INV1_PEA
ID INV1_PEA Reviewed; 555 AA.
AC Q43089;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Beta-fructofuranosidase, cell wall isozyme;
DE EC=3.2.1.26;
DE AltName: Full=Acid invertase;
DE AltName: Full=Sucrose hydrolase;
DE Flags: Precursor;
GN Name=BFRUCT1;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Little Marvel;
RA Zhang L., Cohn N.S., Mitchell J.P.;
RT "A cDNA clone encoding a cell Wall invertase from pea.";
RL (er) Plant Gene Register PGR96-008(1996).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; X85327; CAA59677.1; -; mRNA.
DR PIR; T06491; T06491.
DR AlphaFoldDB; Q43089; -.
DR SMR; Q43089; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..555
FT /note="Beta-fructofuranosidase, cell wall isozyme"
FT /id="PRO_0000033385"
FT ACT_SITE 61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT ACT_SITE 140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 58..61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120..121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 435..481
FT /evidence="ECO:0000250"
SQ SEQUENCE 555 AA; 62655 MW; 7B548E251CFD5D44 CRC64;
MAISSIFLLS LFSLIYVIPI EATHHVYQTL ETLSSHHSSK SNHQPYRTAY HFQPLKNWIN
DPNGPMRYGG FYHLFYQYNP KGAVWGNIVW AHSVSKDLVN WTPLDHAIHP SQPSDIKGCW
SGSATILPGG KPAILYTGID PNNHQVQNIA IPKNMSDPLL REWKKSPKNP LMEPTIANKI
NSSSFRDPTT SWLGKDGFWR VLIGSKIDTK GMAILYKSKN FVDWVEAKHP LHSAEGTGMW
ECPDFYPVLD KNLLRTGVDT SRNGDDDVRH VLKVSLDDTK HDHYLIGSYD VVKDVFVPEN
GFEDNGFVLR YDYGKYYASK TFFDDGKNRR ILLGWVNESS SVADDVKKGW SGIHTIPREI
WLHESGKQLV QWPVKEIENL RMNPVNWPTK VIKGGERISI TGVDSVQADV EISFEISDLG
KVESLRKWID PQLLCSQKGA GVKGGVGPFG LLVFASQGLK EYTAVFFRIF KYQDKNLVLM
CSDQSRSSLN KDNDMTSYGT FVDVDPLHEK LSLRTLIDHS VVESFGGEGR ACVTARVYPT
LAIHDKAMLK LTSEY