SSL11_ARATH
ID SSL11_ARATH Reviewed; 329 AA.
AC P92976; Q0WLG6; Q9C9C1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein STRICTOSIDINE SYNTHASE-LIKE 11 {ECO:0000303|PubMed:10777701};
DE Short=AtSSL11 {ECO:0000303|PubMed:10777701};
DE EC=4.3.3.2;
DE AltName: Full=Strictosidine synthase 12 {ECO:0000303|PubMed:19121120};
DE Short=AtSS12 {ECO:0000303|PubMed:19121120};
DE AltName: Full=Strictosidine synthase 3;
DE Short=SS-3;
DE Flags: Precursor;
GN Name=SSL11 {ECO:0000303|PubMed:10777701};
GN Synonyms=SS12 {ECO:0000303|PubMed:19121120}, SS3;
GN OrderedLocusNames=At1g74000 {ECO:0000312|Araport:AT1G74000};
GN ORFNames=F2P9.13 {ECO:0000312|EMBL:AAG52519.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta;
RA Jain A.K., Nessler C.L.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=10777701; DOI=10.1006/bbrc.2000.2598;
RA Fabbri M., Delp G., Schmidt O., Theopold U.;
RT "Animal and plant members of a gene family with similarity to alkaloid-
RT synthesizing enzymes.";
RL Biochem. Biophys. Res. Commun. 271:191-196(2000).
RN [6]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=19121120; DOI=10.1111/j.1438-8677.2008.00139.x;
RA Sohani M.M., Schenk P.M., Schultz C.J., Schmidt O.;
RT "Phylogenetic and transcriptional analysis of a strictosidine synthase-like
RT gene family in Arabidopsis thaliana reveals involvement in plant defence
RT responses.";
RL Plant Biol. 11:105-117(2009).
CC -!- FUNCTION: Catalyzes the stereospecific condensation of tryptamine with
CC secologanin to form strictosidine, the key intermediate of indole
CC alkaloid biosynthesis. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40595.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U43946; AAB40595.1; ALT_FRAME; mRNA.
DR EMBL; AC016662; AAG52519.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35536.1; -; Genomic_DNA.
DR EMBL; AK230236; BAF02041.1; -; mRNA.
DR PIR; G96767; G96767.
DR RefSeq; NP_177540.3; NM_106059.5.
DR AlphaFoldDB; P92976; -.
DR SMR; P92976; -.
DR STRING; 3702.AT1G74000.1; -.
DR PaxDb; P92976; -.
DR PRIDE; P92976; -.
DR ProteomicsDB; 228376; -.
DR EnsemblPlants; AT1G74000.1; AT1G74000.1; AT1G74000.
DR GeneID; 843738; -.
DR Gramene; AT1G74000.1; AT1G74000.1; AT1G74000.
DR KEGG; ath:AT1G74000; -.
DR Araport; AT1G74000; -.
DR TAIR; locus:2031511; AT1G74000.
DR eggNOG; KOG1520; Eukaryota.
DR HOGENOM; CLU_023267_2_1_1; -.
DR OMA; AYMTESS; -.
DR OrthoDB; 757814at2759; -.
DR PhylomeDB; P92976; -.
DR BioCyc; ARA:AT1G74000-MON; -.
DR UniPathway; UPA00311; UER00447.
DR PRO; PR:P92976; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P92976; baseline and differential.
DR Genevisible; P92976; AT.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0016844; F:strictosidine synthase activity; ISS:TAIR.
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 Pfam; PF03088; Str_synth; 1.
PE 2: Evidence at transcript level;
KW Alkaloid metabolism; Glycoprotein; Lyase; Reference proteome; Signal;
KW Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..329
FT /note="Protein STRICTOSIDINE SYNTHASE-LIKE 11"
FT /id="PRO_0000033331"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 54..55
FT /note="YT -> LP (in Ref. 1; AAB40595)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="T -> N (in Ref. 1; AAB40595)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="E -> D (in Ref. 1; AAB40595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 34667 MW; C549547884B6E1C1 CRC64;
MMRSFVSLIS LLLLLSFSSS VLSTKKSSFQ KLPVPGNRTG PEAFAFDSTG KGFYTGVTGG
KILKYLPKKG YVDFAQITNS SKSSLCDGAL GTTNVEKCGR PAGIAFNTKT GDLYVADAAL
GLHVIPRRGG LAKKIADSVG GKPFLFLDGL DVDPTTGVVY FTSFSSTFGP RDVLKAVATK
DSTGKFFKYD PSKKVVTVLM EGLSGSAGCA VSSDGSFVLV GQFTKSNIKR YWIKGSKAGT
SEDFTNSVSN PDNIKRIGST GNFWVASVVN SATGPTNPSA VKVSSAGKVL QTIPLKDKFG
DTLVSEVNEY KGQLYIGALF GPFAGILKL
