ID   BGL36_ARATH             Reviewed;         484 AA.
AC   Q9C8K1;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Putative myrosinase 6 {ECO:0000250|UniProtKB:Q3ECS3};
DE            EC=3.2.1.147 {ECO:0000250|UniProtKB:Q3ECS3};
DE   AltName: Full=Beta-glucosidase 36 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU36 {ECO:0000303|PubMed:15604686};
DE   AltName: Full=Sinigrinase 6 {ECO:0000250|UniProtKB:Q3ECS3};
DE   AltName: Full=Thioglucosidase 6 {ECO:0000250|UniProtKB:Q3ECS3};
GN   Name=TGG6 {ECO:0000250|UniProtKB:Q3ECS3};
GN   Synonyms=BGLU36 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At1g51490 {ECO:0000312|Araport:AT1G51490};
GN   ORFNames=F5D21.16 {ECO:0000312|EMBL:AAG52622.1};
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 [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   [2]
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   [3]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a thioglucoside + H2O = a sugar + a thiol.; EC=3.2.1.147;
CC         Evidence={ECO:0000250|UniProtKB:Q3ECS3};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG52622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC024261; AAG52622.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; C96553; C96553.
DR   AlphaFoldDB; Q9C8K1; -.
DR   SMR; Q9C8K1; -.
DR   STRING; 3702.Q9C8K1; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q9C8K1; 3 sites, No reported glycans.
DR   PaxDb; 3702-AT1G51490-1; -.
DR   Araport; AT1G51490; -.
DR   TAIR; AT1G51490; BGLU36.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q9C8K1; -.
DR   PhylomeDB; Q9C8K1; -.
DR   BioCyc; ARA:AT1G51490-MONOMER; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C8K1; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0102799; F:glucosinolate glucohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019137; F:thioglucosidase activity; IEA:UniProtKB-EC.
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; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF328; MYROSINASE 6-RELATED; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   Genevisible; Q9C8K1; AT.
PE   5: Uncertain;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..484
FT                   /note="Putative myrosinase 6"
FT                   /id="PRO_0000389598"
FT   BINDING         39
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         140
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         184..185
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GU20"
FT   BINDING         321
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         440
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
FT   BINDING         447..448
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         456
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        204..207
FT                   /evidence="ECO:0000250|UniProtKB:Q7XSK0"
SQ   SEQUENCE   484 AA;  55527 MW;  0ACA3B6F3225154D CRC64;
     MQSRMQGQRT LQLRQNSCIQ PKWISQKNFT FGAATSAYQV EGAAHRALNG WDYFTHRYPE
     RVSDRSIGDL ACNSYDLYKD DVKLLKRMNV QAYRFSIAWS RVLPKGRLIG GVDENGITYY
     NNLINELKAN GIEPFVTIFH WDVPQDFRRR IWRLLKPTYS DFKNYAELLF QRFGDRVKFW
     ITLNQPYSLA VKGYGDGQYP PGRCTDCEFG GDSGTEPYIV GHHELLAHME AVSLYRKRYQ
     KFQGGKIGTT LIGRWFIPLN ETNDLDKAAA KREFDFSVLG STGVRTISKD NERLGDRLPK
     FTPKQSALLK GSLDFLGLNY YVTRYATYRP PPMPTQHSVL TDSGVTIGFE RNGVSIGVKA
     SINFDVKDLR HLVDFFLFVE LLLLSTRIPS DSKSHQKQEL LMLIANALAD NGRIQFQCSH
     LSCLKCAIED GCNVAGYFAW SLMDNYEFGN GYTLRFDMNW VNFTNPADRR EKASGKWFSR
     FIAK
//