWGWAN ESDSQIDDVQ KGWAGIQLIP
     RRIWLDPSGR QLVQWPIEEV EGLRGSELHM RNQKLDMGVH VEVTGITAAQ ADVDATFSFK
     SLDKAESFDP EWINLDAQDV CDSMGSTIQG GLGPFGLLTL ASKDLEEYTP VFFRIFKAED
     QKLKVLMCSD AKRSSLAEGL YKPSFRGFVD VDLSDKKISL RSLIDNSVVE SFGAQRKNLI
     SSRVYPTLAI YNNAHLFVFN NGTEPITVDN LDAWSMNSPS EMN