SPSY_ARATH
ID SPSY_ARATH Reviewed; 359 AA.
AC Q94BN2; B9DFL7; Q8LBG3; Q944S0; Q9FGM4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Spermine synthase;
DE Short=SPMSY;
DE EC=2.5.1.22;
DE AltName: Full=Spermidine aminopropyltransferase;
GN Name=SPMS; Synonyms=SPDS3; OrderedLocusNames=At5g53120; ORFNames=MFH8.5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION, INDUCTION BY ABSCISIC ACID, AND TISSUE SPECIFICITY.
RX PubMed=12220656; DOI=10.1016/s0014-5793(02)03217-9;
RA Hanzawa Y., Imai A., Michael A.J., Komeda Y., Takahashi T.;
RT "Characterization of the spermidine synthase-related gene family in
RT Arabidopsis thaliana.";
RL FEBS Lett. 527:176-180(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH SPDSYN1 AND SPDSYN2.
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 [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17560575; DOI=10.1016/j.febslet.2007.05.074;
RA Knott J.M., Romer P., Sumper M.;
RT "Putative spermine synthases from Thalassiosira pseudonana and Arabidopsis
RT thaliana synthesize thermospermine rather than spermine.";
RL FEBS Lett. 581:3081-3086(2007).
RN [9]
RP INDUCTION BY SALT.
RX PubMed=20137962; DOI=10.1016/j.plaphy.2010.01.013;
RA Naka Y., Watanabe K., Sagor G.H., Niitsu M., Pillai M.A., Kusano T.,
RA Takahashi Y.;
RT "Quantitative analysis of plant polyamines including thermospermine during
RT growth and salinity stress.";
RL Plant Physiol. Biochem. 48:527-533(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) +
CC S-methyl-5'-thioadenosine + spermine; Xref=Rhea:RHEA:19973,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:45725,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:57834; EC=2.5.1.22;
CC Evidence={ECO:0000269|PubMed:17560575};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermine biosynthesis;
CC spermine from spermidine: step 1/1.
CC -!- SUBUNIT: Heterodimer. Component of a multiprotein complex. Interacts
CC with SPDSYN1 and SPDSYN2. {ECO:0000269|PubMed:12368503}.
CC -!- INTERACTION:
CC Q94BN2; Q9ZUB3: SPDSYN1; NbExp=4; IntAct=EBI-1770109, EBI-1770123;
CC Q94BN2; O48661: SPDSYN2; NbExp=4; IntAct=EBI-1770109, EBI-1770100;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q94BN2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in stem internodes, flower
CC buds and roots. {ECO:0000269|PubMed:12220656}.
CC -!- INDUCTION: Up-regulated by abscisic acid and salt stress.
CC {ECO:0000269|PubMed:12220656, ECO:0000269|PubMed:20137962}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64782.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB08415.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025622; BAB08415.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96305.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96306.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96307.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96308.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96309.1; -; Genomic_DNA.
DR EMBL; AF424571; AAL11565.1; -; mRNA.
DR EMBL; AY040013; AAK64170.1; -; mRNA.
DR EMBL; AY079367; AAL85098.1; -; mRNA.
DR EMBL; BT000742; AAN31883.1; -; mRNA.
DR EMBL; AK316822; BAH19534.1; -; mRNA.
DR EMBL; AY087226; AAM64782.1; ALT_INIT; mRNA.
DR RefSeq; NP_001078748.1; NM_001085279.1. [Q94BN2-1]
DR RefSeq; NP_001078749.1; NM_001085280.1. [Q94BN2-1]
DR RefSeq; NP_568785.1; NM_124691.3. [Q94BN2-1]
DR RefSeq; NP_851178.1; NM_180847.2. [Q94BN2-1]
DR RefSeq; NP_851179.1; NM_180848.3. [Q94BN2-1]
DR AlphaFoldDB; Q94BN2; -.
DR SMR; Q94BN2; -.
DR BioGRID; 20637; 4.
DR IntAct; Q94BN2; 2.
DR STRING; 3702.AT5G53120.6; -.
DR PRIDE; Q94BN2; -.
DR EnsemblPlants; AT5G53120.1; AT5G53120.1; AT5G53120. [Q94BN2-1]
DR EnsemblPlants; AT5G53120.2; AT5G53120.2; AT5G53120. [Q94BN2-1]
DR EnsemblPlants; AT5G53120.3; AT5G53120.3; AT5G53120. [Q94BN2-1]
DR EnsemblPlants; AT5G53120.4; AT5G53120.4; AT5G53120. [Q94BN2-1]
DR EnsemblPlants; AT5G53120.5; AT5G53120.5; AT5G53120. [Q94BN2-1]
DR GeneID; 835392; -.
DR Gramene; AT5G53120.1; AT5G53120.1; AT5G53120. [Q94BN2-1]
DR Gramene; AT5G53120.2; AT5G53120.2; AT5G53120. [Q94BN2-1]
DR Gramene; AT5G53120.3; AT5G53120.3; AT5G53120. [Q94BN2-1]
DR Gramene; AT5G53120.4; AT5G53120.4; AT5G53120. [Q94BN2-1]
DR Gramene; AT5G53120.5; AT5G53120.5; AT5G53120. [Q94BN2-1]
DR KEGG; ath:AT5G53120; -.
DR Araport; AT5G53120; -.
DR eggNOG; KOG1562; Eukaryota.
DR HOGENOM; CLU_048199_3_0_1; -.
DR InParanoid; Q94BN2; -.
DR PhylomeDB; Q94BN2; -.
DR UniPathway; UPA00249; UER00315.
DR PRO; PR:Q94BN2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94BN2; baseline and differential.
DR Genevisible; Q94BN2; AT.
DR GO; GO:0004766; F:spermidine synthase activity; IBA:GO_Central.
DR GO; GO:0016768; F:spermine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006597; P:spermine biosynthetic process; IEA:UniProtKB-UniPathway.
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 Alternative splicing; Polyamine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..359
FT /note="Spermine synthase"
FT /id="PRO_0000397673"
FT DOMAIN 53..304
FT /note="PABS"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 205..206
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT CONFLICT 40
FT /note="V -> E (in Ref. 4; BAH19534)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="G -> S (in Ref. 5; AAM64782)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="D -> N (in Ref. 3; AAL11565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39239 MW; 5251D28EBB98865D CRC64;
MEGDVGIGLV CQNTMDGKAS NGNGLEKTVP SCCLKAMACV PEDDAKCHST VVSGWFSEPH
PRSGKKGGKA VYFNNPMWPG EAHSLKVEKV LFKDKSDFQE VLVFESATYG KVLVLDGIVQ
LTEKDECAYQ EMIAHLPLCS ISSPKNVLVV GGGDGGVLRE ISRHSSVEVI DICEIDKMVI
DVSKKFFPEL AVGFDDPRVQ LHIGDAAEFL RKSPEGKYDA IIVDSSDPVG PALALVEKPF
FETLARALKP GGVLCNMAES MWLHTHLIED MISICRQTFK SVHYAWSSVP TYPSGVIGFV
LCSTEGPAVD FKNPINPIEK LDGAMTHKRE LKFYNSDMHR AAFALPTFLR REVASLLAS
