BAGBG_DALNI
ID BAGBG_DALNI Reviewed; 547 AA.
AC A3RF67;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Isoflavonoid 7-O-beta-apiosyl-glucoside beta-glycosidase {ECO:0000303|PubMed:16098548};
DE EC=3.2.1.161;
DE AltName: Full=Beta-glycosidase {ECO:0000312|EMBL:ABN70849.1};
DE Flags: Precursor;
OS Dalbergia nigrescens (Thai blackwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Dalbergia clade; Dalbergia.
OX NCBI_TaxID=298683;
RN [1] {ECO:0000312|EMBL:ABN70849.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seed;
RA Chuankhayan P., Svasti J., Sullivan P.A., Ketudat-Cairns J.R.;
RT "Functional and structural differences between isoflavonoid beta-
RT glycosidase from Dalbergia sp.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 32-37; 106-113; 127-137; 142-151 AND 199-223, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC TISSUE=Seed {ECO:0000269|PubMed:16098548};
RX PubMed=16098548; DOI=10.1016/j.phytochem.2005.06.024;
RA Chuankhayan P., Hua Y., Svasti J., Sakdarat S., Sullivan P.A.,
RA Ketudat Cairns J.R.;
RT "Purification of an isoflavonoid 7-O-beta-apiosyl-glucoside beta-
RT glycosidase and its substrates from Dalbergia nigrescens Kurz.";
RL Phytochemistry 66:1880-1889(2005).
CC -!- FUNCTION: Hydrolyzes dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-
CC glucopyranoside and dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-
CC glucopyranoside. Also has activity towards pNP-beta-D-fucoside and pNP-
CC beta-D-glucoside, but not pNP-beta-cellobioside.
CC {ECO:0000269|PubMed:16098548}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-[beta-D-apiofuranosyl-(1->6)-beta-D-
CC glucopyranosyloxy]isoflavonoid + H2O = a 7-hydroxyisoflavonoid +
CC beta-D-apiofuranosyl-(1->6)-D-glucose.; EC=3.2.1.161;
CC Evidence={ECO:0000269|PubMed:16098548};
CC -!- ACTIVITY REGULATION: Not inhibited by iron, calcium, mercury,
CC manganese, zinc or EDTA. {ECO:0000269|PubMed:16098548}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.7 mM for pNP-beta-D-glucoside {ECO:0000269|PubMed:16098548};
CC KM=1.8 mM for pNP-beta-D-fucoside {ECO:0000269|PubMed:16098548};
CC KM=0.5 mM for dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-
CC glucopyranoside {ECO:0000269|PubMed:16098548};
CC KM=0.7 mM for dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-
CC glucopyranoside {ECO:0000269|PubMed:16098548};
CC KM=0.11 mM for daidzin {ECO:0000269|PubMed:16098548};
CC KM=0.09 mM for genistin {ECO:0000269|PubMed:16098548};
CC pH dependence:
CC Optimum pH is 5.0-6.0. Half maximum activity is seen at pH 3.5 and
CC 6.5. {ECO:0000269|PubMed:16098548};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:16098548};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16098548}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000255}.
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DR EMBL; EF392846; ABN70849.1; -; mRNA.
DR AlphaFoldDB; A3RF67; -.
DR SMR; A3RF67; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PRIDE; A3RF67; -.
DR BioCyc; MetaCyc:MON-13779; -.
DR BRENDA; 3.2.1.161; 8018.
DR SABIO-RK; A3RF67; -.
DR GO; GO:0033956; F:beta-apiosyl-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:16098548"
FT CHAIN 32..547
FT /note="Isoflavonoid 7-O-beta-apiosyl-glucoside beta-
FT glycosidase"
FT /evidence="ECO:0000269|PubMed:16098548"
FT /id="PRO_0000398615"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P26205"
FT ACT_SITE 419
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P26205"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT BINDING 475..476
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q75I93"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 224..232
FT /evidence="ECO:0000250|UniProtKB:P26205"
FT CONFLICT 146
FT /note="L -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="D -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 61859 MW; 03F4AAA6D54EB8F5 CRC64;
MHAMTFKAIL LLGLLALVST SASIAFAKEV RATITEVPPF NRNSFPSDFI FGTAASSYQY
EGEGRVPSIW DNFTHQYPEK IADGSNGDVA VDQFHHYKED VAIMKYMNLD AYRLSISWPR
ILPTGRASGG INSTGVDYYN RLINELLAND ITPFVTIFHW DLPQALEDEY GGFLNHTIVN
DFRDYADLCF NLFGDRVKHW ITVNEPSIFT MNGYAYGIFA PGRCSPSYNP TCTGGDAGTE
PDLVAHNLIL SHAATVQVYK KKYQEHQNGI IGISLQIIWA VPLSNSTSDQ KAAQRYLDFT
GGWFLDPLTA GQYPESMQYL VGDRLPKFTT DEAKLVKGSF DFVGINYYTS SYLTSSDAST
CCPPSYLTDS QVTFSSQRNG VFIGPVTPSG WMCIYPKGLR DLLLYIKEKY NNPLVYITEN
GMDELDDPSQ SLEESLIDTY RIDSYYRHLF YVRSAIGSGA NVKGFFAWSL LDNFEWNEGF
TSRFGLNFVN YTTLTRYHKL SATWFKYFLA RDQEIAKLDI SAPKARWSSS TMIKEEKRKP
KWAIQAF
