GenomeNet

Database: UniProt
Entry: A0A147J935_9SPHN
LinkDB: A0A147J935_9SPHN
Original site: A0A147J935_9SPHN 
ID   A0A147J935_9SPHN        Unreviewed;       505 AA.
AC   A0A147J935;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ORFNames=NS258_08375 {ECO:0000313|EMBL:KTW13780.1};
OS   Sphingomonas sanguinis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=33051 {ECO:0000313|EMBL:KTW13780.1, ECO:0000313|Proteomes:UP000074410};
RN   [1] {ECO:0000313|EMBL:KTW13780.1, ECO:0000313|Proteomes:UP000074410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS258 {ECO:0000313|EMBL:KTW13780.1,
RC   ECO:0000313|Proteomes:UP000074410};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTW13780.1}.
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; LDTC01000059; KTW13780.1; -; Genomic_DNA.
DR   RefSeq; WP_058716633.1; NZ_LDTC01000059.1.
DR   AlphaFoldDB; A0A147J935; -.
DR   PATRIC; fig|33051.5.peg.2659; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000074410; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR   PANTHER; PTHR43317:SF1; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR   Pfam; PF01564; Spermine_synth; 1.
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};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW   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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   TRANSMEM        75..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   TRANSMEM        104..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   TRANSMEM        139..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   TRANSMEM        168..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   TRANSMEM        199..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   DOMAIN          213..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         241
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         271
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         295
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         315
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         349..350
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ   SEQUENCE   505 AA;  55080 MW;  D363F76D3EC4455C CRC64;
     MSQTVPPPRA GAALLLSAFV VATCGLVYEL LAGTLASYLL GDSVTQFSTV IGTYLFAMGI
     GSWCSRYVRR DELAVFVRVE ILVAVIGGSS AALLFLLFDR VADFRLPLYG IVLAIGTLVG
     LEIPLLMRIL KDRLDFGDLV SRVLTFDYIG ALAASLLFPL LLVPKLGLIR TGFLFGLFNV
     AVAIALILRL PGRRLRGELA VAIAVAFGLL AGFLWSERLQ RTAEIAAYGD PIVYAASTPY
     QRIVITKRSD DLRLFLSGNL QFSSRDEYRY HEALVHPALS RVAALHDVLV LGGGDGLAVR
     EILKYPGVRS VTLVDLDPAM TALFRNSAML SALNAHAFSS PKVHVVNADA FRWLRDNRRR
     FDAAIVDFPD PTNFSLGKLY TVSLYRELAR ALSPGAVVSV QSTSPLVAPQ AFWTVATTME
     AAGFNTRGYH VYVPSFGEWG FVLAGLGALP AAGPLPAGLR FLDPTTERLA FAFPRDMARR
     PVSVNRLDNQ VLVRRFEEEW AKVEG
//
DBGET integrated database retrieval system