SPEE_SYNE7
ID SPEE_SYNE7 Reviewed; 286 AA.
AC Q31QK9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Synpcc7942_0628;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
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., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 2-285 IN COMPLEXES WITH
RP PUTRESCINE; SPERMIDINE AND S-METHYL-5'-THIOADENOSINE, AND HOMODIMER.
RX PubMed=30877192; DOI=10.1042/bcj20180811;
RA Guedez G., Pothipongsa A., Siren S., Liljeblad A., Jantaro S.,
RA Incharoensakdi A., Salminen T.A.;
RT "Crystal structure of dimeric Synechococcus spermidine synthase with bound
RT polyamine substrate and product.";
RL Biochem. J. 476:1009-1020(2019).
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 (By similarity). Homodimer
CC (PubMed:30877192). {ECO:0000255|HAMAP-Rule:MF_00198,
CC ECO:0000269|PubMed:30877192}.
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; CP000100; ABB56660.1; -; Genomic_DNA.
DR RefSeq; WP_011243208.1; NC_007604.1.
DR PDB; 6QMM; X-ray; 2.18 A; A/B=2-285.
DR PDBsum; 6QMM; -.
DR AlphaFoldDB; Q31QK9; -.
DR SMR; Q31QK9; -.
DR STRING; 1140.Synpcc7942_0628; -.
DR PRIDE; Q31QK9; -.
DR EnsemblBacteria; ABB56660; ABB56660; Synpcc7942_0628.
DR KEGG; syf:Synpcc7942_0628; -.
DR eggNOG; COG0421; Bacteria.
DR HOGENOM; CLU_048199_0_0_3; -.
DR OMA; LWPGQSF; -.
DR OrthoDB; 1613081at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0628-MON; -.
DR BRENDA; 2.5.1.16; 7781.
DR UniPathway; UPA00248; UER00314.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Polyamine biosynthesis; Spermidine biosynthesis;
KW Transferase.
FT CHAIN 1..286
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_1000197479"
FT DOMAIN 6..239
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 34
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|PubMed:30877192, ECO:0007744|PDB:6QMM"
FT BINDING 65
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|PubMed:30877192, ECO:0007744|PDB:6QMM"
FT BINDING 89
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|PubMed:30877192, ECO:0007744|PDB:6QMM"
FT BINDING 109
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|PubMed:30877192, ECO:0007744|PDB:6QMM"
FT BINDING 140..141
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|PubMed:30877192, ECO:0007744|PDB:6QMM"
FT BINDING 159..162
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:30877192,
FT ECO:0007744|PDB:6QMM"
FT BINDING 166
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|PubMed:30877192, ECO:0007744|PDB:6QMM"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:6QMM"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 17..30
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:6QMM"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:6QMM"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 183..194
FT /evidence="ECO:0007829|PDB:6QMM"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:6QMM"
FT STRAND 230..240
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:6QMM"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:6QMM"
SQ SEQUENCE 286 AA; 31851 MW; 6B2042388692D9CD CRC64;
MSADAPVWID EVFEDRVRYG LRGQILWEET SPFQKITIVD TEHYGRGLLL DDCWMTAERC
EVCYHEYLVH PPLTTAASIA RVLVIGGGDG GTVREVLRYA EVEQVDLVEI DGRVVELSQE
YLGAIGTAWA DPRLNVKIGD GIAFVQTAPD ASYDVILVDG SDPAGPAAGL FNREFYENCR
RVLKPGGVFA SQAESPDSFL AVHLEMIETL SAVFAEAKPY YGWVPMYPSG WWSWLYASDT
PGQFQKPQSD RLAAIEPQVE IYNRDIHQAA FAQPNFVRRG LSARQG
