ID F2BD36_9NEIS Unreviewed; 508 AA.
AC F2BD36;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ECO:0000313|EMBL:EGF10760.1};
GN ORFNames=HMPREF9123_1642 {ECO:0000313|EMBL:EGF10760.1};
OS Neisseria bacilliformis ATCC BAA-1200.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=888742 {ECO:0000313|EMBL:EGF10760.1, ECO:0000313|Proteomes:UP000004105};
RN [1] {ECO:0000313|EMBL:EGF10760.1, ECO:0000313|Proteomes:UP000004105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1200 {ECO:0000313|EMBL:EGF10760.1,
RC ECO:0000313|Proteomes:UP000004105};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) 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 -!- 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00198};
CC Multi-pass membrane protein {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 -!- 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:EGF10760.1}.
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DR EMBL; AFAY01000031; EGF10760.1; -; Genomic_DNA.
DR RefSeq; WP_007342648.1; NZ_GL878494.1.
DR AlphaFoldDB; F2BD36; -.
DR STRING; 267212.GCA_001063965_00055; -.
DR HOGENOM; CLU_034289_1_0_4; -.
DR OrthoDB; 9793120at2; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000004105; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010487; F:thermospermine synthase activity; IEA:UniProt.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 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 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; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW Rule:MF_00198}; Reference proteome {ECO:0000313|Proteomes:UP000004105};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW Rule:MF_00198};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00198}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00198}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 41..65
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 77..100
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 172..190
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT TRANSMEM 202..218
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT DOMAIN 209..448
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT ECO:0000256|PROSITE-ProRule:PRU00354"
FT BINDING 243
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 273
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 297
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 317
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 351..352
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
SQ SEQUENCE 508 AA; 56305 MW; 3BD995EFFE9457E8 CRC64;
MNLRPHSHRT LIISVFVVAS CGLAYELVIA ALASYLLGDS ILQFSSVIGL YLFSMGIGAH
LTKYIKDEDT LARFVEIELL VGVVGGLSAL ALFVAFGLSA APFRTLLYAF VLIVGTVVGM
EIPLVMRVLN RQEADFKELV SRVLTFDYLG ALAVSLLFPL VLAPRLGMAR SALLFGILNA
AVAYLTARVF KADLPNYRTV RLRAFLVLAV LAAAFAYADR ITLKAEQSYF GDPIVYESHS
PYQRLVVTRW KDDTRLYING NLQFSSRDEA RYHEALVLPA MQTAAHAEHI LILGGGDGLA
AREVLKYPQV KKITLVDLDP AMTAVFKTSA ALSALNHGSL SHPKMHVVNA DAAKWLETAR
EKFDVIIIDL PDPSNFSLGK LYSVPMYRLV SQHLAPQGKI VVQSTSPYFA PNAYWSVVAT
LEAADLHTAP YHVYVPSFGE WGFVLAGFDT DFAVPQKFDV PARYLNAQTA AEMFRFPPDM
ARRKVEPNHL NTQILVNYFE NDWRNVIR
//
