ID L0E1X6_THIND Unreviewed; 412 AA.
AC L0E1X6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:AGA35210.1};
DE EC=2.5.1.16 {ECO:0000313|EMBL:AGA35210.1};
GN OrderedLocusNames=TVNIR_3580 {ECO:0000313|EMBL:AGA35210.1};
OS Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA35210.1, ECO:0000313|Proteomes:UP000010809};
RN [1] {ECO:0000313|Proteomes:UP000010809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC {ECO:0000313|Proteomes:UP000010809};
RA Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA Ravin N.V., Popov V.O.;
RT "Complete sequence of Thioalkalivibrio nitratireducens.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867}.
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DR EMBL; CP003989; AGA35210.1; -; Genomic_DNA.
DR RefSeq; WP_015260305.1; NC_019902.2.
DR AlphaFoldDB; L0E1X6; -.
DR STRING; 1255043.TVNIR_3580; -.
DR KEGG; tni:TVNIR_3580; -.
DR PATRIC; fig|1255043.3.peg.3612; -.
DR eggNOG; COG0421; Bacteria.
DR HOGENOM; CLU_667183_0_0_6; -.
DR OrthoDB; 5516475at2; -.
DR Proteomes; UP000010809; Chromosome.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC.
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:SF9; POLYAMINE AMINOPROPYLTRANSFERASE 2; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 72..244
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT REGION 389..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 412 AA; 45439 MW; 2B41DA8362870158 CRC64;
MATGFVYTRS GIDLTASPVR VDASHGETLV ALREGHAAHA AVIEREDGLS IRANNYYTLG
STHAAIAERN QTLIPLLVHP PPETVFFLGM GSGITAGAAL LLPVERVVVC ELLGEVVDLA
RDRFQPWVNG LFDDSRVTIY AEDGRHCLAR SPERFDAIIA DLFTPWKAGT GNLYTQDHYR
LAAERLKPGG MYVQWIPLYQ VSMQELAIIG TTMASVFPEL TLWRGDLYPS RSIVALLGRN
TAEPLDPEVL VRNARRLLGE YEGADEYYEA LGLLFYAGNP EESRFFAEAL INTDDRPLIE
YLAPRTHRAV LTGAAQWGVG VARDRLCWAL FDALPPERDP YLRALDERQL RHVEAGLRYA
LYQGIRVRGT RAEARAVWLG FLEVVTPATR SPDSPAGQAG FGASGFGSGE RN
//
