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Database: UniProt
Entry: Q9FQ62_BRAOL
LinkDB: Q9FQ62_BRAOL
Original site: Q9FQ62_BRAOL 
ID   Q9FQ62_BRAOL            Unreviewed;       663 AA.
AC   Q9FQ62;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=beta-fructofuranosidase {ECO:0000256|ARBA:ARBA00012758};
DE            EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758};
OS   Brassica oleracea (Wild cabbage).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3712 {ECO:0000313|EMBL:AAG36942.1};
RN   [1] {ECO:0000313|EMBL:AAG36942.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Coupe S.A., Sinclair B.K., Greer L.A., Gapper N.E., Watson L.M.,
RA   Hurst P.L.;
RT   "Analysis of acid invertase gene expression during the senescence of
RT   broccoli florets.";
RL   Postharvest Biol. Technol. 28:27-37(2003).
CC   -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004914}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC       lumen {ECO:0000256|ARBA:ARBA00004410}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC       {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU362110}.
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DR   EMBL; AF274298; AAG36942.1; -; mRNA.
DR   AlphaFoldDB; Q9FQ62; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   ExpressionAtlas; Q9FQ62; baseline.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005775; C:vacuolar lumen; 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   CDD; cd18624; GH32_Fruct1-like; 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   PANTHER; PTHR31953:SF1; ACID BETA-FRUCTOFURANOSIDASE 4, VACUOLAR; 1.
DR   PANTHER; PTHR31953; BETA-FRUCTOFURANOSIDASE, INSOLUBLE ISOENZYME CWINV1-RELATED; 1.
DR   Pfam; PF08244; Glyco_hydro_32C; 1.
DR   Pfam; PF00251; Glyco_hydro_32N; 1.
DR   Pfam; PF11837; INV_N; 1.
DR   SMART; SM00640; Glyco_32; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU362110};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362110};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..116
FT                   /note="Beta-fructofuranosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11837"
FT   DOMAIN          124..444
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          447..643
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
SQ   SEQUENCE   663 AA;  73613 MW;  12DF13E01EB0696D CRC64;
     MASSDALLPI SAREEDPLLS DGSRCDPNAE THRRRRPVKG LLAVSFGLLF IAFYVVLIAT
     HDGSSRSNDV KIESDETATT TSRARLAGVS EKSNGQLWKL SGERNTVSFA WNNSVLSWQR
     TAFHFQPEQN WMNDPNGPLF YKGWYHFFYQ YNPNAAVWGD IVWGHAVSKD LIHWVHLPIA
     MVADQWYDAN GVWTGSATFL DDGSLVMLYT GSTDKSVQVQ NLAYPEDLND PLLLKWVKYS
     GNPVLVPPPG ILPKDFRDPT TAWKTSDGKW RITIGSKINK TGISLVYDTI DFKTYEKHDT
     LLHKVPNTGM WECVDFYPVS KTAVNGLDTS VNGPNVKHIV KASMDDTRFD HYAVGTYFDS
     NGTWIPDDPT IDVGMSASLR YDYGKFYASK TFYDQNKGRR ILWSWIGESD SEAADVQKGW
     SSLQGIPRTV VLDTKTGKNL VQWPVEEIKS LRLSSKQFDM EVGPGSVVPV DVDSAAQLDI
     EAEFEINKES LDKILGDASV VVEAEEFSCQ KSGGASVRGA LGPFGFSVLA DKSLSEQTPV
     YFYVAKGKDS KLKTFFCTDT SRSTFANDVV KPIYGSSVPV LKGEKLTMRI LVDHSIVEGF
     AQAGRTCISS RVYPTKAIYG AAKLFVFNNA IDATITASFK VWQMNSAFIH PYSEEAVRAL
     SST
//
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