HGL1B_WHEAT
ID HGL1B_WHEAT Reviewed; 569 AA.
AC Q1XH05;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1b, chloroplastic;
DE EC=3.2.1.182;
DE AltName: Full=Beta-glucosidase 1b;
DE Short=Taglu1b;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=GLU1B;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, SUBUNIT, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 50-569 IN COMPLEX
RP WITH DIMBOA, AND DISULFIDE BOND.
RC STRAIN=cv. Chinese Spring; TISSUE=Shoot;
RX PubMed=16751439; DOI=10.1104/pp.106.077693;
RA Sue M., Yamazaki K., Yajima S., Nomura T., Matsukawa T., Iwamura H.,
RA Miyamoto T.;
RT "Molecular and structural characterization of hexameric beta-D-glucosidases
RT in wheat and rye.";
RL Plant Physiol. 141:1237-1247(2006).
RN [2]
RP PROTEIN SEQUENCE OF 51-62, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (1.80
RP ANGSTROMS) OF 50-569.
RC STRAIN=cv. Asakazekomugi;
RX PubMed=10750901; DOI=10.1007/s004250050029;
RA Sue M., Ishihara A., Iwamura H.;
RT "Purification and characterization of a hydroxamic acid glucoside beta-
RT glucosidase from wheat (Triticum aestivum L.) seedlings.";
RL Planta 210:432-438(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 50-569 IN COMPLEX WITH DIMBOA OR
RP INHIBITOR.
RX PubMed=21421370; DOI=10.1016/j.plantsci.2010.09.001;
RA Sue M., Nakamura C., Miyamoto T., Yajima S.;
RT "Active-site architecture of benzoxazinone-glucoside beta-D-glucosidases in
RT Triticeae.";
RL Plant Sci. 180:268-275(2011).
CC -!- FUNCTION: Acts in defense of young plant parts against pests via the
CC production of hydroxamic acids from hydroxamic acid glucosides.
CC Enzymatic activity is highly correlated with plant growth. The
CC preferred substrate is DIMBOA-beta-D-glucoside.
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:16751439}.
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 -!- 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 -!- 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.34 mM for DIBOA-beta-D-glucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901};
CC KM=1.44 mM for DIBOA-beta-D-glucoside (with recombinant enzyme)
CC {ECO:0000269|PubMed:10750901};
CC KM=0.272 mM for DIMBOA-beta-D-glucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901};
CC KM=0.29 mM for DIMBOA-beta-D-glucoside (with recombinant enzyme)
CC {ECO:0000269|PubMed:10750901};
CC KM=2.02 mM for HBOA-beta-D-glucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901};
CC KM=0.320 mM for HMBOA-beta-D-glucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901};
CC KM=1.7 mM for p-nitrophenyl beta-D-glucopyranoside (with native
CC hexamer) {ECO:0000269|PubMed:10750901};
CC KM=2.16 mM for p-nitrophenyl beta-D-glucopyranoside (with recombinant
CC enzyme) {ECO:0000269|PubMed:10750901};
CC KM=1.78 mM for p-nitrophenyl beta-D-galactopyranoside (with native
CC hexamer) {ECO:0000269|PubMed:10750901};
CC KM=3.11 mM for p-nitrophenyl beta-D-xyloside (with native hexamer)
CC {ECO:0000269|PubMed:10750901};
CC KM=0.67 mM for p-nitrophenyl beta-D-fucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901};
CC KM=0.240 mM for esculin (with native hexamer)
CC {ECO:0000269|PubMed:10750901};
CC Vmax=1060 nmol/sec/mg enzyme with DIBOA-beta-D-glucoside as substrate
CC (with native hexamer) {ECO:0000269|PubMed:10750901};
CC Vmax=4100 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as
CC substrate (with native hexamer) {ECO:0000269|PubMed:10750901};
CC Vmax=220 nmol/sec/mg enzyme with HBOA-beta-D-glucoside as substrate
CC (with native hexamer) {ECO:0000269|PubMed:10750901};
CC Vmax=540 nmol/sec/mg enzyme with HMBOA-beta-D-glucoside as substrate
CC (with native hexamer) {ECO:0000269|PubMed:10750901};
CC Vmax=520 nmol/sec/mg enzyme with p-nitrophenyl beta-D-glucopyranoside
CC as substrate (with native hexamer) {ECO:0000269|PubMed:10750901};
CC Vmax=47 nmol/sec/mg enzyme with p-nitrophenyl beta-D-
CC galactopyranoside as substrate (with native hexamer)
CC {ECO:0000269|PubMed:10750901};
CC Vmax=35 nmol/sec/mg enzyme with p-nitrophenyl beta-D-xyloside as
CC substrate (with native hexamer) {ECO:0000269|PubMed:10750901};
CC Vmax=1080 nmol/sec/mg enzyme with p-nitrophenyl beta-D-fucoside as
CC substrate (with native hexamer) {ECO:0000269|PubMed:10750901};
CC Vmax=320 nmol/sec/mg enzyme with esculin as substrate (with native
CC hexamer) {ECO:0000269|PubMed:10750901};
CC Note=kcat is 214 sec(-1) with DIBOA-beta-D-glucoside as substrate
CC (with recombinant enzyme). kcat is 1201 sec(-1) with DIMBOA-beta-D-
CC glucoside as substrate (with recombinant enzyme). kcat is 128.2 sec(-
CC 1) with p-nitrophenyl beta-D-glucopyranoside as substrate (with
CC recombinant enzyme).;
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:10750901};
CC -!- SUBUNIT: Homo- and heterohexamers. {ECO:0000269|PubMed:10750901,
CC ECO:0000269|PubMed:16751439, ECO:0000269|PubMed:21421370}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings early after
CC germination. {ECO:0000269|PubMed:10750901}.
CC -!- DEVELOPMENTAL STAGE: Peak of expression 36 to 48 hours after
CC imbibition. {ECO:0000269|PubMed:16751439}.
CC -!- MISCELLANEOUS: Wheat is a hexaploid with three different genomes that
CC contains at least four genes coding for GLU1: GLU1A (AC Q1XIR9), GLU1B
CC (AC Q1XH05), GLU1C (AC Q1XH04) and GLU1D (AC D5MTF8). The monomers can
CC aggregate in diverse combinations, reflecting the several isozymes
CC found in the native enzyme described in PubMed:10750901. The hexameric
CC structure is required for activity toward DIMBOA-beta-D-glucoside
CC (PubMed:16751439). {ECO:0000305|PubMed:16751439}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AB236422; BAE92259.1; -; mRNA.
DR PDB; 2DGA; X-ray; 1.80 A; A=50-569.
DR PDB; 3AIQ; X-ray; 1.90 A; A=50-569.
DR PDB; 3AIR; X-ray; 2.00 A; A=50-569.
DR PDB; 3AIS; X-ray; 2.20 A; A=50-569.
DR PDBsum; 2DGA; -.
DR PDBsum; 3AIQ; -.
DR PDBsum; 3AIR; -.
DR PDBsum; 3AIS; -.
DR AlphaFoldDB; Q1XH05; -.
DR SMR; Q1XH05; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PRIDE; Q1XH05; -.
DR EnsemblPlants; TraesCS2B02G599800.1; TraesCS2B02G599800.1; TraesCS2B02G599800.
DR Gramene; TraesCS2B02G599800.1; TraesCS2B02G599800.1; TraesCS2B02G599800.
DR OMA; KEGHIGM; -.
DR BRENDA; 3.2.1.182; 6500.
DR BRENDA; 3.2.1.21; 6500.
DR SABIO-RK; Q1XH05; -.
DR EvolutionaryTrace; Q1XH05; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q1XH05; 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 3D-structure; Chloroplast; Direct protein sequencing; Disulfide bond;
KW Glycosidase; Hydrolase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10750901"
FT CHAIN 51..569
FT /note="4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-
FT benzoxazin-2-yl glucoside beta-D-glucosidase 1b,
FT chloroplastic"
FT /id="PRO_0000424098"
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 456
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT BINDING 92
FT /ligand="substrate"
FT BINDING 239
FT /ligand="substrate"
FT BINDING 243
FT /ligand="substrate"
FT BINDING 504
FT /ligand="substrate"
FT BINDING 511..512
FT /ligand="substrate"
FT DISULFID 259..265
FT /evidence="ECO:0000269|PubMed:16751439"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3AIQ"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2DGA"
FT TURN 124..128
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 130..144
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 213..228
FT /evidence="ECO:0007829|PDB:2DGA"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2DGA"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 275..297
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 305..321
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 365..371
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 376..390
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 433..445
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 475..493
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 512..517
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:2DGA"
FT TURN 527..531
FT /evidence="ECO:0007829|PDB:2DGA"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:2DGA"
FT HELIX 537..545
FT /evidence="ECO:0007829|PDB:2DGA"
SQ SEQUENCE 569 AA; 64482 MW; 44FAB6E047F86F85 CRC64;
MALLAAATLN PTTHLSLRSR AGRNSENLWL RSTASSQKSK GRFCNLTIRA GTPSKPAEPI
GPVFTKLKPW QIPKRDWFDK DFLFGASTSA YQIEGAWNED GKGPSTWDHF CHTYPERISD
MTNGDVAANS YHLYEEDVKA LKDMGMKVYR FSISWSRILP DGTGKVNQAG IDYYNKLINS
LIDNDIVPYV TIWHWDTPQA LEDKYGGFLN RQIVDDYKQF AEVCFKNFGD RVKNWFTFNE
PHTYCCFSYG EGIHAPGRCS PGMDCAVPEG DSLREPYTAG HHILLAHAEA VQLFKARYNM
HGDSKIGMAF DVMGYEPYQD SFLDDQARER SIDYNMGWFL EPVVRGDYPF SMRSLIGDRL
PMFTKEEQEK LASSCDIMGL NYYTSRFSKH VDMSPDFTPT LNTDDAYASS ETTGSDGNDI
GPITGTYWIY MYPKGLTDLL LIMKEKYGNP PVFITENGIA DVEGDESMPD PLDDWKRLDY
LQRHISAVKD AIDQGADVRG HFTWGLIDNF EWSLGYSSRF GLVYIDKNDG NKRKLKKSAK
WFSKFNSVPK PLLKTTNNNA TMTAASVSV
