ID A0A7U9K673_MYCTX Unreviewed; 504 AA. AC A0A7U9K673; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, 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 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:GAA46272.1}; GN ORFNames=NCGM2209_2908 {ECO:0000313|EMBL:GAA46272.1}; OS Mycobacterium tuberculosis NCGM2209. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=1078763 {ECO:0000313|EMBL:GAA46272.1}; RN [1] {ECO:0000313|EMBL:GAA46272.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCGM2209 {ECO:0000313|EMBL:GAA46272.1}; RX PubMed=22072647; DOI=10.1128/JB.06233-11; RA Miyoshi-Akiyama T., Matsumura K., Kobayashi N., Maeda S., Kirikae T.; RT "Genome Sequence of Clinical Isolate Mycobacterium tuberculosis NCGM2209."; RL J. Bacteriol. 193:6792-6792(2011). RN [2] {ECO:0000313|EMBL:GAA46272.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCGM2209 {ECO:0000313|EMBL:GAA46272.1}; RA Akiyama T., Matsumura K., Kirikae T.; RL Submitted (SEP-2011) 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:0000256|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:0000256|HAMAP-Rule:MF_00198}; CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis; CC spermidine from putrescine: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_00198}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00198}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family. CC {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|HAMAP-Rule:MF_00198}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; DF126614; GAA46272.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7U9K673; -. DR UniPathway; UPA00248; UER00314. DR Proteomes; UP000004702; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; 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; 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 SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS01330; PABS_1; 1. DR PROSITE; PS51006; PABS_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00198}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00198}; KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP- KW Rule:MF_00198}; Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00198}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00198}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00198}. FT TRANSMEM 34..53 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" FT TRANSMEM 60..85 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" FT TRANSMEM 97..121 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" FT TRANSMEM 141..159 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" FT TRANSMEM 165..187 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" FT TRANSMEM 196..215 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" FT DOMAIN 212..446 FT /note="PABS" FT /evidence="ECO:0000259|PROSITE:PS51006" FT ACT_SITE 367 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198, FT ECO:0000256|PROSITE-ProRule:PRU00354" FT BINDING 242 FT /ligand="S-methyl-5'-thioadenosine" FT /ligand_id="ChEBI:CHEBI:17509" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" FT BINDING 294 FT /ligand="spermidine" FT /ligand_id="ChEBI:CHEBI:57834" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" FT BINDING 314 FT /ligand="S-methyl-5'-thioadenosine" FT /ligand_id="ChEBI:CHEBI:17509" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" FT BINDING 346..347 FT /ligand="S-methyl-5'-thioadenosine" FT /ligand_id="ChEBI:CHEBI:17509" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198" SQ SEQUENCE 504 AA; 52625 MW; 037AEDF156ED9972 CRC64; MLLAAVAACA ACGLVYELAL LTLAASLNGG GIVATSLIVA GYIAALGAGA LLIKPLLAHA AIAFIAVEAV LGIIGGLSAA ALYAAFAFLD ELDGSTLVLA VGTALIGGLV GAEVPLLMTL LQRGRVAGAA DAGRTLANLN AADYLGALVG GLAWPFLLLP QLGMIRGAAV TGIVNLAAAG VVSIFLLRHV VSGRQLVTAL CALAAALGLI ATLLVHSHDI ETTGRQQLYA DPIIAYRHSA YQEIVVTRRG DDLRLYLDGG LQFCTRDEYR YTESLVYPAV SDGARSVLVL GGGDGLAARE LLRQPGIEQI VQVELDPAVI ELARTTLRDV NAGSLDNPRV HVVIDDAMSW LRGAAVPPAG FDAVIVDLRD PDTPVLGRLY STEFYALAAR ALAPGGLMVV QAGSPYSTPT AFWRIISTIR SAGYAVTPYH VHVPTFGDWG FALARLTDIA PTPAVPSTAP ALRFLDQQVL EAATVFSGDI RPRTLDPSTL DNPHIVEDMR HGWD //