ID A0A0M0MS24_HELPX Unreviewed; 262 AA. AC A0A0M0MS24; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 06-JUL-2016, entry version 7. DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198}; DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198}; DE AltName: Full=Spermidine synthase {ECO:0000256|HAMAP-Rule:MF_00198}; GN Name=speE {ECO:0000256|HAMAP-Rule:MF_00198, GN ECO:0000313|EMBL:KOO65956.1}; GN ORFNames=AK968_07015 {ECO:0000313|EMBL:KOO65956.1}, AP069_05455 GN {ECO:0000313|EMBL:KUG65205.1}; OS Helicobacter pylori (Campylobacter pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210 {ECO:0000313|EMBL:KOO65956.1, ECO:0000313|Proteomes:UP000037452}; RN [1] {ECO:0000313|Proteomes:UP000037452} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UM163 {ECO:0000313|Proteomes:UP000037452}; RA Loke M.F., Vadivelu J., Tay A.C.Y., Thirriot F., Lee W.C., Goh K.L., RA Teh X.; RT "In silico identification of multidrug resistance associated genes in RT Helicobacter pylori strains based on comparative genomics approach."; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KOO65956.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UM163 {ECO:0000313|EMBL:KOO65956.1}; RA Hoefler B.C., Straight P.D.; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KUG65205.1, ECO:0000313|Proteomes:UP000053387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UM163R {ECO:0000313|EMBL:KUG65205.1, RC ECO:0000313|Proteomes:UP000053387}; RA Loke M.F., Vadivelu J., Tay A.C.Y., Thirriot F., Lee W.C., Goh K.L., RA Hanafi A.; RT "The effects of Helicobacter pylori antibiotic resistance on RT compensatory response."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine CC group from the amino donor S-adenosylmethioninamine (decarboxy- CC AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. CC {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine + CC putrescine = 5'-S-methyl-5'-thioadenosine + spermidine. CC {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine CC biosynthesis; spermidine from putrescine: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP- CC Rule:MF_00198}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family. CC {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- SIMILARITY: Contains 1 PABS (polyamine biosynthesis) domain. CC {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- CAUTION: Lacks the conserved Asp active site. {ECO:0000256|HAMAP- CC Rule:MF_00198}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOO65956.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LFJR01000014; KOO65956.1; -; Genomic_DNA. DR EMBL; LLVX01000016; KUG65205.1; -; Genomic_DNA. DR RefSeq; WP_000265047.1; NZ_LLVX01000016.1. DR EnsemblBacteria; KOO65956; KOO65956; AK968_07015. DR UniPathway; UPA00248; UER00314. DR Proteomes; UP000037452; Unassembled WGS sequence. DR Proteomes; UP000053387; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00198; Spermidine_synth; 1. DR InterPro; IPR030374; PABS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR001045; Spermi_synthase. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51006; PABS_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037452, KW ECO:0000313|Proteomes:UP000053387}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00198}; KW Polyamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198}; KW Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00198, KW ECO:0000313|EMBL:KOO65956.1}. FT DOMAIN 1 249 PABS (polyamine biosynthesis). FT {ECO:0000259|PROSITE:PS51006}. FT ACT_SITE 155 155 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00198}. FT BINDING 29 29 S-adenosylmethioninamine. FT {ECO:0000256|HAMAP-Rule:MF_00198}. FT BINDING 83 83 Polyamine. {ECO:0000256|HAMAP-Rule: FT MF_00198}. SQ SEQUENCE 262 AA; 30541 MW; 6DD2681A471C435F CRC64; MWITQEITPY LRKEYTIEAK LLDVRSEHNI LEIFKSKDFG EIAMLNCQLL FKNFLHIESE LLAHMGGCTK KELKEVLIVD GFDLELAHQL FKYDTHIDFV QADEKILDSF ISFFPHFHEV KNNKNFTHAK QLLDLDIKKY DLILCLQEPD IHKIDGLKRM LKEDGVFISV AKHPLLEHVS MQNALKNMGE FFSVAMPFVA PLRILSNKGY IYASFKTHPL KDLMAPKIEA LKSVRYYNED IHRAAFALPK NLQEVFKDNI KS //