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Polyamine aminopropyltransferase (Cadaverine aminopropyltransferase) (EC 2.5.1.-) (Putrescine aminopropyltransferase) (PAPT) (Spermidine aminopropyltransferase) (EC 2.5.1.79) (Spermidine synthase) (SPDS) (SPDSY) (EC 2.5.1.16) (Spermine synthase) (EC 2.5.1.22) (Thermospermine synthase)

 SPEE_ECOLI              Reviewed;         288 AA.
P09158;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 159.
RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:4572733};
AltName: Full=Cadaverine aminopropyltransferase {ECO:0000305|PubMed:4572733};
EC=2.5.1.- {ECO:0000269|PubMed:4572733};
AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000305|PubMed:4572733};
Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
AltName: Full=Spermidine aminopropyltransferase {ECO:0000305|PubMed:4572733};
EC=2.5.1.79 {ECO:0000269|PubMed:4572733};
AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:4572733};
Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:4572733};
Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:4572733};
EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:23001854, ECO:0000269|PubMed:4572733};
AltName: Full=Spermine synthase {ECO:0000303|PubMed:4572733};
EC=2.5.1.22 {ECO:0000269|PubMed:4572733};
AltName: Full=Thermospermine synthase {ECO:0000305|PubMed:4572733};
Name=speE {ECO:0000255|HAMAP-Rule:MF_00198,
ECO:0000303|PubMed:3526348}; OrderedLocusNames=b0121, JW0117;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3316212;
Tabor C.W., Tabor H.;
"The speEspeD operon of Escherichia coli. Formation and processing of
a proenzyme form of S-adenosylmethionine decarboxylase.";
J. Biol. Chem. 262:16037-16040(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8202364; DOI=10.1093/nar/22.9.1637;
Fujita N., Mori H., Yura T., Ishihama A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
2.4-4.1 min (110,917-193,643 bp) region.";
Nucleic Acids Res. 22:1637-1639(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
PubMed=2666401; DOI=10.1128/jb.171.8.4457-4465.1989;
Xie Q.W., Tabor C.W., Tabor H.;
"Spermidine biosynthesis in Escherichia coli: promoter and termination
regions of the speED operon.";
J. Bacteriol. 171:4457-4465(1989).
[6]
PROTEIN SEQUENCE OF 2-31.
PubMed=3526348; DOI=10.1073/pnas.83.16.6040;
Tabor C.W., Tabor H., Xie Q.W.;
"Spermidine synthase of Escherichia coli: localization of the speE
gene.";
Proc. Natl. Acad. Sci. U.S.A. 83:6040-6044(1986).
[7]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
PubMed=4572733;
Bowman W.H., Tabor C.W., Tabor H.;
"Spermidine biosynthesis. Purification and properties of propylamine
transferase from Escherichia coli.";
J. Biol. Chem. 248:2480-2486(1973).
[8]
ENZYME REGULATION, AND REACTION MECHANISM.
PubMed=6993485;
Zappia V., Cacciapuoti G., Pontoni G., Oliva A.;
"Mechanism of propylamine-transfer reactions. Kinetic and inhibition
studies on spermidine synthase from Escherichia coli.";
J. Biol. Chem. 255:7276-7280(1980).
[9]
ENZYME REGULATION.
PubMed=6406265; DOI=10.1016/0014-5793(82)80600-5;
Pegg A.E., Bitonti A.J., McCann P.P., Coward J.K.;
"Inhibition of bacterial aminopropyltransferases by S-adenosyl-1,8-
diamino-3-thiooctane and by dicyclohexylamine.";
FEBS Lett. 155:192-196(1983).
[10]
ENZYME REGULATION.
PubMed=6508744; DOI=10.1042/bj2230823;
Mattila T., Honkanen-Buzalski T., Poso H.;
"Reversible inhibition of bacterial growth after specific inhibition
of spermidine synthase by dicyclohexylamine.";
Biochem. J. 223:823-830(1984).
[11]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-158; CYS-159;
THR-160; ASP-161; PRO-162; ILE-163 AND PRO-165, ACTIVE SITE,
BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, AND REACTION
MECHANISM.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=23001854; DOI=10.1007/s12033-012-9599-3;
Lee M.J., Yang Y.T., Lin V., Huang H.;
"Site-directed mutations of the gatekeeping loop region affect the
activity of Escherichia coli spermidine synthase.";
Mol. Biotechnol. 54:572-580(2013).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND SUBUNIT.
PubMed=20051267; DOI=10.1016/j.jsb.2009.12.024;
Zhou X., Chua T.K., Tkaczuk K.L., Bujnicki J.M., Sivaraman J.;
"The crystal structure of Escherichia coli spermidine synthase SpeE
reveals a unique substrate-binding pocket.";
J. Struct. Biol. 169:277-285(2010).
-!- FUNCTION: Involved in the biosynthesis of polyamines which play a
significant role in the structural and functional organization in
the chromoid of E.coli by compacting DNA and neutralizing negative
charges. Catalyzes the irreversible transfer (ping-pong mechanism)
of a propylamine group from the amino donor S-
adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-
diaminobutane) to yield spermidine. Cadaverine (1,5-
diaminopentane) and spermidine can also be used as the propylamine
acceptor. {ECO:0000269|PubMed:23001854,
ECO:0000269|PubMed:4572733}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.
{ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:23001854,
ECO:0000269|PubMed:4572733}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
spermidine = S-methyl-5'-thioadenosine + spermine.
{ECO:0000269|PubMed:4572733}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine + 1,5-
diaminopentane = S-methyl-5'-thioadenosine + N-(3-aminopropyl)-
1,5-diaminopentane. {ECO:0000269|PubMed:4572733}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
spermidine = S-methyl-5'-thioadenosine + thermospermine + H(+).
{ECO:0000269|PubMed:4572733}.
-!- ENZYME REGULATION: The activity is thought to be regulated mainly
by the availability of decarboxylated S-adenosylmethionine.
Inhibited by dicyclohexylamine, S-adenosyl-1,8-diamino-3-
thiooctane (AdoDATO), sulfonium-deaminated analogs of S-
adenosyl(5')-3-methylthiopropylamine, p-hydroxymercuribenzoate and
N-ethylmaleimide. {ECO:0000269|PubMed:4572733,
ECO:0000269|PubMed:6406265, ECO:0000269|PubMed:6508744,
ECO:0000269|PubMed:6993485}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.2 uM for S-adenosylmethionine {ECO:0000269|PubMed:4572733};
KM=12 uM for putrescine {ECO:0000269|PubMed:4572733};
KM=77.77 uM for putrescine (at pH 7.5 and 37 degrees Celsius)
{ECO:0000269|PubMed:23001854};
KM=84.98 uM for S-adenosylmethionine (at pH 7.5 and 37 degrees
Celsius) {ECO:0000269|PubMed:23001854};
Vmax=2 umol/min/mg enzyme {ECO:0000269|PubMed:4572733};
Vmax=0.560 umol/min/mg enzyme (at pH 7.5 and 37 degrees Celsius)
{ECO:0000269|PubMed:23001854};
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:23001854};
Temperature dependence:
Optimum temperature is 50 degrees Celsius.
{ECO:0000269|PubMed:23001854};
-!- PATHWAY: Amine and polyamine biosynthesis; spermidine
biosynthesis; spermidine from putrescine: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_00198}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20051267,
ECO:0000269|PubMed:4572733}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
-!- MASS SPECTROMETRY: Mass=33823; Method=Electrospray; Range=1-288;
Evidence={ECO:0000269|PubMed:23001854};
-!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
{ECO:0000255|HAMAP-Rule:MF_00198}.
-----------------------------------------------------------------------
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EMBL; J02804; AAA24643.1; -; Genomic_DNA.
EMBL; U00096; AAC73232.1; -; Genomic_DNA.
EMBL; AP009048; BAB96695.1; -; Genomic_DNA.
PIR; A29778; SYECSD.
RefSeq; NP_414663.1; NC_000913.3.
RefSeq; WP_000818411.1; NZ_LN832404.1.
PDB; 3O4F; X-ray; 2.90 A; A/B/C/D/E/F/G/H=1-288.
PDBsum; 3O4F; -.
ProteinModelPortal; P09158; -.
SMR; P09158; -.
BioGrid; 4262092; 263.
IntAct; P09158; 11.
STRING; 316385.ECDH10B_0101; -.
SWISS-2DPAGE; P09158; -.
PaxDb; P09158; -.
PRIDE; P09158; -.
EnsemblBacteria; AAC73232; AAC73232; b0121.
EnsemblBacteria; BAB96695; BAB96695; BAB96695.
GeneID; 947726; -.
KEGG; ecj:JW0117; -.
KEGG; eco:b0121; -.
PATRIC; fig|1411691.4.peg.2161; -.
EchoBASE; EB0956; -.
EcoGene; EG10963; speE.
eggNOG; ENOG4105CCX; Bacteria.
eggNOG; COG0421; LUCA.
HOGENOM; HOG000256146; -.
InParanoid; P09158; -.
KO; K00797; -.
OMA; LWPGQSF; -.
PhylomeDB; P09158; -.
BioCyc; EcoCyc:SPERMIDINESYN-MONOMER; -.
BioCyc; MetaCyc:SPERMIDINESYN-MONOMER; -.
BRENDA; 2.5.1.16; 2026.
UniPathway; UPA00248; UER00314.
PRO; PR:P09158; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0043918; F:cadaverine aminopropyltransferase activity; IDA:UniProtKB.
GO; GO:0004766; F:spermidine synthase activity; IDA:EcoCyc.
GO; GO:0016768; F:spermine synthase activity; IEA:UniProtKB-EC.
GO; GO:0010487; F:thermospermine synthase activity; IDA:UniProtKB.
GO; GO:0008295; P:spermidine biosynthetic process; IMP:EcoCyc.
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;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Polyamine biosynthesis; Reference proteome; Spermidine biosynthesis;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3526348}.
CHAIN 2 288 Polyamine aminopropyltransferase.
/FTId=PRO_0000156479.
DOMAIN 9 238 PABS. {ECO:0000255|HAMAP-Rule:MF_00198}.
REGION 53 54 Polyamine binding. {ECO:0000255|HAMAP-
Rule:MF_00198}.
REGION 140 141 S-adenosylmethioninamine binding.
{ECO:0000255|HAMAP-Rule:MF_00198}.
REGION 159 161 Polyamine binding. {ECO:0000255|HAMAP-
Rule:MF_00198}.
ACT_SITE 158 158 Proton acceptor.
{ECO:0000305|PubMed:23001854}.
BINDING 9 9 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 33 33 S-adenosylmethioninamine.
{ECO:0000255|HAMAP-Rule:MF_00198}.
BINDING 64 64 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 88 88 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 108 108 S-adenosylmethioninamine.
{ECO:0000255|HAMAP-Rule:MF_00198}.
BINDING 165 165 S-adenosylmethioninamine; via carbonyl
oxygen. {ECO:0000255|HAMAP-
Rule:MF_00198}.
MUTAGEN 158 158 D->A: Completely inactive.
{ECO:0000269|PubMed:23001854}.
MUTAGEN 159 159 C->A: Reduction of 23% of the
aminopropyltransferase activity.
{ECO:0000269|PubMed:23001854}.
MUTAGEN 159 159 C->S: No influence on
aminopropyltransferase activity.
{ECO:0000269|PubMed:23001854}.
MUTAGEN 160 160 T->A: Reduction of aminopropyltransferase
activity. {ECO:0000269|PubMed:23001854}.
MUTAGEN 161 161 D->A: Completely inactive.
{ECO:0000269|PubMed:23001854}.
MUTAGEN 162 162 P->A: No influence on
aminopropyltransferase activity.
{ECO:0000269|PubMed:23001854}.
MUTAGEN 163 163 I->A: No influence on
aminopropyltransferase activity.
{ECO:0000269|PubMed:23001854}.
MUTAGEN 165 165 P->A: Reduction of aminopropyltransferase
activity. {ECO:0000269|PubMed:23001854}.
STRAND 5 8 {ECO:0000244|PDB:3O4F}.
STRAND 11 28 {ECO:0000244|PDB:3O4F}.
STRAND 30 32 {ECO:0000244|PDB:3O4F}.
STRAND 35 40 {ECO:0000244|PDB:3O4F}.
TURN 41 43 {ECO:0000244|PDB:3O4F}.
STRAND 44 49 {ECO:0000244|PDB:3O4F}.
STRAND 52 56 {ECO:0000244|PDB:3O4F}.
TURN 57 59 {ECO:0000244|PDB:3O4F}.
HELIX 60 74 {ECO:0000244|PDB:3O4F}.
STRAND 80 85 {ECO:0000244|PDB:3O4F}.
HELIX 90 96 {ECO:0000244|PDB:3O4F}.
STRAND 103 109 {ECO:0000244|PDB:3O4F}.
HELIX 111 120 {ECO:0000244|PDB:3O4F}.
HELIX 122 125 {ECO:0000244|PDB:3O4F}.
HELIX 128 130 {ECO:0000244|PDB:3O4F}.
STRAND 134 139 {ECO:0000244|PDB:3O4F}.
TURN 141 145 {ECO:0000244|PDB:3O4F}.
STRAND 152 158 {ECO:0000244|PDB:3O4F}.
HELIX 173 180 {ECO:0000244|PDB:3O4F}.
STRAND 182 197 {ECO:0000244|PDB:3O4F}.
HELIX 200 212 {ECO:0000244|PDB:3O4F}.
STRAND 214 221 {ECO:0000244|PDB:3O4F}.
STRAND 226 229 {ECO:0000244|PDB:3O4F}.
STRAND 231 238 {ECO:0000244|PDB:3O4F}.
HELIX 242 244 {ECO:0000244|PDB:3O4F}.
HELIX 247 255 {ECO:0000244|PDB:3O4F}.
HELIX 266 272 {ECO:0000244|PDB:3O4F}.
HELIX 277 282 {ECO:0000244|PDB:3O4F}.
SEQUENCE 288 AA; 32321 MW; 31AE026FF6199E9F CRC64;
MAEKKQWHET LHDQFGQYFA VDNVLYHEKT DHQDLIIFEN AAFGRVMALD GVVQTTERDE
FIYHEMMTHV PLLAHGHAKH VLIIGGGDGA MLREVTRHKN VESITMVEID AGVVSFCRQY
LPNHNAGSYD DPRFKLVIDD GVNFVNQTSQ TFDVIISDCT DPIGPGESLF TSAFYEGCKR
CLNPGGIFVA QNGVCFLQQE EAIDSHRKLS HYFSDVGFYQ AAIPTYYGGI MTFAWATDND
ALRHLSTEII QARFLASGLK CRYYNPAIHT AAFALPQYLQ DALASQPS


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