MYRO1_BREBR
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 03-AUG-2022, entry version 74.
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}.
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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 InterPro; IPR001360; Glyco_hydro_1.
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; 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
