INVA_VICFA
ID INVA_VICFA Reviewed; 642 AA.
AC Q43857;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
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;
GN Name=VCINV;
OS Vicia faba (Broad bean) (Faba vulgaris).
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; Vicia.
OX NCBI_TaxID=3906;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Fribo; TISSUE=Seed;
RX PubMed=8535137; DOI=10.2307/3870191;
RA Weber H., Borisjuk L., Heim U., Buchner P., Wobus U.;
RT "Seed coat-associated invertases of fava bean control both unloading and
RT storage functions: cloning of cDNAs and cell type-specific expression.";
RL Plant Cell 7:1835-1846(1995).
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.
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 {ECO:0000305}. 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}.
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DR EMBL; Z49831; CAA89992.1; -; mRNA.
DR PIR; S55521; S55521.
DR AlphaFoldDB; Q43857; -.
DR SMR; Q43857; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
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..95
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P80065"
FT /id="PRO_0000033391"
FT CHAIN 96..642
FT /note="Acid beta-fructofuranosidase"
FT /id="PRO_0000033392"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..642
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ACT_SITE 122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 119..122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 181..182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 245..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 490..538
FT /evidence="ECO:0000250|UniProtKB:Q43866"
SQ SEQUENCE 642 AA; 72029 MW; 099466BFD288D972 CRC64;
MRNDSPYTPL LNASHNNHRR RELLLLFSGL LLLASIIAFS AYIAQPHADA DVSSSSSILS
DEATRPTTLS RGVSSGVSEK SNTFLLSGNL VGEGGSFPWN NTMLSWQRTA FHFQPEKNWM
NDPNGPLYYK GWYHFFYQYN PNGAVWGDIV WGHAVSRDLI HWLHLPLAMV ADQWYDSNGV
WTGSATILPD GQVIMLYTGS TNEFVQVQNL AYPADLNDPL LVDWIKYPSN PVLVPPPGIL
PKDFRDPTTA WLTTEGKWRI TIGSKINKTG VALVYDTVDF KTYERKDMLL NAVPGTGMWE
CVDFFPVSMK SENGLDTSFT GDEVKHVMKV SLDDDRHDYY ALGTYDEKKV KFIADDFEND
VGIGLRYDYG IFYASKTFYD QKKDRRVLWG WIGESDSEYA DVAKGWASVQ SIPRIVKLDK
KTGSNLLQWP VAEVESLRLR SDEFQNLKVK PGAVVSVDIE TATQLDIVAE FEIDKEALEK
TAQSNVEYEC NTSGGASRRG ALGPFGLYVL ADNGLSEYTP VYFYVVKGIN GKLHTSFCSD
QSRSSLANDV HKQIYGSVVP VLEGEKLSLR ILVDHSIVES FAQGGRTCIT SRVYPTRAIY
GAARLFLFNN AIETNVTASL KVWQMNSAFI RPYHPDQKRQ TS
