ID A0A0M0MS24_HELPX Unreviewed; 262 AA. AC A0A0M0MS24; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 16-JAN-2019, entry version 21. DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198}; DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198}; DE Short=PAPT {ECO:0000256|HAMAP-Rule:MF_00198}; DE AltName: Full=Spermidine synthase {ECO:0000256|HAMAP-Rule:MF_00198}; DE Short=SPDS {ECO:0000256|HAMAP-Rule:MF_00198}; DE Short=SPDSY {ECO:0000256|HAMAP-Rule:MF_00198}; DE EC=2.5.1.16 {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_0201680 GN {ECO:0000313|EMBL:OJZ94745.1}, CGC32_04720 GN {ECO:0000313|EMBL:ASM63926.1}; 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:OJZ94745.1, ECO:0000313|Proteomes:UP000053387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UM163R {ECO:0000313|EMBL:OJZ94745.1, 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 levofloxacin and metronidazole RT resistance on the compensatory response."; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ASM63926.1, ECO:0000313|Proteomes:UP000199724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G272 {ECO:0000313|EMBL:ASM63926.1, RC ECO:0000313|Proteomes:UP000199724}; RA Wang Q.; RT "Genomic analysis of a multidrug - resistant strain of Helicobacter RT pylori."; RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:ASM63926.1, ECO:0000313|Proteomes:UP000199724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G272 {ECO:0000313|EMBL:ASM63926.1, RC ECO:0000313|Proteomes:UP000199724}; RA Sun Z.S., Albrecht U., Echele G., Lee C.C.; RL Submitted (JUL-2017) 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: CC Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = CC H(+) + S-methyl-5'-thioadenosine + spermidine; CC Xref=Rhea:RHEA:12721, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, CC ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; CC EC=2.5.1.16; Evidence={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 -!- SIMILARITY: Belongs to the spermidine/spermine synthase family. CC {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- CAUTION: Lacks the conserved Asp active site. {ECO:0000256|HAMAP- CC Rule:MF_00198}. 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; CP022409; ASM63926.1; -; Genomic_DNA. DR EMBL; LFJR01000014; KOO65956.1; -; Genomic_DNA. DR EMBL; LLVX02000002; OJZ94745.1; -; Genomic_DNA. DR RefSeq; WP_000265047.1; NZ_MVVA01000003.1. DR EnsemblBacteria; KOO65956; KOO65956; AK968_07015. DR PATRIC; fig|210.1964.peg.1108; -. DR UniPathway; UPA00248; UER00314. DR Proteomes; UP000037452; Unassembled WGS sequence. DR Proteomes; UP000053387; Unassembled WGS sequence. DR Proteomes; UP000199724; Chromosome. 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 HAMAP; MF_00198; Spermidine_synth; 1. DR InterPro; IPR030374; PABS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR001045; Spermi_synthase. DR InterPro; IPR035246; Spermidine_synt_N. DR InterPro; IPR037163; Spermidine_synt_N_sf. DR Pfam; PF17284; Spermine_synt_N; 1. 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, ECO:0000313|Proteomes:UP000199724}; KW Polyamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198, KW ECO:0000256|PROSITE-ProRule:PRU00354}; KW Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00198, ECO:0000256|PROSITE- KW ProRule:PRU00354, ECO:0000313|EMBL:KOO65956.1}. FT DOMAIN 1 249 PABS. {ECO:0000259|PROSITE:PS51006}. FT ACT_SITE 155 155 Proton acceptor. {ECO:0000256|PROSITE- FT ProRule:PRU00354}. 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 //