ID   BGL35_ARATH             Reviewed;         511 AA.
AC   Q3ECS3; Q9C8J9;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Myrosinase 5 {ECO:0000303|PubMed:19703694};
DE            EC=3.2.1.147 {ECO:0000269|PubMed:19703694};
DE   AltName: Full=Beta-glucosidase 35 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU35 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000269|PubMed:19703694};
DE   AltName: Full=Sinigrinase 5 {ECO:0000303|PubMed:19703694};
DE   AltName: Full=Thioglucosidase 5 {ECO:0000303|PubMed:19703694};
DE   Flags: Precursor;
GN   Name=TGG5 {ECO:0000303|PubMed:19703694};
GN   Synonyms=BGLU35 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At1g51470 {ECO:0000312|Araport:AT1G51470};
GN   ORFNames=F5D21.17 {ECO:0000312|EMBL:AAG52628.1};
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   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   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP   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         Evidence={ECO:0000269|PubMed:19703694};
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:19703694};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=547 uM for sinigrin (at pH 4.5) {ECO:0000269|PubMed:19703694};
CC         KM=80 mM for p-nitrophenyl beta-D-glucoside (at pH 4.5)
CC         {ECO:0000269|PubMed:19703694};
CC         Vmax=48.1 umol/min/mg enzyme with sinigrin as substrate (at pH 4.5)
CC         {ECO:0000269|PubMed:19703694};
CC         Vmax=17 umol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as
CC         substrate (at pH 4.5) {ECO:0000269|PubMed:19703694};
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=AAG52628.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; FJ268796; ACO95140.1; -; Genomic_DNA.
DR   EMBL; AC024261; AAG52628.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32671.1; -; Genomic_DNA.
DR   PIR; A96553; A96553.
DR   RefSeq; NP_175558.3; NM_104025.4.
DR   AlphaFoldDB; Q3ECS3; -.
DR   SMR; Q3ECS3; -.
DR   BioGRID; 26797; 1.
DR   STRING; 3702.Q3ECS3; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q3ECS3; 5 sites, No reported glycans.
DR   PaxDb; 3702-AT1G51470-1; -.
DR   ProteomicsDB; 240336; -.
DR   EnsemblPlants; AT1G51470.1; AT1G51470.1; AT1G51470.
DR   GeneID; 841572; -.
DR   Gramene; AT1G51470.1; AT1G51470.1; AT1G51470.
DR   KEGG; ath:AT1G51470; -.
DR   Araport; AT1G51470; -.
DR   TAIR; AT1G51470; BGLU35.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q3ECS3; -.
DR   OMA; CTENVAP; -.
DR   OrthoDB; 637993at2759; -.
DR   PhylomeDB; Q3ECS3; -.
DR   BRENDA; 3.2.1.147; 399.
DR   SABIO-RK; Q3ECS3; -.
DR   PRO; PR:Q3ECS3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q3ECS3; baseline and differential.
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   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; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF301; MYROSINASE 4-RELATED; 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.
DR   Genevisible; Q3ECS3; AT.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..511
FT                   /note="Myrosinase 5"
FT                   /id="PRO_0000389597"
FT   ACT_SITE        418
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   BINDING         64
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         165
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         210..211
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GU20"
FT   BINDING         351
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         418
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         467
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         474..475
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         483
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        31..450
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..445
FT                   /evidence="ECO:0000250"
FT   DISULFID        230..233
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ   SEQUENCE   511 AA;  57468 MW;  0CEA34FA0DFB95B5 CRC64;
     MAIPKAHYSL AVLVLLFVVV SSSQKVCNPE CKAKEPFHCD NTHAFNRSGF PKNFTFGAAT
     SAYQIEGAAH RALNGWDYFT HRYPEKVPDR SSADLACDSY DLYKDDVKLL KRMNVQAYRL
     SIAWSRVLPK GRLTGGVDEN GITYYNNLIN ELKANGIEPY VTIFHWDVPQ TLEDEYGGFL
     STRIVEDYTN YAELLFQRFG DRVKFWITLN QPLSLALKGY GNGSYPPGRC TGCELGGDSG
     VEPYTVAHNQ LLAHAKTVSL YRKRYQKFQG GKIGTTLIGR WFVPLNEFSE LDKAAAKRAF
     DFFVGWFLDP LVYGKYPTIM REMVGDRLPE FTPEESALVK GSLDFLGLNY YVSQYATDAP
     PPTQPNAITD ARVTLGFYRN GSPIGVVASS FVYYPPGFRQ ILNYIKDNYK NPLTYITENG
     VADLDLGNVT LATALADNGR IQNHCSHLSC LKCAMKDGCN VAGYFAWSLM DNYEFGNGYT
     LRFGMNWVNF TNPADRKEKA SGKWFSKFLA K
//