ID MYRO1_BREBR Reviewed; 464 AA. AC Q95X01; DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Myrosinase 1 {ECO:0000303|PubMed:11804799}; DE EC=3.2.1.147; DE AltName: Full=Beta-glucosidase 1 {ECO:0000303|PubMed:11804799}; DE AltName: Full=Beta-thioglucosidase 1 {ECO:0000303|PubMed:11804799}; DE AltName: Full=Beta-thioglucosidase glucohydrolase 1 {ECO:0000303|PubMed:11804799}; DE AltName: Full=Sinigrinase 1 {ECO:0000303|PubMed:11804799}; DE AltName: Full=Thioglucosidase 1 {ECO:0000312|EMBL:AAL25999.1}; 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; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL25999.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PROTEIN RP SEQUENCE OF 98-111; 188-197; 253-261; 313-327 AND 389-393. RX PubMed=11804799; DOI=10.1016/s0965-1748(01)00088-1; RA Jones A.M., Winge P., Bones A.M., Cole R., Rossiter J.T.; RT "Characterization and evolution of a myrosinase from the cabbage aphid RT Brevicoryne brassicae."; RL Insect Biochem. Mol. Biol. 32:275-284(2002). RN [2] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, ACTIVE SITE GLU-167, ACTIVE SITE RP GLU-374, AND X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS). RX PubMed=16291087; DOI=10.1016/j.ibmb.2005.07.004; RA Husebye H., Arzt S., Burmeister W.P., Hartel F.V., Brandt A., RA Rossiter J.T., Bones A.M.; RT "Crystal structure at 1.1 Angstroms resolution of an insect myrosinase from RT Brevicoryne brassicae shows its close relationship to beta-glucosidases."; RL Insect Biochem. Mol. Biol. 35:1311-1320(2005). RN [3] {ECO:0000305} RP BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, AND PROTEIN SEQUENCE OF RP 98-111; 188-197; 253-261; 313-327 AND 389-393. RX PubMed=11102829; DOI=10.1016/s0965-1748(00)00157-0; RA Jones A.M., Bridges M., Bones A.M., Cole R., Rossiter J.T.; RT "Purification and characterisation of a non-plant myrosinase from the RT cabbage aphid Brevicoryne brassicae (L.)."; RL Insect Biochem. Mol. Biol. 31:1-5(2001). RN [4] {ECO:0000305} RP TISSUE SPECIFICITY. RX PubMed=11798435; DOI=10.1098/rspb.2001.1861; RA Bridges M., Jones A.M., Bones A.M., Hodgson C., Cole R., Bartlet E., RA Wallsgrove R., Karapapa V.K., Watts N., Rossiter J.T.; RT "Spatial organization of the glucosinolate-myrosinase system in brassica RT specialist aphids is similar to that of the host plant."; RL Proc. R. Soc. B 269:187-191(2002). RN [5] {ECO:0000305} RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=17623639; DOI=10.1098/rspb.2007.0237; RA Kazana E., Pope T.W., Tibbles L., Bridges M., Pickett J.A., Bones A.M., RA Powell G., Rossiter J.T.; RT "The cabbage aphid: a walking mustard oil bomb."; RL Proc. R. Soc. B 274:2271-2277(2007). CC -!- FUNCTION: Hydrolyzes glucosinolates to a labile aglycone. This rapidly CC undergoes spontaneous rearrangement, eliminating sulfur to yield a CC number of toxic metabolites. Thereby developing a chemical defense CC system that exploits and mimics the host plant. CC {ECO:0000269|PubMed:11804799, ECO:0000269|PubMed:17623639}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a thioglucoside + H2O = a sugar + a thiol.; EC=3.2.1.147; CC Evidence={ECO:0000269|PubMed:11804799}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.613 mM for allylglucosinolate {ECO:0000269|PubMed:11102829}; CC KM=0.915 mM for benzylglucosinolate {ECO:0000269|PubMed:11102829}; CC pH dependence: CC Optimum pH is 5.5 with sinigrin as substrate. CC {ECO:0000269|PubMed:11102829}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16291087}. CC -!- TISSUE SPECIFICITY: Expressed in the skeletal muscle tissues CC surrounding the head, abdomen and thorax. Not expressed in flight CC muscles (at protein level). {ECO:0000269|PubMed:11798435, CC ECO:0000269|PubMed:17623639}. CC -!- DEVELOPMENTAL STAGE: Expression in the head and thoracic muscle starts CC during embryonic development and levels continue to accumulate after CC the nymphs are born (at protein level). {ECO:0000269|PubMed:17623639}. CC -!- MASS SPECTROMETRY: Mass=54000; Mass_error=500; Method=MALDI; CC Evidence={ECO:0000269|PubMed:11102829}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. CC {ECO:0000269|PubMed:11804799}. 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; AF203780; AAL25999.1; -; mRNA. DR PDB; 1WCG; X-ray; 1.10 A; A/B=1-464. DR PDBsum; 1WCG; -. DR AlphaFoldDB; Q95X01; -. DR SMR; Q95X01; -. DR CAZy; GH1; Glycoside Hydrolase Family 1. DR BRENDA; 3.2.1.147; 981. DR EvolutionaryTrace; Q95X01; -. DR GO; GO:0102799; F:glucosinolate glucohydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 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. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Glycoprotein; Glycosidase; KW Hydrolase; Metal-binding; Zinc. FT CHAIN 1..464 FT /note="Myrosinase 1" FT /id="PRO_0000392945" FT ACT_SITE 167 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:16291087" FT ACT_SITE 374 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:16291087" FT BINDING 19 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P29736" FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P29736" FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P29736" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P29736" FT BINDING 166 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P29736" FT CARBOHYD 397 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 107 FT /note="N -> P (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 322 FT /note="P -> N (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 10..14 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 17..20 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 33..40 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 57..71 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 96..111 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 115..123 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 127..131 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 140..155 FT /evidence="ECO:0007829|PDB:1WCG" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 161..166 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 168..176 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 187..212 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 214..217 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 220..225 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 229..234 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 238..251 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 253..260 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 266..278 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 291..297 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 302..307 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 311..317 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 326..328 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 330..333 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 351..365 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 370..375 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 386..406 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 410..416 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 424..429 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 434..437 FT /evidence="ECO:0007829|PDB:1WCG" FT STRAND 446..448 FT /evidence="ECO:0007829|PDB:1WCG" FT HELIX 450..461 FT /evidence="ECO:0007829|PDB:1WCG" SQ SEQUENCE 464 AA; 53736 MW; 02E76E24504C393A CRC64; MDYKFPKDFM FGTSTASYQI EGGWNEDGKG ENIWDRLVHT SPEVIKDGTN GDIACDSYHK YKEDVAIIKD LNLKFYRFSI SWARIAPSGV MNSLEPKGIA YYNNLINELI KNDIIPLVTM YHWDLPQYLQ DLGGWVNPIM SDYFKEYARV LFTYFGDRVK WWITFNEPIA VCKGYSIKAY APNLNLKTTG HYLAGHTQLI AHGKAYRLYE EMFKPTQNGK ISISISGVFF MPKNAESDDD IETAERANQF ERGWFGHPVY KGDYPPIMKK WVDQKSKEEG LPWSKLPKFT KDEIKLLKGT ADFYALNHYS SRLVTFGSDP NPNFNPDASY VTSVDEAWLK PNETPYIIPV PEGLRKLLIW LKNEYGNPQL LITENGYGDD GQLDDFEKIS YLKNYLNATL QAMYEDKCNV IGYTVWSLLD NFEWFYGYSI HFGLVKIDFN DPQRTRTKRE SYTYFKNVVS TGKP //