ID MYRO2_BREBR Reviewed; 140 AA. AC P83179; DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 2. DT 14-DEC-2022, entry version 51. DE RecName: Full=Myrosinase 2; DE EC=3.2.1.147; DE AltName: Full=Beta-glucosidase 2; DE AltName: Full=Beta-thioglucosidase 2; DE AltName: Full=Beta-thioglucosidase glucohydrolase 2; DE AltName: Full=Myrosinase; DE AltName: Full=Sinigrinase 2; DE AltName: Full=Thioglucosidase 2; DE Flags: Fragments; OS Brevicoryne brassicae (Mealy cabbage aphid). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha; OC Aphidoidea; Aphididae; Macrosiphini; Brevicoryne. OX NCBI_TaxID=69196 {ECO:0000305}; RN [1] {ECO:0000305} RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=11179970; DOI=10.1046/j.1432-1327.2001.01971.x; RA Pontoppidan B., Ekbom B., Eriksson S., Meijer J.; RT "Purification and characterization of myrosinase from the cabbage aphid RT (Brevicoryne brassicae), a brassica herbivore."; RL Eur. J. Biochem. 268:1041-1048(2001). CC -!- FUNCTION: Degradation of glucosinolates (glucose residue linked by a CC thioglucoside bound to an amino acid derivative) to glucose, sulfate CC and any of the products: thiocyanates, isothiocyanates, nitriles, CC epithionitriles or oxazolidine-2-thiones. CC {ECO:0000250|UniProtKB:P37702, ECO:0000269|PubMed:11179970}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a thioglucoside + H2O = a sugar + a thiol.; EC=3.2.1.147; CC Evidence={ECO:0000269|PubMed:11179970}; CC -!- ACTIVITY REGULATION: Inhibited by ascorbate. CC {ECO:0000269|PubMed:11179970}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.41 mM for sinigrin (at pH 4.5 and 37 degrees Celsius) CC {ECO:0000269|PubMed:11179970}; CC KM=0.52 mM for p-nitrophenyl-beta-glucopyranoside (at pH 4.5 and 37 CC degrees Celsius) {ECO:0000269|PubMed:11179970}; CC Temperature dependence: CC Optimum temperature is about 40 degrees Celsius. CC {ECO:0000269|PubMed:11179970}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11179970}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}. CC -!- CAUTION: The order of the peptides shown is unknown. {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 AlphaFoldDB; P83179; -. DR SMR; P83179; -. DR GO; GO:0102799; F:glucosinolate glucohydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0019137; F:thioglucosidase activity; IEA:UniProtKB-EC. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase. FT CHAIN <1..>140 FT /note="Myrosinase 2" FT /id="PRO_0000063904" FT ACT_SITE 70 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055" FT CARBOHYD 114 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT NON_CONS 12..13 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_CONS 26..27 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_CONS 35..36 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_CONS 44..45 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_CONS 58..59 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_CONS 84..85 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_CONS 97..98 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_CONS 111..112 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_CONS 124..125 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_TER 1 FT /evidence="ECO:0000303|PubMed:11179970" FT NON_TER 140 FT /evidence="ECO:0000303|PubMed:11179970" SQ SEQUENCE 140 AA; 15646 MW; A03EF5F737CD8ABD CRC64; DFMFGTSTAS GGLAPSGVMN SLEPKGLAYY NNLLNELLKV LFTYFGDRAY APNSPQRLSL SLSGVFHLLR GTADFYALNH YSSRDKYGLP KLLLTEDGYG DDGQLDDFEK NYLNATLQAM YLMKEQNVTS VHYTVNKCMN //