STSY_CATRO
ID STSY_CATRO Reviewed; 352 AA.
AC P18417;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Strictosidine synthase;
DE EC=4.3.3.2;
DE Flags: Precursor;
GN Name=STR1; Synonyms=SSS;
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 32-52.
RC STRAIN=cv. G. Don;
RX PubMed=1600148; DOI=10.1007/bf00047715;
RA Pasquali G., Goddijn O.J.M., de Waal A., Verpoorte R., Schilperoort R.A.,
RA Hoge J.H.C., Memelink J.;
RT "Coordinated regulation of two indole alkaloid biosynthetic genes from
RT Catharanthus roseus by auxin and elicitors.";
RL Plant Mol. Biol. 18:1121-1131(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Morning mist;
RA Pasquali G., Erven A., Menke F., Memelink J.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-352.
RX PubMed=2395663; DOI=10.1093/nar/18.16.4939;
RA McKnight T.D., Roessner C.A., Devagupta R., Scott A.I., Nessler C.L.;
RT "Nucleotide sequence of a cDNA encoding the vacuolar protein strictosidine
RT synthase from Catharanthus roseus.";
RL Nucleic Acids Res. 18:4939-4939(1990).
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 -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC {ECO:0000305}.
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DR EMBL; X61932; CAA43936.1; -; mRNA.
DR EMBL; Y10182; CAA71255.1; -; Genomic_DNA.
DR EMBL; X53602; CAA37671.1; -; mRNA.
DR PIR; S22464; S22464.
DR PDB; 6ZEA; X-ray; 1.54 A; A=32-352.
DR PDBsum; 6ZEA; -.
DR AlphaFoldDB; P18417; -.
DR SMR; P18417; -.
DR ChEMBL; CHEMBL4369; -.
DR KEGG; ag:CAA37671; -.
DR BioCyc; MetaCyc:MON-11582; -.
DR BRENDA; 4.3.3.2; 1211.
DR UniPathway; UPA00311; UER00447.
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..31
FT /evidence="ECO:0000269|PubMed:1600148"
FT CHAIN 32..352
FT /note="Strictosidine synthase"
FT /id="PRO_0000033332"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 285
FT /note="R -> S (in Ref. 3; CAA37671)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="F -> S (in Ref. 3; CAA37671)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="S -> QLVIN (in Ref. 3; CAA37671)"
FT /evidence="ECO:0000305"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6ZEA"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:6ZEA"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6ZEA"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:6ZEA"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6ZEA"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6ZEA"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:6ZEA"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:6ZEA"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:6ZEA"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:6ZEA"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:6ZEA"
FT TURN 307..311
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:6ZEA"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:6ZEA"
SQ SEQUENCE 352 AA; 39094 MW; 1D6DD289A00272B8 CRC64;
MANFSESKSM MAVFFMFFLL LLSSSSSSSS SSPILKKIFI ESPSYAPNAF TFDSTDKGFY
TSVQDGRVIK YEGPNSGFTD FAYASPFWNK AFCENSTDPE KRPLCGRTYD ISYDYKNSQM
YIVDGHYHLC VVGKEGGYAT QLATSVQGVP FKWLYAVTVD QRTGIVYFTD VSSIHDDSPE
GVEEIMNTSD RTGRLMKYDP STKETTLLLK ELHVPGGAEI SADGSFVVVA EFLSNRIVKY
WLEGPKKGSA EFLVTIPNPG NIKRNSDGHF WVSSSEELDG GQHGRVVSRG IKFDGFGNIL
QVIPLPPPYE GEHFEQIQEH DGLLYIGSLF HSSVGILVYD DHDNKGNSYV SS
