位置:首页 > 蛋白库 > HGL1D_WHEAT
HGL1D_WHEAT
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   03-AUG-2022, entry version 54.
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;
DE   AltName: Full=Beta-glucosidase 1d;
DE            Short=TaGlu1d;
DE            EC=3.2.1.21;
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   -!- 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, 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}.
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; AB548284; BAJ07108.1; -; mRNA.
DR   AlphaFoldDB; D5MTF8; -.
DR   SMR; D5MTF8; -.
DR   STRING; 4565.Traes_2AL_AEB11A672.1; -.
DR   PRIDE; D5MTF8; -.
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; HNDISAN; -.
DR   SABIO-RK; D5MTF8; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; D5MTF8; baseline.
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   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: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"
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"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024