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Polyamine aminopropyltransferase (Agmatine aminopropyltransferase) (EC 2.5.1.104) (Cadaverine aminopropyltransferase) (EC 2.5.1.-) (N1-aminopropylagmatine synthase) (Putrescine aminopropyltransferase) (PAPT) (Spermidine synthase) (SPDS) (SPDSY) (EC 2.5.1.16)

 SPEE_THEKO              Reviewed;         288 AA.
Q5JFG9;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
28-MAR-2018, entry version 91.
RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:20675472};
AltName: Full=Agmatine aminopropyltransferase {ECO:0000305|PubMed:20675472};
EC=2.5.1.104 {ECO:0000269|PubMed:20675472};
AltName: Full=Cadaverine aminopropyltransferase {ECO:0000305|PubMed:20675472};
EC=2.5.1.- {ECO:0000269|PubMed:20675472};
AltName: Full=N1-aminopropylagmatine synthase {ECO:0000305|PubMed:20675472};
AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:20675472};
Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:20675472};
Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:20675472};
EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:20675472};
Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=TK0147;
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
(Pyrococcus kodakaraensis (strain KOD1)).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Thermococcus.
NCBI_TaxID=69014;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
PubMed=15710748; DOI=10.1101/gr.3003105;
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
"Complete genome sequence of the hyperthermophilic archaeon
Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
genomes.";
Genome Res. 15:352-363(2005).
[2]
FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL
PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
PubMed=20675472; DOI=10.1128/JB.00279-10;
Morimoto N., Fukuda W., Nakajima N., Masuda T., Terui Y., Kanai T.,
Oshima T., Imanaka T., Fujiwara S.;
"Dual biosynthesis pathway for longer-chain polyamines in the
hyperthermophilic archaeon Thermococcus kodakarensis.";
J. Bacteriol. 192:4991-5001(2010).
-!- FUNCTION: Involved in the biosynthesis of polyamines which are
thought to support the growth of thermophilic microorganisms under
high-temperature conditions. It seems that long-chain and
branched-chain of polyamines effectively stabilize DNA and RNA,
respectively. Catalyzes the irreversible transfer of a propylamine
group from the amino donor S-adenosylmethioninamine (decarboxy-
AdoMet) to agmatine to yield N1-aminopropylagmatine. It can also
use cadaverine (1,5-diaminopentane) and putrescine (1,4-
diaminobutane) as substrate with a lower activity than that of
agmatine. The reaction involves a nucleophilic attack on the C-3
methylene of the propylamine moiety adjacent to the positively
charged sulfur of decarboxy-AdoMet. {ECO:0000269|PubMed:20675472}.
-!- CATALYTIC ACTIVITY: S-adenosylmethioninamine + agmatine = S-
methyl-5'-thioadenosine + N(1)-(3-aminopropyl)agmatine.
{ECO:0000269|PubMed:20675472}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.
{ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:20675472}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine + 1,5-
diaminopentane = S-methyl-5'-thioadenosine + N-(3-aminopropyl)-
1,5-diaminopentane. {ECO:0000269|PubMed:20675472}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12.2 uM for agmatine (at pH 9 and 70 degrees Celsius)
{ECO:0000269|PubMed:20675472};
KM=80.7 uM for cadaverine (at pH 9 and 70 degrees Celsius)
{ECO:0000269|PubMed:20675472};
KM=1053 uM for putrescine (at pH 9 and 70 degrees Celsius)
{ECO:0000269|PubMed:20675472};
Note=Kcat is 0.3 sec(-1) for aminopropyl transferase activity
with putrescine as substrate (at pH 9 and 70 degrees Celsius).
Kcat is 0.28 sec(-1) for aminopropyl transferase activity with
agmatine as substrate (at pH 9 and 70 degrees Celsius. Kcat is
0.02 sec(-1) for aminopropyl transferase activity with
cadaverine as substrate (at pH 9 and 70 degrees Celsius.
{ECO:0000269|PubMed:20675472};
-!- PATHWAY: Amine and polyamine biosynthesis; spermidine
biosynthesis; spermidine from putrescine: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_00198}.
-!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-
Rule:MF_00198}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198,
ECO:0000269|PubMed:20675472}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene show decreased
growth at 85 and 93 degrees Celsius. The growth rate is slightly
restored at 85 degrees Celsius by the addition of spermidine,
however growth at 93 degrees Celsius is not restored even when
spermidine is added. This mutant accumulates agmatine at 85
degrees Celsius. {ECO:0000269|PubMed:20675472}.
-!- MISCELLANEOUS: In T.kodakarensis, two kinds of synthetic pathways
from agmatine to spermidine are predicted. One is the pathway via
putrescine (pathway I), and the other is that via N1-
aminopropylagmatine (pathway II). {ECO:0000305|PubMed:20675472}.
-!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
{ECO:0000255|HAMAP-Rule:MF_00198}.
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EMBL; AP006878; BAD84336.1; -; Genomic_DNA.
RefSeq; WP_011249102.1; NC_006624.1.
ProteinModelPortal; Q5JFG9; -.
SMR; Q5JFG9; -.
STRING; 69014.TK0147; -.
EnsemblBacteria; BAD84336; BAD84336; TK0147.
GeneID; 3234087; -.
KEGG; tko:TK0147; -.
PATRIC; fig|69014.16.peg.147; -.
eggNOG; arCOG00050; Archaea.
eggNOG; COG0421; LUCA.
HOGENOM; HOG000256146; -.
InParanoid; Q5JFG9; -.
KO; K00797; -.
OMA; LWPGQSF; -.
OrthoDB; POG093Z06G4; -.
BioCyc; MetaCyc:MONOMER-16734; -.
BioCyc; TKOD69014:G1G2A-145-MONOMER; -.
BRENDA; 2.5.1.104; 5246.
UniPathway; UPA00248; UER00314.
Proteomes; UP000000536; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0043919; F:agmatine aminopropyltransferase activity; IDA:UniProtKB.
GO; GO:0043918; F:cadaverine aminopropyltransferase activity; IDA:UniProtKB.
GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC.
GO; GO:0006596; P:polyamine biosynthetic process; IDA:UniProtKB.
GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
Gene3D; 2.30.140.10; -; 1.
HAMAP; MF_00198; Spermidine_synth; 1.
InterPro; IPR030374; PABS.
InterPro; IPR030373; PABS_CS.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR001045; Spermi_synthase.
InterPro; IPR035246; Spermidine_synt_N.
InterPro; IPR037163; Spermidine_synt_N_sf.
Pfam; PF17284; Spermine_synt_N; 1.
SUPFAM; SSF53335; SSF53335; 1.
TIGRFAMs; TIGR00417; speE; 1.
PROSITE; PS01330; PABS_1; 1.
PROSITE; PS51006; PABS_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Polyamine biosynthesis;
Reference proteome; Spermidine biosynthesis; Transferase.
CHAIN 1 288 Polyamine aminopropyltransferase.
/FTId=PRO_0000156532.
DOMAIN 11 245 PABS. {ECO:0000255|HAMAP-Rule:MF_00198}.
REGION 56 57 Polyamine binding. {ECO:0000255|HAMAP-
Rule:MF_00198}.
REGION 148 149 S-adenosylmethioninamine binding.
{ECO:0000255|HAMAP-Rule:MF_00198}.
REGION 167 169 Polyamine binding. {ECO:0000255|HAMAP-
Rule:MF_00198}.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 12 12 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 36 36 S-adenosylmethioninamine.
{ECO:0000255|HAMAP-Rule:MF_00198}.
BINDING 67 67 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 91 91 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 111 111 S-adenosylmethioninamine.
{ECO:0000255|HAMAP-Rule:MF_00198}.
BINDING 173 173 S-adenosylmethioninamine; via carbonyl
oxygen. {ECO:0000255|HAMAP-
Rule:MF_00198}.
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


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