ID   INV2_DAUCA              Reviewed;         592 AA.
AC   Q39692;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme 2;
DE            EC=3.2.1.26;
DE   AltName: Full=Cell wall beta-fructosidase 2;
DE   AltName: Full=Invertase 2;
DE   AltName: Full=Sucrose hydrolase 2;
DE   Flags: Precursor;
GN   Name=INV2;
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; X78424; CAA55189.1; -; Genomic_DNA.
DR   PIR; S56681; S56681.
DR   AlphaFoldDB; Q39692; -.
DR   SMR; Q39692; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   PRIDE; Q39692; -.
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..40
FT                   /evidence="ECO:0000255"
FT   PROPEP          41..?
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033368"
FT   CHAIN           ?..592
FT                   /note="Beta-fructofuranosidase, insoluble isoenzyme 2"
FT                   /id="PRO_0000033369"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        568
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   592 AA;  67398 MW;  2734603836709133 CRC64;
     MLIRCFHIKM ALVTCFHSML FLSAVVFIFS LDVNIRGVEA SHQVFPELQS VSAVNVQLVH
     RTGYHFQPKK HWINDPNGPM YYKGFYHLFY QYNPKGAVWG NIVWAHSISK DLINWVALEP
     AIFPSKPFDK YGCWSGSATV LPGGKPVIMY TGIVTPSPVN TQVQNFAVPA NYSDPYLREW
     IKPDNNPIVR ARSENSSSFR DPTTAWFDGV HWKILVGSRR KHRGIAYLYR SRNFLKWTKA
     KHPLHSKDRT GMWECLDFYP VAPKGMNGLD TSVTGQDIKH VLKVSLYSTR YEYYTVGEYD
     RDNDIYVPDN TSVDGWAGLR YDYGNFYASK TFFDPDKQRR ILWGWANESD SKQDDVQKGW
     AGIQLIPRKL WLDPNGKQLI QWPIEEIQLL RGQNVHMGSQ VLNTGEHIEV KGVTAAQADV
     DATFSFKSLD RAEWFDPNWA KLDALDVCDW MGSTVRGGLG PFGFLTLASE KLEEYTPVFF
     RVFKTKDKLK VLMCSDAKRS STTAEGLYKP PFAGYVDVDL SDKKISLRSL IDNSVVESFG
     AHGRTCITSR VYPKIAIYNN AHVFVFNNGT EAITIDSLDA WSMKAPSLMN NN