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 02-JUN-2021, entry version 94. DE RecName: Full=Myrosinase 5; DE EC=3.2.1.147; DE AltName: Full=Beta-glucosidase 35; DE Short=AtBGLU35; DE EC=3.2.1.21; DE AltName: Full=Sinigrinase 5; DE AltName: Full=Thioglucosidase 5; DE Flags: Precursor; GN Name=TGG5; Synonyms=BGLU35; OrderedLocusNames=At1g51470; ORFNames=F5D21.17; 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, 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 + H(2)O = 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=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}; 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; 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 SMR; Q3ECS3; -. DR BioGRID; 26797; 1. DR STRING; 3702.AT1G51470.1; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR PaxDb; Q3ECS3; -. DR PRIDE; Q3ECS3; -. 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; locus:2033928; AT1G51470. DR eggNOG; KOG0626; Eukaryota. DR HOGENOM; CLU_001859_1_0_1; -. DR InParanoid; Q3ECS3; -. DR OMA; YYTHRYP; -. DR OrthoDB; 408001at2759; -. 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 Genevisible; Q3ECS3; 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 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 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 REGION 474..475 FT /note="Substrate binding" FT /evidence="ECO:0000250" FT ACT_SITE 418 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055" FT BINDING 64 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 165 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 210 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 211 FT /note="Ascorbate" FT /evidence="ECO:0000250" FT BINDING 280 FT /note="Ascorbate" FT /evidence="ECO:0000250" FT BINDING 351 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 467 FT /note="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 222 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; 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 //