INV1_MAIZE
ID INV1_MAIZE Reviewed; 670 AA.
AC P49175;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Beta-fructofuranosidase 1;
DE EC=3.2.1.26;
DE AltName: Full=Invertase 1;
DE AltName: Full=Sucrose 1;
DE Flags: Precursor;
GN Name=IVR1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7630946; DOI=10.1104/pp.108.3.1293;
RA Xu J., Pemberton G.H., Almira E.C., McCarty D.R., Koch K.E.;
RT "The Ivr 1 gene for invertase in maize.";
RL Plant Physiol. 108:1293-1294(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. {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}.
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DR EMBL; U16123; AAA83439.1; -; Genomic_DNA.
DR PIR; T02092; T02092.
DR AlphaFoldDB; P49175; -.
DR SMR; P49175; -.
DR STRING; 4577.GRMZM2G394450_P01; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; P49175; -.
DR PRIDE; P49175; -.
DR MaizeGDB; 86037; -.
DR eggNOG; KOG0228; Eukaryota.
DR BRENDA; 3.2.1.26; 6752.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P49175; baseline and differential.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Vacuole; Zymogen.
FT PROPEP 1..112
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P80065"
FT /id="PRO_0000033377"
FT CHAIN 113..670
FT /note="Beta-fructofuranosidase 1"
FT /id="PRO_0000033378"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..65
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..670
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 136..139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 263..264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q43866"
FT CARBOHYD 165
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 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 519..567
FT /evidence="ECO:0000250|UniProtKB:Q43866"
SQ SEQUENCE 670 AA; 71933 MW; DEDE0989C7E6AEB0 CRC64;
MIPAVADPTT LDGGGARRPL LPETDPRGRA AAGAEQKRPP ATPTVLTAVV SAVLLLVLVA
VTVLASQHVD GQAGGVPAGE DAVVVEVAAS RGVAEGVSEK STAPLLGSGA LQDFSWTNAM
LAWQRTAFHF QPPKNWMNDP NGPLYHKGWY HLFYQWNPDS AVWGNITWGH AVSRDLLHWL
HLPLAMVPDH PYDANGVWSG SATRLPDGRI VMLYTGSTAE SSAQVQNLAE PADASDPLLR
EWVKSDANPV LVPPPGIGPT DFRDPTTACR TPAGNDTAWR VAIGSKDRDH AGLALVYRTE
DFVRYDPAPA LMHAVPGTGM WECVDFYPVA AGSGAAAGSG DGLETSAAPG PGVKHVLKAS
LDDDKHDYYA IGTYDPATDT WTPDSAEDDV GIGLRYDYGK YYASKTFYDP VLRRRVLWGW
VGETDSERAD ILKGWASVQS IPRTVLLDTK TGSNLLQWPV VEVENLRMSG KSFDGVALDR
GSVVPLDVGK ATQLDIEAVF EVDASDAAGV TEADVTFNCS TSAGAAGRGL LGPFGLLVLA
DDDLSEQTAV YFYLLKGTDG SLQTFFCQDE LRASKANDLV KRVYGSLVPV LDGENLSVRI
LVDHSIVESF AQGGRTCITS RVYPTRAIYD SARVFLFNNA THAHVKAKSV KIWQLNSAYI
RPYPATTTSL
