ID A0A161ZVB3_DAUCS Unreviewed; 606 AA.
AC A0A161ZVB3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=DCAR_020663 {ECO:0000313|EMBL:KZM91972.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM91972.1};
RN [1] {ECO:0000313|EMBL:KZM91972.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM91972.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM91972.1}.
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DR EMBL; LNRQ01000006; KZM91972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161ZVB3; -.
DR STRING; 79200.A0A161ZVB3; -.
DR EnsemblPlants; KZM91972; KZM91972; DCAR_020663.
DR Gramene; KZM91972; KZM91972; DCAR_020663.
DR OMA; INARTRD; -.
DR Proteomes; UP000077755; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR30620:SF91; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 2.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..606
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007830725"
FT DOMAIN 49..287
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 288..360
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 397..604
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
SQ SEQUENCE 606 AA; 65867 MW; 9661AE81FBBABCE5 CRC64;
MARNSAIYIG LLVIACCSNV MGLPGYVKYK DSKLPISVRI EDLMSRMSLE EKIGQMTQIE
RTLASTEVMN KYFIGSVLSE GGSVPGVRAS AEAWVNMVNE IQKGALSTPL AIPMIYGIDA
VHGHNTAFGA TIFPHNIGLG ATRQVVLWDP ELVKNIGAAT ALEVRATGIS YAFAPCIAVC
RDPRWGRCYE SYSEDTNLVR AMTEIIPGLQ GDIPAYSQKG FPFVSGKNKI ASCAKHFVGD
GGTNKGINEN NTLISENGLL RIHMAPYFDA VKKGVATIMI SYSSWNGGFV ISDYQGIDRI
TTPSHANYTF SIESGINAGI DMIMVPKAYE EFIDGLSSLV RNKFVPMTRI NDAVERILRV
KFVMGLFEDP WADLSMAKYL GSKEHKELAR EAVRKSLVLL KNGKSADQPL LPLPKKVPKI
LVVGKHANNI GYQCGGWTID WQGQDGNITV GTTILNAIES TVDKKTEVVY QENPEADLFK
ANTFSYAIVV VGEAPYAETF GDSLNLTIPE PGPSIISNVC GSVKCIVVLF TGRPVVIQPY
LANIDALVAA WLPGTEGQGI ADVLFGDYGF TGKLPQTWFK TVDQLPMNVG DSHYDPLFPF
GFGLAT
//