SPEE_DICDI
ID SPEE_DICDI Reviewed; 284 AA.
AC Q9XY92; Q55EL1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Spermidine synthase;
DE Short=SPDSY;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase;
GN Name=spsA; ORFNames=DDB_G0268630;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10209300; DOI=10.1016/s0167-4889(99)00018-x;
RA Guo K., Chang W.T., Newell P.C.;
RT "Isolation of spermidine synthase gene (spsA) of Dictyostelium
RT discoideum.";
RL Biochim. Biophys. Acta 1449:211-216(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the production of spermidine from putrescine and
CC decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference
CC for putrescine as substrate (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
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DR EMBL; AF069757; AAD32851.1; -; Genomic_DNA.
DR EMBL; AAFI02000004; EAL72904.1; -; Genomic_DNA.
DR RefSeq; XP_647009.1; XM_641917.1.
DR AlphaFoldDB; Q9XY92; -.
DR SMR; Q9XY92; -.
DR STRING; 44689.DDB0191167; -.
DR PaxDb; Q9XY92; -.
DR EnsemblProtists; EAL72904; EAL72904; DDB_G0268630.
DR GeneID; 8616702; -.
DR KEGG; ddi:DDB_G0268630; -.
DR dictyBase; DDB_G0268630; spsA.
DR eggNOG; KOG1562; Eukaryota.
DR HOGENOM; CLU_048199_1_0_1; -.
DR InParanoid; Q9XY92; -.
DR OMA; LWPGQSF; -.
DR PhylomeDB; Q9XY92; -.
DR Reactome; R-DDI-351202; Metabolism of polyamines.
DR UniPathway; UPA00248; UER00314.
DR PRO; PR:Q9XY92; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0036360; P:sorocarp stalk morphogenesis; IMP:dictyBase.
DR GO; GO:0008295; P:spermidine biosynthetic process; IMP:dictyBase.
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 3: Inferred from homology;
KW Polyamine biosynthesis; Reference proteome; Spermidine biosynthesis;
KW Transferase.
FT CHAIN 1..284
FT /note="Spermidine synthase"
FT /id="PRO_0000156447"
FT DOMAIN 6..241
FT /note="PABS"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 143..144
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 161..164
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT CONFLICT 39
FT /note="F -> I (in Ref. 1; AAD32851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 31724 MW; ACF8EE78C13D4FF0 CRC64;
MDKIQNGWFS EISEFWPGNS FSLEVEKVLH HEKSEYQDFL VFKSKSFGNV LVLDGVIQAT
ERDEFAYQEM ITHIPLFSHP SPKRVLVVGG GDGGVLREVV KHPLVESVTL CEIDKGVIEA
SRNFLPNMRV GFDHPKVTLF IGDGMEFMRQ RKGEFDVIIT DSSDPIGPAQ GLFERAYYEL
LKAALAPGGI VCSQCESMWL HLDTIKGLTT FCKELYPNVE YAYTSIPSYP GGSIGFILCS
LGGSTKAPIR EITPEVQSQM QYYNGEVHKA SFVLPQFAAK KLNL
