SPEE_THEKO
ID SPEE_THEKO Reviewed; 288 AA.
AC Q5JFG9;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:20675472};
DE AltName: Full=Agmatine aminopropyltransferase {ECO:0000305|PubMed:20675472};
DE EC=2.5.1.104 {ECO:0000269|PubMed:20675472};
DE AltName: Full=Cadaverine aminopropyltransferase {ECO:0000305|PubMed:20675472};
DE EC=2.5.1.- {ECO:0000269|PubMed:20675472};
DE AltName: Full=N1-aminopropylagmatine synthase {ECO:0000305|PubMed:20675472};
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, ECO:0000303|PubMed:20675472};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:20675472};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:20675472};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:20675472};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=TK0147;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=20675472; DOI=10.1128/jb.00279-10;
RA Morimoto N., Fukuda W., Nakajima N., Masuda T., Terui Y., Kanai T.,
RA Oshima T., Imanaka T., Fujiwara S.;
RT "Dual biosynthesis pathway for longer-chain polyamines in the
RT hyperthermophilic archaeon Thermococcus kodakarensis.";
RL J. Bacteriol. 192:4991-5001(2010).
CC -!- FUNCTION: Involved in the biosynthesis of polyamines which are thought
CC to support the growth of thermophilic microorganisms under high-
CC temperature conditions. It seems that long-chain and branched-chain of
CC polyamines effectively stabilize DNA and RNA, respectively. Catalyzes
CC the irreversible transfer of a propylamine group from the amino donor
CC S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1-
CC aminopropylagmatine. It can also use cadaverine (1,5-diaminopentane)
CC and putrescine (1,4-diaminobutane) as substrate with a lower activity
CC than that of agmatine. The reaction involves a nucleophilic attack on
CC the C-3 methylene of the propylamine moiety adjacent to the positively
CC charged sulfur of decarboxy-AdoMet. {ECO:0000269|PubMed:20675472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) +
CC N(1)-aminopropylagmatine + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:36487, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:58145, ChEBI:CHEBI:64335;
CC EC=2.5.1.104; Evidence={ECO:0000269|PubMed:20675472};
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 ECO:0000269|PubMed:20675472};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cadaverine + S-adenosyl 3-(methylsulfanyl)propylamine =
CC aminopropylcadaverine + H(+) + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:33387, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:58384, ChEBI:CHEBI:64858;
CC Evidence={ECO:0000269|PubMed:20675472};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.2 uM for agmatine (at pH 9 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:20675472};
CC KM=80.7 uM for cadaverine (at pH 9 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:20675472};
CC KM=1053 uM for putrescine (at pH 9 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:20675472};
CC Note=kcat is 0.3 sec(-1) for aminopropyl transferase activity with
CC putrescine as substrate (at pH 9 and 70 degrees Celsius). kcat is
CC 0.28 sec(-1) for aminopropyl transferase activity with agmatine as
CC substrate (at pH 9 and 70 degrees Celsius. kcat is 0.02 sec(-1) for
CC aminopropyl transferase activity with cadaverine as substrate (at pH
CC 9 and 70 degrees Celsius. {ECO:0000269|PubMed:20675472};
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 ECO:0000269|PubMed:20675472}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show decreased growth at
CC 85 and 93 degrees Celsius. The growth rate is slightly restored at 85
CC degrees Celsius by the addition of spermidine, however growth at 93
CC degrees Celsius is not restored even when spermidine is added. This
CC mutant accumulates agmatine at 85 degrees Celsius.
CC {ECO:0000269|PubMed:20675472}.
CC -!- MISCELLANEOUS: In T.kodakarensis, two kinds of synthetic pathways from
CC agmatine to spermidine are predicted. One is the pathway via putrescine
CC (pathway I), and the other is that via N1-aminopropylagmatine (pathway
CC II). {ECO:0000305|PubMed:20675472}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
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DR EMBL; AP006878; BAD84336.1; -; Genomic_DNA.
DR RefSeq; WP_011249102.1; NC_006624.1.
DR AlphaFoldDB; Q5JFG9; -.
DR SMR; Q5JFG9; -.
DR STRING; 69014.TK0147; -.
DR EnsemblBacteria; BAD84336; BAD84336; TK0147.
DR GeneID; 3234087; -.
DR KEGG; tko:TK0147; -.
DR PATRIC; fig|69014.16.peg.147; -.
DR eggNOG; arCOG00050; Archaea.
DR HOGENOM; CLU_048199_0_1_2; -.
DR InParanoid; Q5JFG9; -.
DR OMA; LWPGQSF; -.
DR OrthoDB; 77175at2157; -.
DR PhylomeDB; Q5JFG9; -.
DR BioCyc; MetaCyc:MON-16734; -.
DR BRENDA; 2.5.1.104; 5246.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043919; F:agmatine aminopropyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043918; F:cadaverine aminopropyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006596; P:polyamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Polyamine biosynthesis; Reference proteome;
KW Spermidine biosynthesis; Transferase.
FT CHAIN 1..288
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156532"
FT DOMAIN 11..245
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 36
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 67
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 91
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 111
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 148..149
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 166..169
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 173
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 288 AA; 33447 MW; 618BE8E5B27982FE CRC64;
MGYNEQERAF IEWYPRGYGV GFKVKRRLFE TQTEYQRLEI YETEGFGKLL VLDGTVQLVE
VGEESYHEVL VHPVMLAHPN PRKVLVIGGG DGGTLREVLR HDTVEKAIMV EIDEGVVEAS
YLYLDVAKDL LDRLIKKEEP RAELIIGDGV KYLRETDERF DVIIVDSTDP VGPAKLLFSE
EFYRDAYEKL NEKGLYVTQA GSVYLFTNEL LDAYKAMKKV FDRVYYFSFP VIGYASPWSF
LVGVKGDVDF TRIDLERAKK LDLYYYDPER HETLFQMPRY VRKLLEGQ
