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   27-MAR-2024, entry version 90.
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 {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:16751439};
DE   AltName: Full=Beta-glucosidase 1b;
DE            Short=Taglu1b;
DE            EC=3.2.1.21 {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:16751439};
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
RP   BETA-D-GLUCOSE.
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         Evidence={ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:16751439};
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:10750901, ECO:0000269|PubMed:16751439};
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:10750901, ECO:0000269|PubMed:16751439};
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=0.32 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=0.24 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
CC         beta-D-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
CC         DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme). kcat
CC         is 128.2 sec(-1) with p-nitrophenyl beta-D-glucopyranoside as
CC         substrate (with 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   STRING; 4565.Q1XH05; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   EnsemblPlants; TraesCS2B02G599800.1; TraesCS2B02G599800.1; TraesCS2B02G599800.
DR   EnsemblPlants; TraesCS2B03G1500200.1; TraesCS2B03G1500200.1.CDS; TraesCS2B03G1500200.
DR   Gramene; TraesCS2B02G599800.1; TraesCS2B02G599800.1; TraesCS2B02G599800.
DR   Gramene; TraesCS2B03G1500200.1; TraesCS2B03G1500200.1.CDS; TraesCS2B03G1500200.
DR   OMA; WNNYERD; -.
DR   OrthoDB; 334393at2759; -.
DR   BRENDA; 3.2.1.182; 6500.
DR   BRENDA; 3.2.1.21; 6500.
DR   SABIO-RK; Q1XH05; -.
DR   EvolutionaryTrace; Q1XH05; -.
DR   Proteomes; UP000019116; Chromosome 2B.
DR   ExpressionAtlas; Q1XH05; 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   Gene3D; 3.20.20.80; Glycosidases; 1.
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:SF326; 4-HYDROXY-7-METHOXY-3-OXO-3,4-DIHYDRO-2H-1,4-BENZOXAZIN-2-YL GLUCOSIDE BETA-D-GLUCOSIDASE 2, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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|UniProtKB:Q8L7J2"
FT   ACT_SITE        456
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   BINDING         92
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:21421370,
FT                   ECO:0007744|PDB:3AIR, ECO:0007744|PDB:3AIS"
FT   BINDING         194
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         239..240
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:21421370,
FT                   ECO:0007744|PDB:3AIR"
FT   BINDING         383
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         456
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         504
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:21421370,
FT                   ECO:0007744|PDB:3AIS"
FT   BINDING         511..512
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:21421370,
FT                   ECO:0007744|PDB:3AIR, ECO:0007744|PDB:3AIS"
FT   BINDING         520
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000305|PubMed:21421370,
FT                   ECO:0007744|PDB:3AIS"
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
//