INV5_ARATH
ID INV5_ARATH Reviewed; 572 AA.
AC Q9LIB9; F4JEI9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Beta-fructofuranosidase, insoluble isoenzyme CWINV5;
DE EC=3.2.1.26;
DE AltName: Full=Cell wall beta-fructosidase 5;
DE AltName: Full=Cell wall invertase 5;
DE Short=AtcwINV5;
DE AltName: Full=Sucrose hydrolase 5;
DE Flags: Precursor;
GN Name=CWINV5; OrderedLocusNames=At3g13784; ORFNames=MMM17.25;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12508063; DOI=10.1093/jxb/erg055;
RA Sherson S.M., Alford H.L., Forbes S.M., Wallace G., Smith S.M.;
RT "Roles of cell-wall invertases and monosaccharide transporters in the
RT growth and development of Arabidopsis.";
RL J. Exp. Bot. 54:525-531(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16339783; DOI=10.1093/jxb/erj039;
RA Quilliam R.S., Swarbrick P.J., Scholes J.D., Rolfe S.A.;
RT "Imaging photosynthesis in wounded leaves of Arabidopsis thaliana.";
RL J. Exp. Bot. 57:55-69(2006).
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, extracellular space, apoplast
CC {ECO:0000305}. Secreted, cell wall {ECO:0000305}. Note=Associated to
CC the cell wall. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, and, to a lower extent, in
CC leaves. {ECO:0000269|PubMed:12508063, ECO:0000269|PubMed:16339783}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE75413.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP001307; BAB01929.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75413.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; ANM63953.1; -; Genomic_DNA.
DR RefSeq; NP_001326013.1; NM_001338076.1.
DR RefSeq; NP_187994.1; NM_112231.2.
DR AlphaFoldDB; Q9LIB9; -.
DR SMR; Q9LIB9; -.
DR STRING; 3702.AT3G13784.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PaxDb; Q9LIB9; -.
DR PRIDE; Q9LIB9; -.
DR ProteomicsDB; 247178; -.
DR EnsemblPlants; AT3G13784.2; AT3G13784.2; AT3G13784.
DR GeneID; 820590; -.
DR Gramene; AT3G13784.2; AT3G13784.2; AT3G13784.
DR KEGG; ath:AT3G13784; -.
DR Araport; AT3G13784; -.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_6_0_1; -.
DR InParanoid; Q9LIB9; -.
DR PhylomeDB; Q9LIB9; -.
DR PRO; PR:Q9LIB9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIB9; baseline and differential.
DR Genevisible; Q9LIB9; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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 Apoplast; Cell wall; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..572
FT /note="Beta-fructofuranosidase, insoluble isoenzyme CWINV5"
FT /id="PRO_0000348351"
FT ACT_SITE 57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 54..57
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118..119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 434..481
FT /evidence="ECO:0000250"
SQ SEQUENCE 572 AA; 64603 MW; 9538338DBD0DAC70 CRC64;
MANIVWCNIA MFLLVSLFLT DDAVVVLDAL DNVPNNIKNQ PYRTGYHFQP PKNWMNDPNG
PMIYKGIYHL FYQWNQNGAV MDVNKTVWGH ATSTDLINWI TLSPAIRPSR PSDINGCWSG
SVTILPNGKP VILYTGNDRY NRQVQNLVKP KNLTDPYLRH WTKSPENPLV TPSPVNHINS
SAFRDPTTAW FGRDGRWRIT TGSQEGRRGL AILHTSKDFV IWKQSPKPLH YHDGTGMWEC
PDFFPVARTD SRGLDTSFSS GPMVKHVLKV SLTDTFNDYY TIGTYDEVRD VYVPDKGFVQ
DETAPRYDYG KFYASKTFYD SVNQRRILWG WVNESSPEKD NIKKGWAGLQ AIPRKVWLDE
SGKRLVQWPV KEIERLRTTQ VKWGNKLLKG GSVMEVHGVT APQADVEVFF KVSGFDLEKA
DVIEPGWTDP QLICSQRNAS SGLGPFGLMV LASKNMEEYT SVNIRIFRAG ENSKEHVVVM
CSDQSTSSLE KGNDKTTYGA FLDISPYQPI SLRTLIDKSI VESFGGKGKT CITSRVYPKL
AIGERTHLFA FNKGSQNVNV LSLSAWSMKS SL
