ID   SPEE_BIFLO              Reviewed;         446 AA.
AC   Q8G4L4;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Probable polyamine aminopropyl transferase;
DE   AltName: Full=Putrescine aminopropyltransferase;
DE            Short=PAPT;
DE   AltName: Full=Spermidine synthase;
DE            Short=SPDS;
DE            Short=SPDSY;
DE            EC=2.5.1.16;
GN   Name=speE; OrderedLocusNames=BL1365;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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:0000250}.
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   -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC       spermidine from putrescine: step 1/1.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AE014295; AAN25165.1; -; Genomic_DNA.
DR   RefSeq; NP_696529.1; NC_004307.2.
DR   AlphaFoldDB; Q8G4L4; -.
DR   SMR; Q8G4L4; -.
DR   STRING; 206672.BL1365; -.
DR   EnsemblBacteria; AAN25165; AAN25165; BL1365.
DR   KEGG; blo:BL1365; -.
DR   PATRIC; fig|206672.9.peg.223; -.
DR   HOGENOM; CLU_049703_0_0_11; -.
DR   OMA; PIGRENA; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000000439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Polyamine biosynthesis; Reference proteome;
KW   Spermidine biosynthesis; Transferase.
FT   CHAIN           1..446
FT                   /note="Probable polyamine aminopropyl transferase"
FT                   /id="PRO_0000156471"
FT   DOMAIN          116..351
FT                   /note="PABS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00354"
FT   REGION          1..117
FT                   /note="Unknown"
FT   REGION          64..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..353
FT                   /note="Spermidine synthase"
FT   COMPBIAS        76..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00354"
FT   BINDING         147
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000250"
FT   BINDING         251..252
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   446 AA;  49452 MW;  02DF0F234EF97BAA CRC64;
     MVEPAIGRNH IRAGRHHGRA RIVFARTKNH AYLSHDAYCS RYPPIGRENA DRLRIRTVVD
     RRTGRGAERW HRSPRQANGR FSNQRYSSTS PNSSPACPLI YFISIKAKRI ACVVSAVIFV
     ATSCVSPLTG FAFWETNLAY EGESIYNYLQ VKNLSDRTIL STNVLFGVQS VTMKDKGLTG
     MYYDTALAAP ALADNANSAL ILGMGTGTYA RQLKQYYPKM NITGVEIDQK ITDLAGEYFD
     EPADIPVTTY DGRAWLAASH DKYDVIMVDA YQDITIPFQM SSTEFFTMVR EHLNPGGVMV
     VNMNMISDGQ GSINEALSDT IASVFGNGNT LTADVPNTTN RELFAKKPGS GSEENSMQQA
     SKALNLRETT YERTGSEDLE WYMEEVASRF RKVNEPDSAS TILTDDKAPV EVLGMHAIDQ
     IIADEAGPYR QILKDEGFGG LLRAVQ