STSY_RAUSE
ID STSY_RAUSE Reviewed; 344 AA.
AC P68175; P15324;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Strictosidine synthase;
DE EC=4.3.3.2;
DE Flags: Precursor;
GN Name=STR1;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3049153; DOI=10.1016/0014-5793(88)80167-4;
RA Kutchan T.M., Hampp N., Lottspeich F., Beyreuther K., Zenk M.H.;
RT "The cDNA clone for strictosidine synthase from Rauvolfia serpentina. DNA
RT sequence determination and expression in Escherichia coli.";
RL FEBS Lett. 237:40-44(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND TISSUE SPECIFICITY.
RX PubMed=1567228; DOI=10.1016/0003-9861(92)90746-j;
RA Bracher D., Kutchan T.M.;
RT "Strictosidine synthase from Rauvolfia serpentina: analysis of a gene
RT involved in indole alkaloid biosynthesis.";
RL Arch. Biochem. Biophys. 294:717-723(1992).
CC -!- FUNCTION: Catalyzes the stereospecific condensation of tryptamine with
CC secologanin to form strictosidine, the key intermediate of indole
CC alkaloid biosynthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha(S)-strictosidine + H2O = secologanin + tryptamine;
CC Xref=Rhea:RHEA:15013, ChEBI:CHEBI:15377, ChEBI:CHEBI:18002,
CC ChEBI:CHEBI:57887, ChEBI:CHEBI:58193; EC=4.3.3.2;
CC -!- PATHWAY: Alkaloid biosynthesis; 3alpha(S)-strictosidine biosynthesis;
CC 3alpha(S)-strictosidine from secologanin and tryptamine: step 1/1.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Vacuole.
CC -!- TISSUE SPECIFICITY: Expressed predominantly, but not exclusively, in
CC the root. {ECO:0000269|PubMed:1567228}.
CC -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC {ECO:0000305}.
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DR EMBL; Y00756; CAA68725.1; -; mRNA.
DR EMBL; X62334; CAA44208.1; -; Genomic_DNA.
DR PIR; S01325; S01325.
DR PDB; 2FP8; X-ray; 2.30 A; A/B=23-344.
DR PDB; 2FP9; X-ray; 2.96 A; A/B=23-344.
DR PDB; 2FPB; X-ray; 2.80 A; A/B=23-344.
DR PDB; 2FPC; X-ray; 3.00 A; A/B=23-344.
DR PDB; 2V91; X-ray; 3.01 A; A/B=32-333.
DR PDB; 2VAQ; X-ray; 3.01 A; A/B=23-344.
DR PDB; 3V1S; X-ray; 2.33 A; A/B=23-344.
DR PDB; 4IMB; X-ray; 2.70 A; A/B=32-332.
DR PDB; 4IYG; X-ray; 2.70 A; A/B=32-333.
DR PDB; 6N5V; X-ray; 2.55 A; A/B=29-344.
DR PDBsum; 2FP8; -.
DR PDBsum; 2FP9; -.
DR PDBsum; 2FPB; -.
DR PDBsum; 2FPC; -.
DR PDBsum; 2V91; -.
DR PDBsum; 2VAQ; -.
DR PDBsum; 3V1S; -.
DR PDBsum; 4IMB; -.
DR PDBsum; 4IYG; -.
DR PDBsum; 6N5V; -.
DR AlphaFoldDB; P68175; -.
DR SMR; P68175; -.
DR KEGG; ag:CAA44208; -.
DR BRENDA; 4.3.3.2; 5309.
DR UniPathway; UPA00311; UER00447.
DR EvolutionaryTrace; P68175; -.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0016844; F:strictosidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR018119; Strictosidine_synth_cons-reg.
DR InterPro; IPR004141; Strictosidine_synthase.
DR PANTHER; PTHR10426:SF57; PTHR10426:SF57; 1.
DR Pfam; PF03088; Str_synth; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alkaloid metabolism; Direct protein sequencing; Glycoprotein;
KW Lyase; Signal; Vacuole.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..344
FT /note="Strictosidine synthase"
FT /id="PRO_0000033334"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2FPB"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2FP8"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:2FP8"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2FP8"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2FP8"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2FP8"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:2FP8"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:2FP8"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:2FP8"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6N5V"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:2FP8"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:2FP8"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:2FP8"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:2FP8"
FT TURN 301..305
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2FP8"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:2FP8"
SQ SEQUENCE 344 AA; 38162 MW; 7CD38882621F768A CRC64;
MAKLSDSQTM ALFTVFLLFL SSSLALSSPI LKEILIEAPS YAPNSFTFDS TNKGFYTSVQ
DGRVIKYEGP NSGFVDFAYA SPYWNKAFCE NSTDAEKRPL CGRTYDISYN LQNNQLYIVD
CYYHLSVVGS EGGHATQLAT SVDGVPFKWL YAVTVDQRTG IVYFTDVSTL YDDRGVQQIM
DTSDKTGRLI KYDPSTKETT LLLKELHVPG GAEVSADSSF VLVAEFLSHQ IVKYWLEGPK
KGTAEVLVKI PNPGNIKRNA DGHFWVSSSE ELDGNMHGRV DPKGIKFDEF GNILEVIPLP
PPFAGEHFEQ IQEHDGLLYI GTLFHGSVGI LVYDKKGNSF VSSH
