SPEE_YEAST
ID SPEE_YEAST Reviewed; 293 AA.
AC Q12074; D6W473;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Spermidine synthase SPE3 {ECO:0000303|PubMed:9073064};
DE Short=SPDSY;
DE EC=2.5.1.16 {ECO:0000269|PubMed:9073064};
DE AltName: Full=Putrescine aminopropyltransferase;
GN Name=SPE3; OrderedLocusNames=YPR069C; ORFNames=YP9499.24C;
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.
RX PubMed=9073064; DOI=10.1016/s0378-1119(96)00660-9;
RA Hamasaki-Katagiri N., Tabor C.W., Tabor H.;
RT "Spermidine biosynthesis in Saccharomyces cerevisae: polyamine requirement
RT of a null mutant of the SPE3 gene (spermidine synthase).";
RL Gene 187:35-43(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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).
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 Evidence={ECO:0000269|PubMed:9073064};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12722;
CC Evidence={ECO:0000305|PubMed:9073064};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000305|PubMed:9073064}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
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DR EMBL; U27519; AAC17191.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94977.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89186.1; -; Genomic_DNA.
DR EMBL; U51033; AAB68120.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11489.1; -; Genomic_DNA.
DR PIR; S54090; S54090.
DR RefSeq; NP_015394.1; NM_001184166.1.
DR AlphaFoldDB; Q12074; -.
DR SMR; Q12074; -.
DR BioGRID; 36241; 321.
DR DIP; DIP-6618N; -.
DR IntAct; Q12074; 5.
DR MINT; Q12074; -.
DR STRING; 4932.YPR069C; -.
DR iPTMnet; Q12074; -.
DR MaxQB; Q12074; -.
DR PaxDb; Q12074; -.
DR PRIDE; Q12074; -.
DR EnsemblFungi; YPR069C_mRNA; YPR069C; YPR069C.
DR GeneID; 856182; -.
DR KEGG; sce:YPR069C; -.
DR SGD; S000006273; SPE3.
DR VEuPathDB; FungiDB:YPR069C; -.
DR eggNOG; KOG1562; Eukaryota.
DR GeneTree; ENSGT00870000136521; -.
DR HOGENOM; CLU_048199_1_0_1; -.
DR InParanoid; Q12074; -.
DR OMA; LWPGQSF; -.
DR BioCyc; MetaCyc:YPR069C-MON; -.
DR BioCyc; YEAST:YPR069C-MON; -.
DR Reactome; R-SCE-351202; Metabolism of polyamines.
DR UniPathway; UPA00248; UER00314.
DR PRO; PR:Q12074; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12074; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004766; F:spermidine 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:0008295; P:spermidine 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 Polyamine biosynthesis; Reference proteome; Spermidine biosynthesis;
KW Transferase.
FT CHAIN 1..293
FT /note="Spermidine synthase SPE3"
FT /id="PRO_0000156462"
FT DOMAIN 12..248
FT /note="PABS"
FT ACT_SITE 168
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 74
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 75
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 150..151
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 168..171
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 33324 MW; 5B1B361E084ED09F CRC64;
MAQEITHPTI VDGWFREISD TMWPGQAMTL KVEKVLHHEK SKYQDVLIFK STTYGNVLVL
DNVIQATERD EFAYQEMIAH LALNSHPNPK KVLVIGGGDG GVLREVVKHD SVEEAWLCDI
DEAVIRLSKE YLPEMAASYS HPKVKTHIGD GFQFLRDYQN TFDVIITDSS DPEGPAETLF
QKEYFQLLNS ALTEKGVITT QAESMWIHLP IIKDLKKACS EVFPVAEYSF VTIPTYPTGT
IGFMVCSKDK TCNVKKPLRE ISDEKEAELY RYYNKKIHEA SFVLPTWAAK ELN
