SPSY_YEAST
ID SPSY_YEAST Reviewed; 300 AA.
AC Q12455; D6VYE0; Q2VQW3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Spermine synthase SPE4;
DE Short=SPMSY;
DE EC=2.5.1.22 {ECO:0000269|PubMed:9573363};
DE AltName: Full=Spermidine aminopropyltransferase;
GN Name=SPE4; OrderedLocusNames=YLR146C; ORFNames=L9634.5;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=2602;
RX PubMed=9573363; DOI=10.1016/s0378-1119(98)00027-4;
RA Hamasaki-Katagiri N., Katagiri Y., Tabor C.W., Tabor H.;
RT "Spermine is not essential for growth of Saccharomyces cerevisiae:
RT identification of the SPE4 gene (spermine synthase) and characterization of
RT a spe4 deletion mutant.";
RL Gene 210:195-201(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-82.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=15905473; DOI=10.1093/nar/gki583;
RA Zhang Z., Dietrich F.S.;
RT "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT SAGE.";
RL Nucleic Acids Res. 33:2838-2851(2005).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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:9573363};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermine biosynthesis;
CC spermine from spermidine: step 1/1. {ECO:0000305|PubMed:9573363}.
CC -!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
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DR EMBL; AF067970; AAC19368.1; -; Genomic_DNA.
DR EMBL; Z73318; CAA97718.1; -; Genomic_DNA.
DR EMBL; U53879; AAB82380.1; -; Genomic_DNA.
DR EMBL; AY899255; AAX83940.1; -; mRNA.
DR EMBL; BK006945; DAA09456.1; -; Genomic_DNA.
DR PIR; S64995; S64995.
DR RefSeq; NP_013247.1; NM_001182033.1.
DR AlphaFoldDB; Q12455; -.
DR SMR; Q12455; -.
DR BioGRID; 31415; 111.
DR DIP; DIP-4811N; -.
DR IntAct; Q12455; 2.
DR MINT; Q12455; -.
DR STRING; 4932.YLR146C; -.
DR iPTMnet; Q12455; -.
DR MaxQB; Q12455; -.
DR PaxDb; Q12455; -.
DR PRIDE; Q12455; -.
DR EnsemblFungi; YLR146C_mRNA; YLR146C; YLR146C.
DR GeneID; 850838; -.
DR KEGG; sce:YLR146C; -.
DR SGD; S000004136; SPE4.
DR VEuPathDB; FungiDB:YLR146C; -.
DR eggNOG; KOG1562; Eukaryota.
DR GeneTree; ENSGT00870000136521; -.
DR HOGENOM; CLU_048199_1_0_1; -.
DR InParanoid; Q12455; -.
DR OMA; HEMVAHP; -.
DR BioCyc; MetaCyc:YLR146C-MON; -.
DR BioCyc; YEAST:YLR146C-MON; -.
DR UniPathway; UPA00249; UER00315.
DR PRO; PR:Q12455; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12455; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016768; F:spermine synthase activity; IMP:SGD.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IMP:SGD.
DR GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006597; P:spermine biosynthetic process; IMP:SGD.
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 Phosphoprotein; Polyamine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..300
FT /note="Spermine synthase SPE4"
FT /id="PRO_0000156540"
FT DOMAIN 12..255
FT /note="PABS"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
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 119
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 151..152
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 300 AA; 34091 MW; FE7FE6EE308F3CC9 CRC64;
MVNNSQHPYI KDGWFREIND KSFPGQAFTM TVDSILYEAR SEFQDILIFR NKVYGTVLVL
DGIVQCTEFD EFAYQEMITH IAMFAHSNPK RVLIIGGGDG GVLREVAKHS CVEDITMVEI
DSSVIELSRK FLPTLSNGAF DDERLDLKLC DGFKFLQDIG ASDVHKKFDV IITDSSDPEG
PAEAFFQERY FELLKDALNP NGVVIMQSSE NFWLNLKYLH DLKNTAKKVF PNTEYCYTMV
PTYTSGQLGL IVCSNNANIP LNIPQRKISE QEQGKLKYYN PQIHSSAFVL PTWADKVINE
