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Database: UniProt
Entry: A0A0L9TQ51_PHAAN
LinkDB: A0A0L9TQ51_PHAAN
Original site: A0A0L9TQ51_PHAAN 
ID   A0A0L9TQ51_PHAAN        Unreviewed;       646 AA.
AC   A0A0L9TQ51;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=beta-fructofuranosidase {ECO:0000256|ARBA:ARBA00012758};
DE            EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758};
GN   ORFNames=LR48_Vigan01g216200 {ECO:0000313|EMBL:KOM32606.1};
OS   Phaseolus angularis (Azuki bean) (Vigna angularis).
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; Vigna.
OX   NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM32606.1, ECO:0000313|Proteomes:UP000053144};
RN   [1] {ECO:0000313|Proteomes:UP000053144}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX   PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA   Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA   Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA   Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA   Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT   "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT   high starch and low fat accumulation and domestication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
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; CM003371; KOM32606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L9TQ51; -.
DR   STRING; 3914.A0A0L9TQ51; -.
DR   EnsemblPlants; KOM32606; KOM32606; LR48_Vigan01g216200.
DR   Gramene; KOM32606; KOM32606; LR48_Vigan01g216200.
DR   OMA; TTFFCQD; -.
DR   Proteomes; UP000053144; Chromosome 1.
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; 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.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000053144};
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        24..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..112
FT                   /note="Beta-fructofuranosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11837"
FT   DOMAIN          120..435
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          438..629
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
FT   REGION          50..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  71863 MW;  A5AC69523D5A1D90 CRC64;
     MEHHKPLLPT SSHAAPTPTT RKDLLFIVCG LLFLSSLVAY GGYRASGVPH THVSSPTSNH
     QQDHQSPTSL LSSQWYPVSR GVSSGVSEKS SNLLFASEGG ASEAFPWDNS MLSWQRTSFH
     FQPEKNWMNG PMYYKGWYHF FYQYNPNGAV WGDIVWGHAV SRDMIHWLHL PLAMVADQWY
     DKQGVWTGSA TILPNGEIIM LYTGSTNESV QVQNLAYPAD PSDPLLLDWI KHTGNPVLVP
     PPGIGAKDFR DPTTAWLTSE GKWRITIGSK LNKTGIALVY DTEDFKTFEL KEGLLRAVPG
     TGMWECVDFF PVSKKNGNGL DTSVNGAEVK HVMKVSLDDD RHDYYAIGTY DDNKVLFTPD
     DVKNDVGVGL RYDYGIFYAS KTFFDQNKNR RILWGWIGES DSEYADVTKG WASVQSIPRT
     VRLDTKTGSN LLQWPVAEVE SLRLRSDEFK SLKAKPGSVV SLDIETATQL DVVAEFEIDT
     ESLQKTAESN EEFTCSSSGG AAQRGALGPF GLLVLADEGL SEYTPVYFYV IKGRNGNLRT
     SFCSDQSRSS QANDVRKQIF GSVVPVLKGE KFSIRMLVDH SIVESFAQGG RTCVTSRVYP
     TKAIYGAARL FLFNNATEAT VTASLKVWQM NSAFIRPFPF KPDQKS
//
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