ID B8J3B6_DESDA Unreviewed; 510 AA.
AC B8J3B6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Spermine synthase {ECO:0000313|EMBL:ACL49926.1};
GN OrderedLocusNames=Ddes_2030 {ECO:0000313|EMBL:ACL49926.1};
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL49926.1};
RN [1] {ECO:0000313|EMBL:ACL49926.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL49926.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) 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; CP001358; ACL49926.1; -; Genomic_DNA.
DR AlphaFoldDB; B8J3B6; -.
DR STRING; 525146.Ddes_2030; -.
DR KEGG; dds:Ddes_2030; -.
DR eggNOG; COG4262; Bacteria.
DR HOGENOM; CLU_008530_1_0_7; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR036259; MFS_trans_sf.
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 Membrane {ECO:0000256|SAM:Phobius};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..449
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 510 AA; 54589 MW; 4664EB319B8C4D3C CRC64;
MLELTVFFSG ALVMVLEMVG ARVLAPYVGT SAIVWTSLIG VVLACLALGA WAGGRMADRH
LSRRGLALAL AGAGAGSALT ALCHPLVGQW VTEGIGNLYV AAVAAAVGIF ALPAFFFGMV
SPYAIRLRIG SLDTSGATVG RLYALSTAGS ILGTFLGGFV LISFFGSSSI LWGVAVCMLA
LSLCNAPGGA KGRAALLALC ILGTAINGMY GNWREDRGSM HLVESPYNSI RVYEGTDWGE
GGRAVRLMAT DPGYSQSGMY LDAPDELYFQ YTRFYALGPY FVPHARSILM LGGGGYSVPK
WILAGKSALA APEDVRMTVV EIDPAMTDVA RRWFALGDDV RLSVRHEDAR AFLNRQDGRF
DLVFVDVFNS HYAVPFQMGT VEAARALRRA VAPGGAVLMN VISAVEGEDG RLFQSIFKAL
STSFAEVQVY CVSRPDRPGE VQNLMVAAFP EKRDRAAPLA AGSTQVQLTE QKPVEMMLAT
RYTGPLDFAT LPLTDDFAPV ERYALMLLRQ
//