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Polyamine aminopropyltransferase 1 (Caldopentamine synthase) (Norspermidine aminopropyltransferase) (EC 2.5.1.126) (Norspermine aminopropyltransferase) (EC 2.5.1.127) (Norspermine synthase) (Spermidine aminopropyltransferase) (EC 2.5.1.79) (Thermospermine synthase) (Triamine/tetramine aminopropyltransferase)

 SPEE1_HYPBU             Reviewed;         292 AA.
A2BIX4;
04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
28-FEB-2018, entry version 70.
RecName: Full=Polyamine aminopropyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:19822146};
AltName: Full=Caldopentamine synthase {ECO:0000305|PubMed:19822146};
AltName: Full=Norspermidine aminopropyltransferase {ECO:0000305|PubMed:19822146};
EC=2.5.1.126 {ECO:0000269|PubMed:19822146};
AltName: Full=Norspermine aminopropyltransferase {ECO:0000305|PubMed:19822146};
EC=2.5.1.127 {ECO:0000269|PubMed:19822146};
AltName: Full=Norspermine synthase {ECO:0000305|PubMed:19822146};
AltName: Full=Spermidine aminopropyltransferase {ECO:0000305|PubMed:19822146};
EC=2.5.1.79 {ECO:0000269|PubMed:19822146};
AltName: Full=Thermospermine synthase {ECO:0000305|PubMed:19822146};
AltName: Full=Triamine/tetramine aminopropyltransferase {ECO:0000303|PubMed:19822146};
Name=speE1 {ECO:0000255|HAMAP-Rule:MF_00198,
ECO:0000303|PubMed:19822146}; OrderedLocusNames=Hbut_0057;
Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
Pyrodictiaceae; Hyperthermus.
NCBI_TaxID=415426;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
PubMed=17350933; DOI=10.1155/2007/745987;
Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A.,
Awayez M., She Q., Garrett R.A., Klenk H.-P.;
"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
Archaea 2:127-135(2007).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
PubMed=19822146; DOI=10.1016/j.febslet.2009.10.014;
Knott J.M.;
"Biosynthesis of long-chain polyamines by crenarchaeal polyamine
synthases from Hyperthermus butylicus and Pyrobaculum aerophilum.";
FEBS Lett. 583:3519-3524(2009).
-!- 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 norspermidine, spermidine and norspermine to yield
norspermine, thermospermine and caldopentamine, respectively. It
can also synthesize sym-norspermidine (bis(3-aminopropyl)amine)
from 1,3-diaminopropane with a very low activity. The biosynthesis
of caldohexamine and caldoheptamine from caldopentamine has been
also observed. {ECO:0000269|PubMed:19822146}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
norspermine = S-methyl-5'-thioadenosine + caldopentamine.
{ECO:0000269|PubMed:19822146}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
norspermidine = S-methyl-5'-thioadenosine + norspermine.
{ECO:0000269|PubMed:19822146}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
spermidine = S-methyl-5'-thioadenosine + thermospermine + H(+).
{ECO:0000269|PubMed:19822146}.
-!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-
Rule:MF_00198}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
-!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
{ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000255|RuleBase:RU003836}.
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EMBL; CP000493; ABM79935.1; -; Genomic_DNA.
RefSeq; WP_011821252.1; NC_008818.1.
ProteinModelPortal; A2BIX4; -.
SMR; A2BIX4; -.
STRING; 415426.Hbut_0057; -.
EnsemblBacteria; ABM79935; ABM79935; Hbut_0057.
GeneID; 4781772; -.
KEGG; hbu:Hbut_0057; -.
eggNOG; arCOG00050; Archaea.
eggNOG; COG0421; LUCA.
HOGENOM; HOG000256146; -.
KO; K00797; -.
OMA; MDLTDPY; -.
OrthoDB; POG093Z06G4; -.
BRENDA; 2.5.1.127; 10772.
Proteomes; UP000002593; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0050314; F:sym-norspermidine synthase activity; IDA:UniProtKB.
GO; GO:0010487; F:thermospermine synthase activity; IDA:UniProtKB.
GO; GO:0006596; P:polyamine 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.
PROSITE; PS01330; PABS_1; 1.
PROSITE; PS51006; PABS_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Polyamine biosynthesis;
Reference proteome; Transferase.
CHAIN 1 292 Polyamine aminopropyltransferase 1.
/FTId=PRO_0000431724.
DOMAIN 1 244 PABS. {ECO:0000255|HAMAP-Rule:MF_00198}.
REGION 55 56 Polyamine binding. {ECO:0000255|HAMAP-
Rule:MF_00198}.
REGION 142 143 S-adenosylmethioninamine binding.
{ECO:0000255|HAMAP-Rule:MF_00198}.
ACT_SITE 163 163 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 35 35 S-adenosylmethioninamine.
{ECO:0000255|HAMAP-Rule:MF_00198}.
BINDING 66 66 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 90 90 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 110 110 S-adenosylmethioninamine.
{ECO:0000255|HAMAP-Rule:MF_00198}.
SEQUENCE 292 AA; 32856 MW; 9C9AC95C44D96550 CRC64;
MELGMFRLNI YQPGGPIGAL YPVEKILYHG RSQYQEIMIL VLRGFGKTLV LDGLIQSTES
DEHIYHETLV HPAMTVHPNP RRVLILGGGE GATLREVLKH NTVEKAVMVD IDGEVVRVAR
EYLPEWHQGA FDDPRAQVVI MDGFEYIKEA ARRGEDFDVI IMDLTDPFGP KIAAKLYTKE
AIGLVKSVLR SDGILVTQAG CAALFPEAFE KVYGSVKSLF AHAEEYGVWV PSFMYVNSFV
FASDKYRLTD LSMEEVDRRL RERGVETRFY SGLRHYTLIG LGGIRLLEGR GS


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