HGGL2_MAIZE
ID HGGL2_MAIZE Reviewed; 563 AA.
AC Q41761;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 2, chloroplastic;
DE EC=3.2.1.182;
DE AltName: Full=Beta-glucosidase 2;
DE Short=ZmGlu2;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=GLU2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73;
RA Bandaranayake H., Esen A.;
RT "Nucleotide Sequence of a Beta-Glucosidase (glu2) cDNA from maize
RT (Accession No. U44087) (PGR96-009).";
RL Plant Physiol. 110:1048-1048(1996).
RN [2]
RP TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBSTRATE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10099619;
RX DOI=10.1002/(sici)1097-0290(19990520)63:4<392::aid-bit2>3.0.co;2-m;
RA Cicek M., Esen A.;
RT "Expression of soluble and catalytically active plant (monocot) beta-
RT glucosidases in E. coli.";
RL Biotechnol. Bioeng. 63:392-400(1999).
CC -!- FUNCTION: Beta-glucosidase acting poorly on artificial aryl beta-
CC glucosides. Has no activity toward the chromogenic substrate 6-bromo-2-
CC naphthyl-beta-D-glucoside (6BNGlc). {ECO:0000269|PubMed:10099619}.
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:0000269|PubMed:10099619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DIMBOA beta-D-glucoside + H2O = D-glucose + DIMBOA;
CC Xref=Rhea:RHEA:33975, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18048, ChEBI:CHEBI:37573; EC=3.2.1.182;
CC Evidence={ECO:0000269|PubMed:10099619};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA;
CC Xref=Rhea:RHEA:33979, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:63558, ChEBI:CHEBI:63670; EC=3.2.1.182;
CC Evidence={ECO:0000269|PubMed:10099619};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.84 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG) (with
CC recombinant enzyme) {ECO:0000269|PubMed:10099619};
CC KM=1.25 mM for o-nitrophenyl beta-D-glucopyranoside (with recombinant
CC enzyme) {ECO:0000269|PubMed:10099619};
CC Vmax=52.8 umol/h/ug enzyme with p-nitrophenyl beta-D-glucopyranoside
CC as substrate (with recombinant enzyme) {ECO:0000269|PubMed:10099619};
CC Vmax=168.3 umol/h/ug enzyme with o-nitrophenyl beta-D-glucopyranoside
CC as substrate (with recombinant enzyme) {ECO:0000269|PubMed:10099619};
CC -!- SUBUNIT: Homo- and heterodimer. {ECO:0000269|PubMed:10099619}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves only starting at day 6 after
CC germination. {ECO:0000269|PubMed:10099619}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; U44087; AAD09850.1; -; mRNA.
DR PIR; T02720; T02720.
DR RefSeq; NP_001105892.1; NM_001112422.1.
DR AlphaFoldDB; Q41761; -.
DR SMR; Q41761; -.
DR STRING; 4577.GRMZM2G008247_P01; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q41761; -.
DR GeneID; 732807; -.
DR KEGG; zma:732807; -.
DR eggNOG; KOG0626; Eukaryota.
DR OrthoDB; 408001at2759; -.
DR SABIO-RK; Q41761; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q41761; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0102726; F:DIMBOA glucoside beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
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.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Disulfide bond; Glycosidase; Hydrolase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..563
FT /note="4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-
FT benzoxazin-2-yl glucoside beta-D-glucosidase 2,
FT chloroplastic"
FT /id="PRO_0000424097"
FT REGION 17..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..358
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT REGION 391..402
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT REGION 447..450
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 22..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 242
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 457
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 508
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 515..516
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 261..267
FT /evidence="ECO:0000250"
SQ SEQUENCE 563 AA; 64111 MW; D8FD8E31215E2A9E CRC64;
MAPLLAAAMN HAAHPVLRSH LGPNNESFSR HHLSSSPQSS KRRFNLSFTP RSARVGNQNG
VQLLSPSEIP RRDWFPSDFI FGAATSAYQI EGAWNEDGKG ESNWDHFCHN FPERIMDGSN
ADIGANSYHM YKTDVRLLKE MGMDAYRFSI SWPRILPKGT VEGGINQDGI DYYKRLINLL
LENGIEPYVT IFHWDVPQAL EEKYGGFLDK TQKRIVNDYK NFAKVCFDNF GDKVKNWLTF
NEPQTFTSFS YGTGVFAPGR CSPGLDCAIP TGNSLVEPYI AGHNILLAHA EAVDLYNKYY
KGENGRIGLA FDVMGRVPYG TSFLDEQAKE RSMDINLGWF LEPVVRGDYP FSMRSLARER
LPFFSDKQQE KLVGSYNMLG INYYTSIFSK HIDISPKYSP VLNTDDAYAS QETYGPDGKP
IGPPMGNPWI YLYPEGLKDI LMIMKNKYGN PPIYITENGI GDVDTKEKPL PMEAALNDYK
RLDYIQRHIS TLKESIDLGA NVHGYFAWSL LDNFEWYAGY TERYGIVYVD RKNNYTRYMK
ESAKWLKEFN TAKKPSKKII TPA
