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 15-MAR-2017, entry version 74. 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; GN ORFNames=F5D21.17; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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 RT 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., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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., RA Esen A.; RT "Functional genomic analysis of Arabidopsis thaliana glycoside RT hydrolase 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 RT different catalytic properties."; RL Phytochemistry 70:1345-1354(2009). CC -!- FUNCTION: Hydrolyzes sinigrin and, with lower efficiency, p- CC nitrophenyl beta-D-glucoside. {ECO:0000269|PubMed:19703694}. CC -!- CATALYTIC ACTIVITY: A thioglucoside + H(2)O = a sugar + a thiol. CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D- CC glucosyl residues with release of beta-D-glucose. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=547 uM for sinigrin (at pH 4.5) CC {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 CC 4.5) {ECO:0000269|PubMed:19703694}; CC Vmax=17 umol/min/mg enzyme with p-nitrophenyl beta-D-glucoside CC as 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 CC donor in plant myrosinases is not impairing the hydrolysis of CC glucosinolates. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. CC {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 UniGene; At.25235; -. DR UniGene; At.48300; -. DR ProteinModelPortal; Q3ECS3; -. 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 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 eggNOG; COG2723; LUCA. DR HOGENOM; HOG000088630; -. DR InParanoid; Q3ECS3; -. DR KO; K01237; -. DR OMA; CFEKRIL; -. DR OrthoDB; EOG0936077Q; -. DR PhylomeDB; Q3ECS3; -. DR Reactome; R-ATH-189085; Digestion of dietary carbohydrate. 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: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:0019762; P:glucosinolate catabolic process; IBA:GO_Central. DR GO; GO:0009725; P:response to hormone; IBA:GO_Central. DR GO; GO:0009651; P:response to salt stress; IEP:TAIR. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR001360; Glyco_hydro_1. DR InterPro; IPR018120; Glyco_hydro_1_AS. DR InterPro; IPR033132; Glyco_hydro_1_N_CS. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. 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 Complete proteome; Disulfide bond; Glycoprotein; Glycosidase; KW Hydrolase; Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 511 Myrosinase 5. FT /FTId=PRO_0000389597. FT REGION 474 475 Substrate binding. {ECO:0000250}. FT ACT_SITE 418 418 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU10055}. FT BINDING 64 64 Substrate. {ECO:0000250}. FT BINDING 165 165 Substrate. {ECO:0000250}. FT BINDING 210 210 Substrate. {ECO:0000250}. FT BINDING 211 211 Ascorbate. {ECO:0000250}. FT BINDING 280 280 Ascorbate. {ECO:0000250}. FT BINDING 351 351 Substrate. {ECO:0000250}. FT BINDING 467 467 Substrate. {ECO:0000250}. FT CARBOHYD 46 46 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 53 53 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 222 222 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 428 428 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 489 489 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 31 450 {ECO:0000250}. FT DISULFID 39 445 {ECO:0000250}. FT DISULFID 230 233 {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 //