HGL1A_WHEAT
ID HGL1A_WHEAT Reviewed; 569 AA.
AC Q1XIR9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1a, chloroplastic;
DE EC=3.2.1.182;
DE AltName: Full=Beta-glucosidase 1a;
DE Short=TaGlu1a;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=GLU1A;
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, AND MUTAGENESIS OF GLU-240; PHE-247; TYR-427; GLU-456;
RP SER-513 AND PHE-520.
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, 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: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=1.40 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=0.36 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=1.85 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=5200 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as
CC substrate (with recombinant enzyme) {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 48.8 sec(-1) with DIBOA-beta-D-glucoside as substrate
CC (with recombinant enzyme). kcat is 338 sec(-1) with DIMBOA-beta-D-
CC glucoside as substrate (with recombinant enzyme). kcat is 99.2 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}.
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.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB100035; BAE92901.1; -; mRNA.
DR AlphaFoldDB; Q1XIR9; -.
DR SMR; Q1XIR9; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PRIDE; Q1XIR9; -.
DR EnsemblPlants; TraesCS2B02G600200.2; TraesCS2B02G600200.2; TraesCS2B02G600200.
DR Gramene; TraesCS2B02G600200.2; TraesCS2B02G600200.2; TraesCS2B02G600200.
DR OMA; HRIQCIL; -.
DR BRENDA; 3.2.1.21; 6500.
DR SABIO-RK; Q1XIR9; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q1XIR9; 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; Direct protein sequencing; Disulfide bond; Glycosidase;
KW 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 1a,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_5000050749"
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 /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 511..512
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 259..265
FT /evidence="ECO:0000250"
FT MUTAGEN 240
FT /note="E->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:16751439"
FT MUTAGEN 247
FT /note="F->A: 99% loss of activity with DIBOA-Glc and
FT DIMBOA-Glc."
FT /evidence="ECO:0000269|PubMed:16751439"
FT MUTAGEN 427
FT /note="Y->A: 88% loss of activity with DIBOA-Glc and
FT DIMBOA-Glc."
FT /evidence="ECO:0000269|PubMed:16751439"
FT MUTAGEN 427
FT /note="Y->F: 77% loss of activity with DIBOA-Glc and 30%
FT with DIMBOA-Glc."
FT /evidence="ECO:0000269|PubMed:16751439"
FT MUTAGEN 456
FT /note="E->A: Total loss of activity."
FT /evidence="ECO:0000269|PubMed:16751439"
FT MUTAGEN 513
FT /note="S->F: 16% loss of activity with DIBOA-Glc and 94%
FT with DIMBOA-Glc."
FT /evidence="ECO:0000269|PubMed:16751439"
FT MUTAGEN 520
FT /note="F->Y: 43% loss of activity with DIBOA-Glc and 71%
FT with DIMBOA-Glc."
FT /evidence="ECO:0000269|PubMed:16751439"
SQ SEQUENCE 569 AA; 64508 MW; DA31869DCCC49C51 CRC64;
MALLAAATLN PTTHLSLRSR AGRNSENLWL RSAASSQKSK GRFCNLTIRA GTPSKPAEPI
GPVFTKLKPW QIPKRDWFDK DFLFGASTSA YQIEGAWNED GKGPSTWDHF CHTYPERISD
RTNGDVAANS YHLYEEDVKA LKDMGMKVYR FSIAWSRILP DGTGKVNQAG IDYYNKLINS
LIDNDIVPYV TIWHWDTPQA LEDKYGGFLN RKIVDDYKQF AEVCFKNFGD RVKNWFTFNE
PHTYCCFSYG EGIHAPGRCS PGMDCAVPKG DSLREPYTAG HHILLAHAEA VELFKACYNK
HGDSKIGMAF DVMGYEPFQD SFLDDQARER SIDYNLGWFL EPVVRGDYPF SMRSLIGDRL
PKFTKEEQEK LASSCDIMGL NYYTSRFSKH IDISSDFTPK LNTDDAYASS ETKGSDGNDI
GPITGTYWIY MYPKGLTDLL LIMKEKYGNP PIFITENGIA DVDSDPTMTD PLDDWKRLDY
LQRHISAVKD AIDQGADVRG HFTWGLIDNF EWSLGYSSRF GLVYIDKKDG NKRKLKKSAK
WFAKFNSVPK RLLKTTNNNA TVTVTSVSV
