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Database: UniProt
Entry: A0A258TST7_9PROT
LinkDB: A0A258TST7_9PROT
Original site: A0A258TST7_9PROT 
ID   A0A258TST7_9PROT        Unreviewed;       257 AA.
AC   A0A258TST7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=PABS domain-containing protein {ECO:0000259|PROSITE:PS51006};
GN   ORFNames=B7Y41_06675 {ECO:0000313|EMBL:OYY94513.1};
OS   Hydrogenophilales bacterium 28-61-23.
OC   Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX   NCBI_TaxID=1970530 {ECO:0000313|EMBL:OYY94513.1, ECO:0000313|Proteomes:UP000215898};
RN   [1] {ECO:0000313|EMBL:OYY94513.1, ECO:0000313|Proteomes:UP000215898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=28-61-23 {ECO:0000313|EMBL:OYY94513.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) 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:OYY94513.1}.
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DR   EMBL; NCGJ01000004; OYY94513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A258TST7; -.
DR   Proteomes; UP000215898; 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   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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00354}.
FT   DOMAIN          1..222
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ   SEQUENCE   257 AA;  29069 MW;  F9B1709FE6B2B0CC CRC64;
     MNFFRRRSPG HAPVEISERN DTRFLHLGGP AVQSAMRIKE PYALDLEYTR AMMAFLLFCR
     EPEDIALIGL GGGSIAKYIH RHLPESRLTA LEINPEVVAA ARAYFMLPQD DERLSVITGD
     GAAFVHENPD SQDVLLVDGY DAKRIVDALA SPEFYRACKA MLRPGGVAVF NLWGSDEYYP
     RYFDRLARAF GEHVLQLPAE KKGNIIVFAF RKPLPIVTMA PLLREAHRLE AELGLEFEAF
     VTRMRNWNPT STDNFIV
//
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