INVA_PHAVU
ID INVA_PHAVU Reviewed; 651 AA.
AC O24509;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Acid beta-fructofuranosidase;
DE EC=3.2.1.26;
DE AltName: Full=Acid invertase;
DE Short=AI;
DE AltName: Full=Acid sucrose hydrolase;
DE AltName: Full=Vacuolar invertase;
DE Flags: Precursor;
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Blee K.A., Anderson A.J.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Glycan biosynthesis; sucrose metabolism. {ECO:0000305}.
CC -!- SUBUNIT: May be present in two forms, a 70 kDa monomer and a
CC heterodimer of the 30 kDa and 38 kDa subunits. The ratio of the levels
CC of the two forms within cells appears to be regulated developmentally
CC (By similarity). {ECO:0000250|UniProtKB:P29001}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}. Vacuole lumen
CC {ECO:0000250|UniProtKB:Q39041}. Note=May be released into the lumen of
CC the vacuole from the tonoplast through a proteolytic processing.
CC {ECO:0000250|UniProtKB:Q39041}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U92438; AAB68679.1; -; mRNA.
DR PIR; T12083; T12083.
DR AlphaFoldDB; O24509; -.
DR SMR; O24509; -.
DR STRING; 3885.XP_007155629.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR eggNOG; KOG0228; Eukaryota.
DR UniPathway; UPA00238; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR021792; Beta-fructofuranosidase_N.
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; PF11837; DUF3357; 1.
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; Membrane;
KW Signal-anchor; Transmembrane; Transmembrane helix; Vacuole; Zymogen.
FT PROPEP 1..103
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P80065"
FT /id="PRO_0000033389"
FT CHAIN 104..651
FT /note="Acid beta-fructofuranosidase"
FT /id="PRO_0000033390"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..651
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 48..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 127..130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 500..548
FT /evidence="ECO:0000250|UniProtKB:Q43866"
SQ SEQUENCE 651 AA; 72686 MW; 6303538073EFA479 CRC64;
MEHHKPLLPT SSHAAPNPRT RKDLLLLLCA LLFLSSLVAF GRNRASNVPH DHVSSSASNH
QQEHQSPTSL PSSKWHAVSR GVSSGVSEKS SSMLFSGEGG ASEAFPWDNS MLSWQRTSFH
FQPEKNWMND PNGPMYYKGW YHFFYQYNPN GAVWGDIVWG HAVSRDMIHW LHLPLAMVAD
QWYDKQGVWT GSATILPNGE IIMLYTGSTN ESVQVQNLAY PADPSDPLLV DWIKHPGNPV
LVPPPGIGAK DFRDPTTAWL TSEGKWRITI GSKLNKTGIA LVYDTDDFKT YELKNGHLRA
VPGTGMWECV DFFPVSKKNE NGLDTSLSIN GAEVKYVMKV SLDDDRHDYY TIGTYDENKV
LFTPDDVKND VGVGLRYDYG IFYASKTFYD QNMDRRILWG WIGESDSEYA DVTKGWASVQ
SIPRTVRLDK KTGSNLLQWP VAEVESLRLR SDEFKSLKAK PGSVVSLDIE TATQLDVVAE
FEIDAESLQK TAQSNEEFTC STSGGAAQRG ALGPFGLLVL ADEGLSEYTP VYFYVIKGRN
GNLKTSFCSD QSRSSQPNDV RKQIFGNIVP VLEGEKFSLR MLVDHSIVES FAQGGRTCVT
SRVYPTKAIY GAARLFLFNN ATEATVTASL KIWQMNSAFI RPFPFNPDQK N
