SPEE_PROM9
ID SPEE_PROM9 Reviewed; 283 AA.
AC Q317V6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198};
GN OrderedLocusNames=PMT9312_1778;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine group
CC from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to
CC putrescine (1,4-diaminobutane) to yield spermidine. {ECO:0000255|HAMAP-
CC Rule:MF_00198}.
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:0000255|HAMAP-Rule:MF_00198};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00198}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
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DR EMBL; CP000111; ABB50839.1; -; Genomic_DNA.
DR RefSeq; WP_011377320.1; NC_007577.1.
DR AlphaFoldDB; Q317V6; -.
DR SMR; Q317V6; -.
DR STRING; 74546.PMT9312_1778; -.
DR EnsemblBacteria; ABB50839; ABB50839; PMT9312_1778.
DR KEGG; pmi:PMT9312_1778; -.
DR eggNOG; COG0421; Bacteria.
DR HOGENOM; CLU_048199_0_0_3; -.
DR OMA; LWPGQSF; -.
DR OrthoDB; 1613081at2; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000002715; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR035246; Spermidine_synt_N.
DR InterPro; IPR037163; Spermidine_synt_N_sf.
DR PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Polyamine biosynthesis; Spermidine biosynthesis; Transferase.
FT CHAIN 1..283
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_1000012009"
FT DOMAIN 5..238
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 32
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 63
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 87
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 107
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 139..140
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 158..161
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 283 AA; 32780 MW; EBCBCA73D26BFC23 CRC64;
MTHISTWIDE YHKGSRFGLN GEILIKQNSK YQEIIVIENE YYGRALMLDG CWMTSLKDEK
YYHECLVHPA LSSIDEKSNV LIIGGGDGGT ARECVKYPQI SKIDLVEIDE EVIKISKKFL
KEIGGEAWSD KRLKIHIDDG VQWVKKTRDN FYDVIFIDCS DPSELSNLLF SDSFYRECKR
ILTKNGILAT QSESPESFKN IHISILKTLK KFFRVSETMY SFVPIYPSGI WSWTFASEEV
LHLSKRNCNE ALRIEKSCEI WNLNFQNAAF KMMPNKIVKE LNS
