SPDS2_ARATH
ID SPDS2_ARATH Reviewed; 340 AA.
AC O48661; O64606;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Spermidine synthase 2;
DE Short=SPDSY 2;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase 2;
GN Name=SPDSYN2; OrderedLocusNames=At1g70310; ORFNames=F17O7.16;
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. Columbia;
RA Franceschetti M., Michael A.J.;
RT "Plant aminopropyltransferase families.";
RL Submitted (NOV-1999) 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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-340.
RC STRAIN=cv. Columbia;
RX PubMed=9517003; DOI=10.1093/oxfordjournals.pcp.a029291;
RA Hashimoto T., Tamaki K., Suzuki K., Yamada Y.;
RT "Molecular cloning of plant spermidine synthases.";
RL Plant Cell Physiol. 39:73-79(1998).
RN [6]
RP INTERACTION WITH SPMS AND SPDSYN1.
RX PubMed=12368503; DOI=10.1105/tpc.004077;
RA Panicot M., Minguet E.G., Ferrando A., Alcazar R., Blazquez M.A.,
RA Carbonell J., Altabella T., Koncz C., Tiburcio A.F.;
RT "A polyamine metabolon involving aminopropyl transferase complexes in
RT Arabidopsis.";
RL Plant Cell 14:2539-2551(2002).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) +
CC S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16;
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1.
CC -!- SUBUNIT: Heterodimer. Component of a multiprotein complex. Interacts
CC with SPMS and SPDSYN1. {ECO:0000269|PubMed:12368503}.
CC -!- INTERACTION:
CC O48661; Q9ZUB3: SPDSYN1; NbExp=7; IntAct=EBI-1770100, EBI-1770123;
CC O48661; Q94BN2: SPMS; NbExp=4; IntAct=EBI-1770100, EBI-1770109;
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ251297; CAB61615.1; -; mRNA.
DR EMBL; AC003671; AAC18808.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35044.1; -; Genomic_DNA.
DR EMBL; AF375409; AAK52993.1; -; mRNA.
DR EMBL; AB006693; BAA24536.1; -; mRNA.
DR PIR; T01492; T01492.
DR RefSeq; NP_177188.1; NM_105699.4.
DR PDB; 6O64; X-ray; 2.00 A; A/B/C/D/E/F/G/H=39-340.
DR PDBsum; 6O64; -.
DR AlphaFoldDB; O48661; -.
DR SMR; O48661; -.
DR BioGRID; 28587; 10.
DR IntAct; O48661; 2.
DR STRING; 3702.AT1G70310.1; -.
DR iPTMnet; O48661; -.
DR PaxDb; O48661; -.
DR PRIDE; O48661; -.
DR ProteomicsDB; 228455; -.
DR EnsemblPlants; AT1G70310.1; AT1G70310.1; AT1G70310.
DR GeneID; 843367; -.
DR Gramene; AT1G70310.1; AT1G70310.1; AT1G70310.
DR KEGG; ath:AT1G70310; -.
DR Araport; AT1G70310; -.
DR TAIR; locus:2016129; AT1G70310.
DR eggNOG; KOG1562; Eukaryota.
DR HOGENOM; CLU_048199_3_2_1; -.
DR InParanoid; O48661; -.
DR OMA; KEPSCMS; -.
DR OrthoDB; 1059849at2759; -.
DR PhylomeDB; O48661; -.
DR BRENDA; 2.5.1.16; 399.
DR UniPathway; UPA00248; UER00314.
DR PRO; PR:O48661; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O48661; baseline and differential.
DR Genevisible; O48661; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0004766; F:spermidine synthase activity; IDA:TAIR.
DR GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0008295; P:spermidine biosynthetic process; IDA:TAIR.
DR Gene3D; 2.30.140.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR030373; PABS_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR InterPro; IPR030668; Spermi_synthase_euk.
DR InterPro; IPR035246; Spermidine_synt_N.
DR InterPro; IPR037163; Spermidine_synt_N_sf.
DR PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR PIRSF; PIRSF000502; Spermidine_synth; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Polyamine biosynthesis; Reference proteome;
KW Spermidine biosynthesis; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..340
FT /note="Spermidine synthase 2"
FT /id="PRO_0000156449"
FT DOMAIN 49..286
FT /note="PABS"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 186..187
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 205..208
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 48..50
FT /note="IPG -> TRP (in Ref. 5; BAA24536)"
FT /evidence="ECO:0000305"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 62..76
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:6O64"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 158..167
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:6O64"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:6O64"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:6O64"
FT HELIX 329..335
FT /evidence="ECO:0007829|PDB:6O64"
SQ SEQUENCE 340 AA; 37140 MW; 35704CE45ED4128F CRC64;
MSSTQEASVT DLPVKRPREA EEDNNGGAME TENGGGEIKE PSCMSSIIPG WFSEISPMWP
GEAHSLKVEK ILFQGKSDYQ DVIVFQSATY GKVLVLDGVI QLTERDECAY QEMITHLPLC
SISNPKKVLV IGGGDGGVLR EVARHSSVEQ IDICEIDKMV VDVAKQYFPN VAVGYEDPRV
NLIIGDGVAF LKNAAEGTYD AVIVDSSDPI GPAKELFEKP FFESVNRALR PGGVVCTQAE
SLWLHMDIIE DIVSNCRDIF KGSVNYAWTS VPTYPSGVIG FMLCSSEGPQ VDFKKPVSLI
DTDESSIKSH CPLKYYNAEI HSAAFCLPSF AKKVIDSKAN
