SPEE_CLOD6
ID SPEE_CLOD6 Reviewed; 283 AA.
AC Q18A85;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=CD630_08900;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ67723.1; -; Genomic_DNA.
DR RefSeq; WP_009888722.1; NZ_CP010905.2.
DR RefSeq; YP_001087364.1; NC_009089.1.
DR AlphaFoldDB; Q18A85; -.
DR SMR; Q18A85; -.
DR STRING; 272563.CD630_08900; -.
DR EnsemblBacteria; CAJ67723; CAJ67723; CD630_08900.
DR GeneID; 66353394; -.
DR KEGG; cdf:CD630_08900; -.
DR KEGG; pdc:CDIF630_01010; -.
DR PATRIC; fig|272563.120.peg.914; -.
DR eggNOG; COG0421; Bacteria.
DR OMA; EYTIEAK; -.
DR PhylomeDB; Q18A85; -.
DR BioCyc; PDIF272563:G12WB-998-MON; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000001978; 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; 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 PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 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..283
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_1000011994"
FT DOMAIN 2..238
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 31
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 62
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 86
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 106
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 137..138
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 156..159
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 163
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 283 AA; 32992 MW; E33FE32272E16047 CRC64;
MELWYTEEWT ENVRFSIKVN KHLFEGKSQF QRIDVFDSDE FGKFLTIDGL MMVTYKDEFI
YHEMITHVPM ATNLNIKKVL VIGGGDGGTV RELSRYPQIE KIDMVEIDKM VVDVSKEYMD
ICSCKLDDKR VSLYFEDGVN FVKCAHDKSY DLIIVDSTDP IGPGEGLFST DFYKDCYRIL
TDDGILVNQS ESPYFDFNAK EMKRANKKLK QIFPISEVYQ AHIPTYPSGH WLFGFASKKL
NPVKNQDRNG WEKLSLKTKY YNSDIHLGSF MLPQYVKEML DEE
