ID HGL1D_WHEAT Reviewed; 564 AA.
AC D5MTF8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1d, chloroplastic;
DE EC=3.2.1.182 {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
DE AltName: Full=Beta-glucosidase 1d;
DE Short=TaGlu1d;
DE EC=3.2.1.21 {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
DE Flags: Precursor;
GN Name=GLU1D;
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, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Chinese Spring;
RX PubMed=21875895; DOI=10.1104/pp.111.182378;
RA Sue M., Nakamura C., Nomura T.;
RT "Dispersed benzoxazinone gene cluster: molecular characterization and
RT chromosomal localization of glucosyltransferase and glucosidase genes in
RT wheat and rye.";
RL Plant Physiol. 157:985-997(2011).
RN [2]
RP PROTEIN SEQUENCE OF 51-62, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND SUBUNIT.
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).
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:21875895}.
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:21875895};
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:21875895};
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:21875895};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.34 mM for DIBOA-beta-D-glucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=1.83 mM for DIBOA-beta-D-glucoside (with recombinant enzyme)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=0.272 mM for DIMBOA-beta-D-glucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=0.79 mM for DIMBOA-beta-D-glucoside (with recombinant enzyme)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=2.02 mM for HBOA-beta-D-glucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=0.320 mM for HMBOA-beta-D-glucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=1.7 mM for p-nitrophenyl beta-D-glucopyranoside (with native
CC hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=1.78 mM for p-nitrophenyl beta-D-galactopyranoside (with native
CC hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=3.11 mM for p-nitrophenyl beta-D-xyloside (with native hexamer)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=0.67 mM for p-nitrophenyl beta-D-fucoside (with native hexamer)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC KM=0.240 mM for esculin (with native hexamer)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC Vmax=1060 nmol/sec/mg enzyme with DIBOA-beta-D-glucoside as substrate
CC (with native hexamer) {ECO:0000269|PubMed:10750901,
CC ECO:0000269|PubMed:21875895};
CC Vmax=4100 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as
CC substrate (with native hexamer) {ECO:0000269|PubMed:10750901,
CC ECO:0000269|PubMed:21875895};
CC Vmax=220 nmol/sec/mg enzyme with HBOA-beta-D-glucoside as substrate
CC (with native hexamer) {ECO:0000269|PubMed:10750901,
CC ECO:0000269|PubMed:21875895};
CC Vmax=540 nmol/sec/mg enzyme with HMBOA-beta-D-glucoside as substrate
CC (with native hexamer) {ECO:0000269|PubMed:10750901,
CC ECO:0000269|PubMed:21875895};
CC Vmax=520 nmol/sec/mg enzyme with p-nitrophenyl beta-D-glucopyranoside
CC as substrate (with native hexamer) {ECO:0000269|PubMed:10750901,
CC ECO:0000269|PubMed:21875895};
CC Vmax=47 nmol/sec/mg enzyme with p-nitrophenyl beta-D-
CC galactopyranoside as substrate (with native hexamer)
CC {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC Vmax=35 nmol/sec/mg enzyme with p-nitrophenyl beta-D-xyloside as
CC substrate (with native hexamer) {ECO:0000269|PubMed:10750901,
CC ECO:0000269|PubMed:21875895};
CC Vmax=1080 nmol/sec/mg enzyme with p-nitrophenyl beta-D-fucoside as
CC substrate (with native hexamer) {ECO:0000269|PubMed:10750901,
CC ECO:0000269|PubMed:21875895};
CC Vmax=320 nmol/sec/mg enzyme with esculin as substrate (with native
CC hexamer) {ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:21875895};
CC Note=kcat is 5728 sec(-1) with DIBOA-beta-D-glucoside as substrate
CC (with recombinant enzyme). kcat is 330 sec(-1) with DIMBOA-beta-D-
CC glucoside as substrate (with recombinant enzyme).;
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:10750901,
CC ECO:0000269|PubMed:21875895};
CC -!- SUBUNIT: Homo- and heterohexamers. {ECO:0000269|PubMed:10750901}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings early after
CC germination. {ECO:0000269|PubMed:10750901}.
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.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AB548284; BAJ07108.1; -; mRNA.
DR AlphaFoldDB; D5MTF8; -.
DR SMR; D5MTF8; -.
DR STRING; 4565.D5MTF8; -.
DR PaxDb; 4565-Traes_2AL_AEB11A672-1; -.
DR EnsemblPlants; TraesCSU02G036600.1; TraesCSU02G036600.1; TraesCSU02G036600.
DR EnsemblPlants; TraesWEE_scaffold_048529_01G000100.1; TraesWEE_scaffold_048529_01G000100.1; TraesWEE_scaffold_048529_01G000100.
DR Gramene; TraesCSU02G036600.1; TraesCSU02G036600.1; TraesCSU02G036600.
DR Gramene; TraesWEE_scaffold_048529_01G000100.1; TraesWEE_scaffold_048529_01G000100.1; TraesWEE_scaffold_048529_01G000100.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR OMA; CHEYPER; -.
DR OrthoDB; 334393at2759; -.
DR SABIO-RK; D5MTF8; -.
DR Proteomes; UP000019116; Chromosome Un.
DR ExpressionAtlas; D5MTF8; baseline and differential.
DR Genevisible; D5MTF8; TA.
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 Chloroplast; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 51..564
FT /note="4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-
FT benzoxazin-2-yl glucoside beta-D-glucosidase 1d,
FT chloroplastic"
FT /id="PRO_0000424100"
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
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:0000250|UniProtKB:Q7XSK0"
FT BINDING 194
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 239..240
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 383
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
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:0000250|UniProtKB:Q7XSK0"
FT BINDING 511..512
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT BINDING 520
FT /ligand="a beta-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22798"
FT /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT DISULFID 259..265
FT /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ SEQUENCE 564 AA; 63747 MW; 740B430A9A8A8027 CRC64;
MALLAAATLN PTTHLSLRSR AGRNSENLWL RSAASSQKSK GRFCNLTVRA GTPSKPAEPI
GPVFTKLKPW QIPKRDWFDK DFLFGASTSA YQIEGAWNED GKGPSTWDHF CHKYPERISD
GTNGDVAADS YHLYEEDVKA LKDMGMKVYR FSISWSRILP NGTGEVNQAG IDYYNKLINS
LISHDIVPYV TIWHWDTPQA LEDKYGGFLD PQIVDDYKQF AKLCFESFGD RVKNWFTFNE
PHTYCCFSYG EGIHAPGRCS PGMDCAVPEG DSLREPYTAG HHILLAHAEA VEMFRTHYNM
HGDSKIGMAF DVMGYEPYQD SFLDDQARER SIDYNLGWFL EPVVRGDYPF SMRSLIGDRL
PVFTKEEQEK LASSCDIMGL NYYTSRFSKH VDISPDVTPK LNTDDAYASS ETTGSDGNDI
GPITGTYWIY MYPKGLTDLL LIMKEKYGNP PIFITENGIA DVDGDETMPD PLDDWKRLDY
LQRHISAVKD AIDQGADVRG HFTWGLIDNF EWGSGYSSRF GLVYIDKNDG FKRKLKKSAK
WFSKFNAVPK HLLGTTKPTG QAPV
//
