ID A0A061G109_THECC Unreviewed; 445 AA.
AC A0A061G109;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=beta-fructofuranosidase {ECO:0000256|ARBA:ARBA00012758};
DE EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758};
GN ORFNames=TCM_014931 {ECO:0000313|EMBL:EOY22897.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY22897.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY22897.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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}.
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DR EMBL; CM001881; EOY22897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061G109; -.
DR EnsemblPlants; EOY22897; EOY22897; TCM_014931.
DR Gramene; EOY22897; EOY22897; TCM_014931.
DR HOGENOM; CLU_001528_6_2_1; -.
DR Proteomes; UP000026915; Chromosome 3.
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; IPR001362; Glyco_hydro_32.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR31953:SF84; ACID BETA-FRUCTOFURANOSIDASE; 1.
DR PANTHER; PTHR31953; BETA-FRUCTOFURANOSIDASE, INSOLUBLE ISOENZYME CWINV1-RELATED; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EOY22897.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 12..49
FT /note="Beta-fructofuranosidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11837"
FT DOMAIN 58..377
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 49746 MW; 52C886F78BA637ED CRC64;
MPNRVPSASP TSKPASFSEA EPRGVAEGVS AKSNPSLLNE ASFNWTNAMF SWQRSAYHFQ
PQKNWMNDPD GPLYHKGWYH LFYQYNPDSA IWGNITWGHA VSRDLIHWLY LPLAMVPDCW
YDINGVWTGS ATLLPDGQIV MLYTGSTNES AQVQNLAYPA NLSDPLLLDW LKYPGNPVIV
PPAGIETDEF RDPTTAWLGP DGTWRITIGS RFNETIGISL VYQTTNFTDY ELLDGVLHAV
PGTGMWECVD FYPVAINGSV GLDTSAFGPG IKHVLKASLD DTKVDHYALG TYDPVTDKWT
PDNPEEDVGI GLKVDYGRYY ASKTFFDQDK QRRILWGWIN ETDTETADLK KGWASLQTIP
RSVLYDNKTG THLLQWPVKE VESLRLNSTV FEEVLVEAGS IVPLDIGPAT QVLSSRLALC
LPKLTMSSNK CMEARFQCLT MKTTI
//
