ID A0A2G4IB56_9BACT Unreviewed; 521 AA.
AC A0A2G4IB56;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:PHX95768.1};
GN ORFNames=CK546_00865 {ECO:0000313|EMBL:PHX95768.1};
OS Pedosphaera sp.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Limisphaerales; Pedosphaera.
OX NCBI_TaxID=2024890 {ECO:0000313|EMBL:PHX95768.1, ECO:0000313|Proteomes:UP000223988};
RN [1] {ECO:0000313|EMBL:PHX95768.1, ECO:0000313|Proteomes:UP000223988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baikal-G1 {ECO:0000313|EMBL:PHX95768.1};
RX PubMed=29079621;
RA Cabello-Yeves P.J., Zemskaya T.I., Rosselli R., Coutinho F.H.,
RA Zakharenko A.S., Blinov V.V., Rodriguez-Valera F.;
RT "Genomes of novel microbial lineages assembled from the sub-ice waters of
RT Lake Baikal.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
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:PHX95768.1}.
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DR EMBL; NSHY01000014; PHX95768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4IB56; -.
DR Proteomes; UP000223988; Unassembled WGS sequence.
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; 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 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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..458
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 521 AA; 56509 MW; D445907F7257F1B6 CRC64;
MSKPAVPTTA PLSPGLRRFL YGTAATTGAA ILIVEILGAK MLSPYVGTSH FVWTAQIAVT
LLSLAVGYWF GGWLVDRSQN LRRLYTCILL AAVYLCFTVP FTAKVAFACL QFPLAVGSLL
ASLFLFFVPL TLLATVGPFV IRVLTSVVAG VGGTVGRLSA VSTLGSVLGT VLIGYVLIPF
LPNSVTMFIT AGVLMALSAV YFVVWREKGD SMNGPVVLVA LGVFAGWAGI RIDAKSPSDS
MTEVARRNSN FGLMQVFETG GGGRRYYLND YLTQNTYDPE AKQSISLFTY GLHGLATVYT
AQIKDVLCIG MGVGIVPMQF AREGSKVDVV EINDAIANVA KAHFHLEPDK LNLTVGDGRQ
FVNAATKQYD AVILDAFLGD SSPSHLMTQE AFTAMRRVLR PDGVLVINSF GDFEPGQDFF
TASLDKTLRS VFGTVRIHAS GNGNVFFVAT PAKELKQHRT MDFAAMHPTV RQQARDALEG
IRTTNPKSGI VLTDDFNPVE FHDAKNREQF RRQLAFSMRP K
//
