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4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1c, chloroplastic (EC 3.2.1.182) (Beta-glucosidase 1c) (Taglu1c) (EC 3.2.1.21)

 HGL1C_WHEAT             Reviewed;         570 AA.
Q1XH04;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 1.
05-DEC-2018, entry version 62.
RecName: Full=4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1c, chloroplastic;
EC=3.2.1.182;
AltName: Full=Beta-glucosidase 1c;
Short=Taglu1c;
EC=3.2.1.21;
Flags: Precursor;
Name=GLU1C;
Triticum aestivum (Wheat).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
NCBI_TaxID=4565;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
DEVELOPMENTAL STAGE, AND SUBUNIT.
STRAIN=cv. Chinese Spring; TISSUE=Shoot;
PubMed=16751439; DOI=10.1104/pp.106.077693;
Sue M., Yamazaki K., Yajima S., Nomura T., Matsukawa T., Iwamura H.,
Miyamoto T.;
"Molecular and structural characterization of hexameric beta-D-
glucosidases in wheat and rye.";
Plant Physiol. 141:1237-1247(2006).
[2]
PROTEIN SEQUENCE OF 51-62, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND SUBUNIT.
STRAIN=cv. Asakazekomugi;
PubMed=10750901; DOI=10.1007/s004250050029;
Sue M., Ishihara A., Iwamura H.;
"Purification and characterization of a hydroxamic acid glucoside
beta-glucosidase from wheat (Triticum aestivum L.) seedlings.";
Planta 210:432-438(2000).
-!- FUNCTION: Acts in defense of young plant parts against pests via
the production of hydroxamic acids from hydroxamic acid
glucosides. Enzymatic activity is highly correlated with plant
growth. The preferred substrate is DIMBOA-beta-D-glucoside.
{ECO:0000269|PubMed:10750901, ECO:0000269|PubMed:16751439}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl
residues with release of beta-D-glucose.; EC=3.2.1.21;
-!- CATALYTIC ACTIVITY:
Reaction=DIMBOA beta-D-glucoside + H2O = D-glucose + DIMBOA;
Xref=Rhea:RHEA:33975, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
ChEBI:CHEBI:18048, ChEBI:CHEBI:37573; EC=3.2.1.182;
-!- CATALYTIC ACTIVITY:
Reaction=DIBOA beta-D-glucoside + H2O = D-glucose + DIBOA;
Xref=Rhea:RHEA:33979, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
ChEBI:CHEBI:63558, ChEBI:CHEBI:63670; EC=3.2.1.182;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.34 mM for DIBOA-beta-D-glucoside (with native hexamer)
{ECO:0000269|PubMed:10750901};
KM=1.05 mM for DIBOA-beta-D-glucoside (with recombinant enzyme)
{ECO:0000269|PubMed:10750901};
KM=0.272 mM for DIMBOA-beta-D-glucoside (with native hexamer)
{ECO:0000269|PubMed:10750901};
KM=0.39 mM for DIMBOA-beta-D-glucoside (with recombinant enzyme)
{ECO:0000269|PubMed:10750901};
KM=2.02 mM for HBOA-beta-D-glucoside (with native hexamer)
{ECO:0000269|PubMed:10750901};
KM=0.320 mM for HMBOA-beta-D-glucoside (with native hexamer)
{ECO:0000269|PubMed:10750901};
KM=1.7 mM for p-nitrophenyl beta-D-glucopyranoside (with native
hexamer) {ECO:0000269|PubMed:10750901};
KM=1.75 mM for p-nitrophenyl beta-D-glucopyranoside (with
recombinant enzyme) {ECO:0000269|PubMed:10750901};
KM=1.78 mM for p-nitrophenyl beta-D-galactopyranoside (with
native hexamer) {ECO:0000269|PubMed:10750901};
KM=3.11 mM for p-nitrophenyl beta-D-xyloside (with native
hexamer) {ECO:0000269|PubMed:10750901};
KM=0.67 mM for p-nitrophenyl beta-D-fucoside (with native
hexamer) {ECO:0000269|PubMed:10750901};
KM=0.240 mM for esculin (with native hexamer)
{ECO:0000269|PubMed:10750901};
Vmax=1060 nmol/sec/mg enzyme with DIBOA-beta-D-glucoside as
substrate (with native hexamer) {ECO:0000269|PubMed:10750901};
Vmax=4100 nmol/sec/mg enzyme with DIMBOA-beta-D-glucoside as
substrate (with native hexamer) {ECO:0000269|PubMed:10750901};
Vmax=220 nmol/sec/mg enzyme with HBOA-beta-D-glucoside as
substrate (with native hexamer) {ECO:0000269|PubMed:10750901};
Vmax=540 nmol/sec/mg enzyme with HMBOA-beta-D-glucoside as
substrate (with native hexamer) {ECO:0000269|PubMed:10750901};
Vmax=520 nmol/sec/mg enzyme with p-nitrophenyl beta-D-
glucopyranoside as substrate (with native hexamer)
{ECO:0000269|PubMed:10750901};
Vmax=47 nmol/sec/mg enzyme with p-nitrophenyl beta-D-
galactopyranoside as substrate (with native hexamer)
{ECO:0000269|PubMed:10750901};
Vmax=35 nmol/sec/mg enzyme with p-nitrophenyl beta-D-xyloside as
substrate (with native hexamer) {ECO:0000269|PubMed:10750901};
Vmax=1080 nmol/sec/mg enzyme with p-nitrophenyl beta-D-fucoside
as substrate (with native hexamer)
{ECO:0000269|PubMed:10750901};
Vmax=320 nmol/sec/mg enzyme with esculin as substrate (with
native hexamer) {ECO:0000269|PubMed:10750901};
Note=kcat is 137 sec(-1) with DIBOA-beta-D-glucoside as
substrate (with recombinant enzyme). kcat is 773 sec(-1) with
DIMBOA-beta-D-glucoside as substrate (with recombinant enzyme).
kcat is 235.9 sec(-1) with p-nitrophenyl beta-D-glucopyranoside
as substrate (with recombinant enzyme).;
pH dependence:
Optimum pH is 5.5. {ECO:0000269|PubMed:10750901};
-!- SUBUNIT: Homo- and heterohexamers. {ECO:0000269|PubMed:10750901,
ECO:0000269|PubMed:16751439}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in young seedlings early after
germination. {ECO:0000269|PubMed:10750901}.
-!- DEVELOPMENTAL STAGE: Peak of expression 36 to 48 hours after
imbibition. {ECO:0000269|PubMed:16751439}.
-!- MISCELLANEOUS: Wheat is a hexaploid with three different genomes
that contains at least four genes coding for GLU1: GLU1A (AC
Q1XIR9), GLU1B (AC Q1XH05), GLU1C (AC Q1XH04) and GLU1D (AC
D5MTF8). The monomers can aggregate in diverse combinations,
reflecting the several isozymes found in the native enzyme
described in PubMed:10750901.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB236423; BAE92260.1; -; mRNA.
UniGene; Ta.90767; -.
ProteinModelPortal; Q1XH04; -.
SMR; Q1XH04; -.
CAZy; GH1; Glycoside Hydrolase Family 1.
PRIDE; Q1XH04; -.
EnsemblPlants; TraesCS2D02G594400.1; TraesCS2D02G594400.1; TraesCS2D02G594400.
Gramene; TraesCS2D02G594400.1; TraesCS2D02G594400.1; TraesCS2D02G594400.
OMA; ERCSGHN; -.
BRENDA; 3.2.1.21; 6500.
SABIO-RK; Q1XH04; -.
Proteomes; UP000019116; Unplaced.
ExpressionAtlas; Q1XH04; baseline.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0102726; F:DIMBOA glucoside beta-D-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
InterPro; IPR001360; Glyco_hydro_1.
InterPro; IPR018120; Glyco_hydro_1_AS.
InterPro; IPR033132; Glyco_hydro_1_N_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR10353; PTHR10353; 1.
Pfam; PF00232; Glyco_hydro_1; 1.
PRINTS; PR00131; GLHYDRLASE1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycosidase; Hydrolase; Plastid; Reference proteome;
Transit peptide.
TRANSIT 1 50 Chloroplast. {ECO:0000250}.
CHAIN 51 570 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-
1,4-benzoxazin-2-yl glucoside beta-D-
glucosidase 1c, chloroplastic.
/FTId=PRO_0000424099.
REGION 511 512 Substrate binding. {ECO:0000250}.
ACT_SITE 240 240 Proton donor. {ECO:0000250}.
ACT_SITE 456 456 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10055}.
BINDING 92 92 Substrate. {ECO:0000250}.
BINDING 239 239 Substrate. {ECO:0000250}.
BINDING 243 243 Substrate. {ECO:0000250}.
BINDING 504 504 Substrate. {ECO:0000250}.
DISULFID 259 265 {ECO:0000250}.
SEQUENCE 570 AA; 64565 MW; 00C7D62E9232F02F CRC64;
MALLAAATLN PTTHLSIRSR AGHNSENLWL RSAASSQKSK GRFCNLTVRA GTPSKPAEPI
GPVFTKLKPW QIPKRDWFDK DFLFGASTSA YQIEGAWNED GKGPSTWDHF CHTYPERISD
RTNGDVAANS YHLYEEDVKA LKDMGMKVYR FSISWSRILP NGTGKPNQKG IDYYNNLINS
LIHHGIVPYV TIWHWDTPQA LEDKYGGFLN RQIVNDYKHF AKVCFESFGD RVKNWFTFNE
PHTYCCFSYG EGIHAPGRCS PGMDCAVPEG DSLREPYTAG HHILLAHAEA VELFKAHYNE
HGDSKIGMAF DVMGYEPYQD SFLDDQARER SIDYNLGWFL EPVVRGDYPF SMRSLIGDRL
PMFTKEEQEK LASSCDIMGL NYYTSRFSKH VDISSDFTPK LNTDDAYASS ETKGSDGNDI
GPITGTYWIY MYPKGLTDLL LIMKEKYGNP PIFITENGIA DVDSDPTMTD PLDDWKRLDY
LQRHISAVKD AIDQGADVRG HFTWGLIDNF EWSLGYSSRF GLVYIDKKDG NKRKLKKSAK
WFAKFNSVPK ALLKTTNTNN KPAVTASVSL


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