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Database: UniProt
Entry: A0A1G0WBW4_9BACT
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ID   A0A1G0WBW4_9BACT        Unreviewed;       316 AA.
AC   A0A1G0WBW4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=PABS domain-containing protein {ECO:0000259|PROSITE:PS51006};
GN   ORFNames=A2X47_07365 {ECO:0000313|EMBL:OGV18658.1};
OS   Lentisphaerae bacterium GWF2_38_69.
OC   Bacteria; Lentisphaerota.
OX   NCBI_TaxID=1798570 {ECO:0000313|EMBL:OGV18658.1, ECO:0000313|Proteomes:UP000176746};
RN   [1] {ECO:0000313|EMBL:OGV18658.1, ECO:0000313|Proteomes:UP000176746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGV18658.1}.
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DR   EMBL; MHBE01000044; OGV18658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0WBW4; -.
DR   STRING; 1798570.A2X47_07365; -.
DR   Proteomes; UP000176746; Unassembled WGS sequence.
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: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          47..297
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ   SEQUENCE   316 AA;  36691 MW;  778BE96AE2AEE0AD CRC64;
     MPILFEFIGF LRKAFFFIIL AFLFSAFDLS AVCYPSLQPS SQSNYANFWY DIFSPVSFLL
     PPHYPKKVIY ETKSNYSEIR VYDDGEGWRY LVFLPEYGYQ SVLDTKNPEV LVSQYAKLSF
     LAIPALGQES HKVLFIGMGG AIMPTYFRHY YPDAQIDIVD IDNSIPSIAE TYFNFKANKN
     TKVYIEDGRK FIEETNDKYD IIFLDVYDAE TIPQQFTTEE FFQLLRMRLS PEGVLSLNLA
     NFSDKFVLKI FKSVKSAFPN TYAFLTENEH NYVLISLNSE EKALKDLELK SLILDSRNTF
     NINFQTMLNP VTIIKE
//
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