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Database: UniProt
Entry: R5XAY8_9FIRM
LinkDB: R5XAY8_9FIRM
Original site: R5XAY8_9FIRM 
ID   R5XAY8_9FIRM            Unreviewed;       283 AA.
AC   R5XAY8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Polyamine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
DE   AltName: Full=Putrescine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
DE            Short=PAPT {ECO:0000256|HAMAP-Rule:MF_00198};
DE   AltName: Full=Spermidine synthase {ECO:0000256|HAMAP-Rule:MF_00198};
DE            Short=SPDS {ECO:0000256|HAMAP-Rule:MF_00198};
DE            Short=SPDSY {ECO:0000256|HAMAP-Rule:MF_00198};
DE            EC=2.5.1.16 {ECO:0000256|HAMAP-Rule:MF_00198};
GN   Name=speE {ECO:0000256|HAMAP-Rule:MF_00198};
GN   ORFNames=BN568_01972 {ECO:0000313|EMBL:CDA05561.1};
OS   Blautia sp. CAG:257.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=1262756 {ECO:0000313|EMBL:CDA05561.1, ECO:0000313|Proteomes:UP000018056};
RN   [1] {ECO:0000313|EMBL:CDA05561.1, ECO:0000313|Proteomes:UP000018056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:257 {ECO:0000313|Proteomes:UP000018056};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine group
CC       from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to
CC       putrescine (1,4-diaminobutane) to yield spermidine. {ECO:0000256|HAMAP-
CC       Rule:MF_00198}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) +
CC         S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC         ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00198,
CC         ECO:0000256|RuleBase:RU003837};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC       spermidine from putrescine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00198}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_00198}.
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|HAMAP-Rule:MF_00198,
CC       ECO:0000256|RuleBase:RU003836}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00198}.
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:CDA05561.1}.
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DR   EMBL; CBBB010000128; CDA05561.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5XAY8; -.
DR   STRING; 1262756.BN568_01972; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000018056; Unassembled WGS sequence.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.140.10; Spermidine synthase, tetramerisation domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00198; Spermidine_synth; 1.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR030373; PABS_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001045; Spermi_synthase.
DR   InterPro; IPR035246; Spermidine_synt_N.
DR   InterPro; IPR037163; Spermidine_synt_N_sf.
DR   NCBIfam; TIGR00417; speE; 1.
DR   PANTHER; PTHR11558:SF11; SPERMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR11558; SPERMIDINE/SPERMINE SYNTHASE; 1.
DR   Pfam; PF17284; Spermine_synt_N; 1.
DR   Pfam; PF01564; Spermine_synth; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01330; PABS_1; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW   Rule:MF_00198}; Reference proteome {ECO:0000313|Proteomes:UP000018056};
KW   Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198,
KW   ECO:0000256|RuleBase:RU003837};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00198}.
FT   DOMAIN          2..237
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT                   ECO:0000256|PROSITE-ProRule:PRU00354"
FT   BINDING         31
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         62
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         86
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         106
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         137..138
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT   BINDING         155..158
FT                   /ligand="spermidine"
FT                   /ligand_id="ChEBI:CHEBI:57834"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ   SEQUENCE   283 AA;  32720 MW;  5B28D3351E1ECD30 CRC64;
     MEMWFSDEHT EDVKLSIRVR EQLFSAQSEF QQIDVLDSKE FGKILVVDGD LTLTEKDEFI
     YHEMITHVPM AVHPLVKDVL VIGGGDGGVV RELVKYEEIE HIDMVEIDPL LVEVCRKYLP
     QIACSLNDPR VQIFHEDGLR FVRSKTDCYD LIIIDSPNPF GLGEGLFTKE FYGNCFGALR
     EDGIMINQNE SPFYTEEAFQ CQRMHKRILE TFPICRVYQA HLPSYPSGHW LFGFASKKYH
     PLTDLNGVAW KLKGIHTRYY EPRLHAGVFA LPVYVEELLE DVE
//
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