BGL34_ARATH
ID BGL34_ARATH Reviewed; 511 AA.
AC Q8GRX1; Q9SX92;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Myrosinase 4;
DE EC=3.2.1.147;
DE AltName: Full=Beta-glucosidase 34;
DE Short=AtBGLU34;
DE EC=3.2.1.21;
DE AltName: Full=Sinigrinase 4;
DE AltName: Full=Thioglucosidase 4;
DE Flags: Precursor;
GN Name=TGG4; Synonyms=BGLU34; OrderedLocusNames=At1g47600; ORFNames=F16N3.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Zhang J.;
RT "Characterization of a new subfamily of thioglucoside glucohydrolases.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT family 1.";
RL Plant Mol. Biol. 55:343-367(2004).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=19703694; DOI=10.1016/j.phytochem.2009.07.036;
RA Andersson D., Chakrabarty R., Bejai S., Zhang J., Rask L., Meijer J.;
RT "Myrosinases from root and leaves of Arabidopsis thaliana have different
RT catalytic properties.";
RL Phytochemistry 70:1345-1354(2009).
CC -!- FUNCTION: Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl
CC beta-D-glucoside. {ECO:0000269|PubMed:19703694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a thioglucoside + H2O = a sugar + a thiol.; EC=3.2.1.147;
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=245 uM for sinigrin (at pH 4.5) {ECO:0000269|PubMed:19703694};
CC KM=28 mM for p-nitrophenyl beta-D-glucoside (at pH 4.5)
CC {ECO:0000269|PubMed:19703694};
CC Vmax=12.2 umol/min/mg enzyme with sinigrin as substrate (at pH 4.5)
CC {ECO:0000269|PubMed:19703694};
CC Vmax=7.3 umol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as
CC substrate (at pH 4.5) {ECO:0000269|PubMed:19703694};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8GRX1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots.
CC {ECO:0000269|PubMed:19703694}.
CC -!- MISCELLANEOUS: It seems that the absence of a catalytic proton donor in
CC plant myrosinases is not impairing the hydrolysis of glucosinolates.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD46026.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ268795; ACO95139.1; -; Genomic_DNA.
DR EMBL; AC007519; AAD46026.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32191.1; -; Genomic_DNA.
DR EMBL; BT000471; AAN17448.1; -; mRNA.
DR EMBL; BT002202; AAN72213.1; -; mRNA.
DR EMBL; BT002458; AAO00818.1; -; mRNA.
DR PIR; G96516; G96516.
DR RefSeq; NP_175191.2; NM_103653.3. [Q8GRX1-1]
DR AlphaFoldDB; Q8GRX1; -.
DR SMR; Q8GRX1; -.
DR BioGRID; 26394; 1.
DR STRING; 3702.AT1G47600.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PaxDb; Q8GRX1; -.
DR ProteomicsDB; 240831; -. [Q8GRX1-1]
DR EnsemblPlants; AT1G47600.1; AT1G47600.1; AT1G47600. [Q8GRX1-1]
DR GeneID; 841169; -.
DR Gramene; AT1G47600.1; AT1G47600.1; AT1G47600. [Q8GRX1-1]
DR KEGG; ath:AT1G47600; -.
DR Araport; AT1G47600; -.
DR TAIR; locus:2015338; AT1G47600.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; Q8GRX1; -.
DR OMA; YGGWGSR; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q8GRX1; -.
DR BRENDA; 3.2.1.147; 399.
DR SABIO-RK; Q8GRX1; -.
DR PRO; PR:Q8GRX1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GRX1; baseline and differential.
DR Genevisible; Q8GRX1; AT.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0102799; F:glucosinolate glucohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0019137; F:thioglucosidase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
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 Alternative splicing; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..511
FT /note="Myrosinase 4"
FT /id="PRO_0000389596"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 474..475
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..450
FT /evidence="ECO:0000250"
FT DISULFID 39..445
FT /evidence="ECO:0000250"
FT DISULFID 230..233
FT /evidence="ECO:0000250"
SQ SEQUENCE 511 AA; 57542 MW; A977148B22E21D0E CRC64;
MAIPKAHYSL AVLVLLFVVV SSSQKVCNPE CKAKEPFHCD NTHAFNRTGF PRNFTFGAAT
SAYQIEGAAH RALNGWDYFT HRYPEKVPDR SSGDLACDSY DLYKDDVKLL KRMNVQAYRL
SIAWSRVLPK GRLTGGVDEN GITYYNNLIN ELKANGIEPY VTIFHWDVPQ TLEDEYGGFL
STRIVEDYTN YAELLFQRFG DRVKFWITLN QPFSLATKGY GDGSYPPGRC TGCELGGDSG
VEPYTVAHNQ LLAHAKTVSL YRKRYQKFQG GKIGTTLIGR WFAPLNEFSE LDKAAAKRAF
DFFVGWFLDP LVYGKYPTIM REMVGDRLPE FTPEQSALVK GSLDFLGLNY YVTQYATDAP
PPTQLNAITD ARVTLGFYRN GVPIGVVAPS FVYYPPGFRQ ILNYIKDNYK NPLTYITENG
VADLDLGNVT LATALADNGR IQNHCSHLSC LKCAMKDGCN VAGYFAWSLM DNYEFGNGYT
LRFGMNWVNF TNPADRKEKA SGKWFSKFLA K
