SPEE2_RALSO
ID SPEE2_RALSO Reviewed; 510 AA.
AC Q8XQC5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Polyamine aminopropyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Putrescine aminopropyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=PAPT 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine synthase 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDS 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDSY 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198};
GN Name=speE2 {ECO:0000255|HAMAP-Rule:MF_00198}; Synonyms=speE1;
GN OrderedLocusNames=RSp1337; ORFNames=RS04762;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG Plasmid megaplasmid Rsp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00198};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|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; AL646053; CAD18488.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8XQC5; -.
DR SMR; Q8XQC5; -.
DR STRING; 267608.RSp1337; -.
DR EnsemblBacteria; CAD18488; CAD18488; RSp1337.
DR KEGG; rso:RSp1337; -.
DR eggNOG; COG4262; Bacteria.
DR HOGENOM; CLU_034289_1_0_4; -.
DR OMA; SFGEWGY; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000001436; Plasmid megaplasmid Rsp.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Plasmid; Polyamine biosynthesis;
KW Reference proteome; Spermidine biosynthesis; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..510
FT /note="Polyamine aminopropyltransferase 2"
FT /id="PRO_0000156500"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT DOMAIN 205..449
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT REGION 207..456
FT /note="Spermidine synthase"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 244
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 274
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 298
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 318
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 352..353
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 510 AA; 56611 MW; 1814AE8BDA2A56AB CRC64;
MNRGNALLVL AVFVVASCGL AYELIAGALA SYLLGDSILQ FSSIIGAYLF AMGIGSWVSR
YVADDALLAR FVDLELLVGL FGGVSAAALF LLFALESAPF RLVLYALVTV IGVLVGMEIP
LVMRMLHRRQ AKFSDLVSRV LTFDYLGALA VSLLFPLVLA PRLGLVRTGF LFGLCNTAIA
VWTLWHFRAE LGLSARLRGA MAWRAGMVGA ALLAGFAASD RLTHWSERAL FGDEIIHAIS
SPYQRLVVTR WKDDLRLYIN GNLQFSSRDE YRYHEALVLP ALESVRGARR VLVLGGGDGL
ALRQILKYPQ VEHVTLVDLD PRMTSLFSHA EALVALNQHA FSDPRVTVVN ADAGQWLQTA
ADMFDVAIVD FPDPSNFSIG KLYSVPFYRL LSRHVADTGL VVIQATSPYF APRSYWCVDA
TLKEAGYRTW PYHALVPSFG EWGFILAAPG RADFRPPTTY RVPTRFLDAD TTHQMFSFAP
DMPRPQVEPN RLNNQSLVRY FEEDWHGVLR
