SG1_RAUSE
ID SG1_RAUSE Reviewed; 532 AA.
AC Q8GU20;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Strictosidine-O-beta-D-glucosidase;
DE EC=3.2.1.105;
GN Name=SGR1;
OS Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Rauvolfiinae; Rauvolfia.
OX NCBI_TaxID=4060;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Protoplast;
RA Gerasimenko I., Sheludko Y., Stoeckigt J.;
RT "Molecular cloning and functional bacterial expression of strictosidine
RT glucosidase from Rauvolfia serpentina cell suspension cultures.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22004291; DOI=10.1021/cb200267w;
RA Xia L., Ruppert M., Wang M., Panjikar S., Lin H., Rajendran C.,
RA Barleben L., Stoeckigt J.;
RT "Structures of alkaloid biosynthetic glucosidases decode substrate
RT specificity.";
RL ACS Chem. Biol. 7:226-234(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) IN COMPLEX WITH SUBSTRATE,
RP MUTAGENESIS OF HIS-161; GLU-207; PHE-373; GLY-386; TRP-388; GLU-416 AND
RP TYR-481, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17890378; DOI=10.1105/tpc.106.045682;
RA Barleben L., Panjikar S., Ruppert M., Koepke J., Stoeckigt J.;
RT "Molecular architecture of strictosidine glucosidase: the gateway to the
RT biosynthesis of the monoterpenoid indole alkaloid family.";
RL Plant Cell 19:2886-2897(2007).
CC -!- FUNCTION: Glucosidase specifically involved in alkaloid biosynthesis
CC leading to the accumulation of several alkaloids, including ajmaline,
CC an important plant-derived pharmaceutical used in the therapy of heart
CC disorders. {ECO:0000269|PubMed:22004291}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha(S)-strictosidine + H2O = D-glucose + strictosidine
CC aglycone; Xref=Rhea:RHEA:12917, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58012, ChEBI:CHEBI:58193; EC=3.2.1.105;
CC Evidence={ECO:0000269|PubMed:17890378};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for strictosidine (at pH 5.7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17890378};
CC KM=120 uM for strictosidine {ECO:0000269|PubMed:22004291};
CC Note=kcat is 9.8 sec(-1) with strictosidine as substrate (at pH 5.7
CC and 30 degrees Celsius. {ECO:0000269|PubMed:17890378};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AJ302044; CAC83098.1; -; mRNA.
DR PDB; 2JF6; X-ray; 2.82 A; A/B=1-532.
DR PDB; 2JF7; X-ray; 2.48 A; A/B=1-532.
DR PDB; 3ZJ7; X-ray; 2.50 A; A/B=1-532.
DR PDB; 3ZJ8; X-ray; 3.01 A; A/B=1-532.
DR PDBsum; 2JF6; -.
DR PDBsum; 2JF7; -.
DR PDBsum; 3ZJ7; -.
DR PDBsum; 3ZJ8; -.
DR AlphaFoldDB; Q8GU20; -.
DR SMR; Q8GU20; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PRIDE; Q8GU20; -.
DR KEGG; ag:CAC83098; -.
DR BioCyc; MetaCyc:MON-12391; -.
DR BRENDA; 3.2.1.105; 5309.
DR EvolutionaryTrace; Q8GU20; -.
DR GO; GO:0050422; F:strictosidine beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0009821; P:alkaloid biosynthetic process; IDA:UniProtKB.
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; Alkaloid metabolism; Glycosidase; Hydrolase.
FT CHAIN 1..532
FT /note="Strictosidine-O-beta-D-glucosidase"
FT /id="PRO_0000418401"
FT REGION 512..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /note="Proton donor"
FT ACT_SITE 416
FT /note="Nucleophile"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17890378"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17890378"
FT BINDING 206..207
FT /ligand="substrate"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17890378"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17890378"
FT BINDING 472..473
FT /ligand="substrate"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17890378"
FT SITE 388
FT /note="Controls the gate shape and acceptance of
FT substrates"
FT MUTAGEN 161
FT /note="H->L,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17890378"
FT MUTAGEN 207
FT /note="E->D,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17890378"
FT MUTAGEN 373
FT /note="F->T: Reduced affinity but increased activity."
FT /evidence="ECO:0000269|PubMed:17890378"
FT MUTAGEN 386
FT /note="G->S: Reduced affinity and activity."
FT /evidence="ECO:0000269|PubMed:17890378"
FT MUTAGEN 388
FT /note="W->A: Loss of activity and reduced affinity."
FT /evidence="ECO:0000269|PubMed:17890378"
FT MUTAGEN 416
FT /note="E->D,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17890378"
FT MUTAGEN 481
FT /note="Y->F: Reduced affinity."
FT /evidence="ECO:0000269|PubMed:17890378"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 95..109
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 180..195
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3ZJ7"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 237..259
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 284..297
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 327..333
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 393..407
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:2JF6"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 436..454
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 459..465
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:2JF7"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:2JF7"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:2JF7"
FT HELIX 497..507
FT /evidence="ECO:0007829|PDB:2JF7"
SQ SEQUENCE 532 AA; 60881 MW; FC65D93E90212710 CRC64;
MDNTQAEPLV VAIVPKPNAS TEHTNSHLIP VTRSKIVVHR RDFPQDFIFG AGGSAYQCEG
AYNEGNRGPS IWDTFTQRSP AKISDGSNGN QAINCYHMYK EDIKIMKQTG LESYRFSISW
SRVLPGGRLA AGVNKDGVKF YHDFIDELLA NGIKPSVTLF HWDLPQALED EYGGFLSHRI
VDDFCEYAEF CFWEFGDKIK YWTTFNEPHT FAVNGYALGE FAPGRGGKGD EGDPAIEPYV
VTHNILLAHK AAVEEYRNKF QKCQEGEIGI VLNSMWMEPL SDVQADIDAQ KRALDFMLGW
FLEPLTTGDY PKSMRELVKG RLPKFSADDS EKLKGCYDFI GMNYYTATYV TNAVKSNSEK
LSYETDDQVT KTFERNQKPI GHALYGGWQH VVPWGLYKLL VYTKETYHVP VLYVTESGMV
EENKTKILLS EARRDAERTD YHQKHLASVR DAIDDGVNVK GYFVWSFFDN FEWNLGYICR
YGIIHVDYKS FERYPKESAI WYKNFIAGKS TTSPAKRRRE EAQVELVKRQ KT
