ID A0A370N3T7_9BURK Unreviewed; 277 AA.
AC A0A370N3T7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:RDK00290.1};
GN ORFNames=DLM46_23495 {ECO:0000313|EMBL:RDK00290.1};
OS Paraburkholderia lacunae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2211104 {ECO:0000313|EMBL:RDK00290.1, ECO:0000313|Proteomes:UP000254875};
RN [1] {ECO:0000313|Proteomes:UP000254875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S27 {ECO:0000313|Proteomes:UP000254875};
RA Feng T.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867}.
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:RDK00290.1}.
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; QHKS01000016; RDK00290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370N3T7; -.
DR OrthoDB; 117774at2; -.
DR Proteomes; UP000254875; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; NF037959; MFS_SpdSyn; 1.
DR PANTHER; PTHR43317:SF12; POLYAMINE AMINOPROPYLTRANSFERASE; 1.
DR PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|PROSITE-
KW ProRule:PRU00354}; Reference proteome {ECO:0000313|Proteomes:UP000254875};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 74..242
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 277 AA; 31180 MW; 5FE28C6A5AB2D1D5 CRC64;
MPETTHAPAD RSRNDSRPIK PTKKRQRKLN RPLVIQNDQV ISLYFDARGV QSTMLRHNPT
ALALGYTRTM MGFLLFRPFP RRIAMIGLGG GSLAKYCYRH LPDTAITAVE INPDVIALRE
LFQLPRDDDR FRVVCADGAR YINASDHTPD VLLLDGFNAD GLPAELGSRS FYEACRRRLS
DDGILVANLV TDEPEFHSYL RSLRNVFANS VALAPSEGSE HNVTVFAWNG IEGLPSLTSM
LDRARALQYS HPVNLHATAM SIECGRKFDW NRYDETC
//
