SPEE2_CALS4
ID SPEE2_CALS4 Reviewed; 297 AA.
AC Q8R977;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Polyamine aminopropyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Putrescine aminopropyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=PAPT 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine synthase 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDS 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDSY 2 {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198};
GN Name=speE2 {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=TTE1748;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(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:0000255|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:0000255|HAMAP-Rule:MF_00198};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00198}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
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DR EMBL; AE008691; AAM24942.1; -; Genomic_DNA.
DR RefSeq; WP_011025944.1; NC_003869.1.
DR AlphaFoldDB; Q8R977; -.
DR SMR; Q8R977; -.
DR STRING; 273068.TTE1748; -.
DR EnsemblBacteria; AAM24942; AAM24942; TTE1748.
DR KEGG; tte:TTE1748; -.
DR eggNOG; COG0421; Bacteria.
DR HOGENOM; CLU_048199_0_1_9; -.
DR OMA; YGSDEHE; -.
DR OrthoDB; 1613081at2; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000000555; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR030374; PABS.
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 Pfam; PF17284; Spermine_synt_N; 1.
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..297
FT /note="Polyamine aminopropyltransferase 2"
FT /id="PRO_0000156515"
FT DOMAIN 26..258
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 53
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 84
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 108
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 128
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 157..158
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 184
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 297 AA; 34122 MW; 46F6906BAAA7A52A CRC64;
MILKLEVGVG LKNLNGKWGL DSSKEFYWEP DVEGGYRVYK VKSVIIEHQS LYQKIDIVEL
ETWGKSLFLD GSLQSTESDE FIYHELLVHP AMRVHPSPKR VLICGVGEGK SVREVLKYPT
VKEVIGVDID KEVVALCQKH LGKTPIDDKR VRLVYQDVAE FIKNYRGEPF DVAIVDVTDD
LDGPARSVHQ LDFYKRLYEI LGEKATVVVQ GTSAFSKVKN VGFCHIYEIL KEVFPFVIPY
ADYIPSFSDL WTFFVALKGI KDLTPRHEIP RDLKYYDEYT NERIFTLAKP LREKLGV
