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Polyamine aminopropyltransferase (Putrescine aminopropyltransferase) (PAPT) (Spermidine synthase) (SPDS) (SPDSY) (EC 2.5.1.16)

 SPEE_HELPY              Reviewed;         262 AA.
O25503;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
10-OCT-2018, entry version 104.
RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:16009566};
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:16009566};
Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:16009566};
Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:16009566};
EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:16009566};
Name=speE {ECO:0000255|HAMAP-Rule:MF_00198};
OrderedLocusNames=HP_0832;
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter
pylori).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Helicobacteraceae; Helicobacter.
NCBI_TaxID=85962;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700392 / 26695;
PubMed=9252185; DOI=10.1038/41483;
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
Smith H.O., Fraser C.M., Venter J.C.;
"The complete genome sequence of the gastric pathogen Helicobacter
pylori.";
Nature 388:539-547(1997).
[2]
CRYSTALLIZATION, AND SUBUNIT.
STRAIN=ATCC 700392 / 26695;
PubMed=15502329; DOI=10.1107/S0907444904021985;
Lu P.-K., Chien S.-Y., Tsai J.-Y., Fong C.-T., Lee M.-J., Huang H.,
Sun Y.-J.;
"Crystallization and preliminary X-ray diffraction analysis of
spermidine synthase from Helicobacter pylori.";
Acta Crystallogr. D 60:2067-2069(2004).
[3]
FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, ACTIVITY REGULATION,
SUBUNIT, AND SUBSTRATE SPECIFICITY.
STRAIN=ATCC 700392 / 26695;
PubMed=16009566; DOI=10.1016/j.pep.2005.04.017;
Lee M.-J., Huang C.-Y., Sun Y.-J., Huang H.;
"Cloning and characterization of spermidine synthase and its
implication in polyamine biosynthesis in Helicobacter pylori strain
26695.";
Protein Expr. Purif. 43:140-148(2005).
[4]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
PubMed=17357156; DOI=10.1002/prot.21315;
Lu P.K., Tsai J.Y., Chien H.Y., Huang H., Chu C.H., Sun Y.J.;
"Crystal structure of Helicobacter pylori spermidine synthase: a
Rossmann-like fold with a distinct active site.";
Proteins 67:743-754(2007).
-!- FUNCTION: Involved in the cell growth and proliferation. Catalyzes
the irreversible transfer of a propylamine group from the amino
donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine
(1,4-diaminobutane) to yield spermidine. Spermidine cannot be used
as an aminopropyl acceptor. {ECO:0000269|PubMed:16009566}.
-!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.
{ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:16009566}.
-!- ACTIVITY REGULATION: Inhibited by methylglyoxal
bis(cyclopentylamidinohydrazone)(MGBCP).
{ECO:0000269|PubMed:16009566}.
-!- PATHWAY: Amine and polyamine biosynthesis; spermidine
biosynthesis; spermidine from putrescine: step 1/1.
{ECO:0000255|HAMAP-Rule:MF_00198}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15502329,
ECO:0000269|PubMed:16009566, ECO:0000269|PubMed:17357156}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
-!- MASS SPECTROMETRY: Mass=31945; Method=Electrospray; Range=1-262;
Evidence={ECO:0000269|PubMed:16009566};
-!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
{ECO:0000255|HAMAP-Rule:MF_00198}.
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EMBL; AE000511; AAD07882.1; -; Genomic_DNA.
PIR; H64623; H64623.
RefSeq; NP_207625.1; NC_000915.1.
RefSeq; WP_000265099.1; NC_018939.1.
PDB; 2CMG; X-ray; 2.00 A; A/B=1-262.
PDB; 2CMH; X-ray; 2.30 A; A/B/C=1-262.
PDB; 5X0Z; X-ray; 2.70 A; A/B/C/D=1-262.
PDBsum; 2CMG; -.
PDBsum; 2CMH; -.
PDBsum; 5X0Z; -.
ProteinModelPortal; O25503; -.
SMR; O25503; -.
STRING; 85962.HP0832; -.
PaxDb; O25503; -.
EnsemblBacteria; AAD07882; AAD07882; HP_0832.
GeneID; 899365; -.
KEGG; heo:C694_04265; -.
KEGG; hpy:HP0832; -.
PATRIC; fig|85962.47.peg.887; -.
eggNOG; ENOG41084QV; Bacteria.
eggNOG; COG0421; LUCA.
KO; K00797; -.
OMA; ISFFPHF; -.
BioCyc; HPY:HP0832-MONOMER; -.
BRENDA; 2.5.1.16; 2604.
UniPathway; UPA00248; UER00314.
EvolutionaryTrace; O25503; -.
Proteomes; UP000000429; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
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; 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; PS51006; PABS_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Polyamine biosynthesis;
Reference proteome; Spermidine biosynthesis; Transferase.
CHAIN 1 262 Polyamine aminopropyltransferase.
/FTId=PRO_0000156483.
DOMAIN 1 249 PABS. {ECO:0000255|HAMAP-Rule:MF_00198}.
ACT_SITE 155 155 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 6 6 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
BINDING 29 29 S-adenosylmethioninamine.
{ECO:0000255|HAMAP-Rule:MF_00198}.
BINDING 83 83 Polyamine. {ECO:0000255|HAMAP-
Rule:MF_00198}.
STRAND 2 8 {ECO:0000244|PDB:2CMG}.
STRAND 11 16 {ECO:0000244|PDB:2CMG}.
STRAND 18 25 {ECO:0000244|PDB:2CMG}.
STRAND 30 36 {ECO:0000244|PDB:2CMG}.
TURN 37 39 {ECO:0000244|PDB:2CMG}.
STRAND 40 45 {ECO:0000244|PDB:2CMG}.
STRAND 48 51 {ECO:0000244|PDB:2CMG}.
HELIX 52 54 {ECO:0000244|PDB:2CMG}.
HELIX 56 67 {ECO:0000244|PDB:2CMG}.
STRAND 75 81 {ECO:0000244|PDB:2CMG}.
HELIX 84 90 {ECO:0000244|PDB:2CMG}.
STRAND 96 100 {ECO:0000244|PDB:2CMG}.
HELIX 104 107 {ECO:0000244|PDB:2CMG}.
HELIX 108 110 {ECO:0000244|PDB:2CMG}.
TURN 111 113 {ECO:0000244|PDB:2CMG}.
HELIX 117 121 {ECO:0000244|PDB:2CMG}.
STRAND 126 131 {ECO:0000244|PDB:2CMG}.
HELIX 132 134 {ECO:0000244|PDB:2CMG}.
STRAND 140 147 {ECO:0000244|PDB:2CMG}.
HELIX 151 158 {ECO:0000244|PDB:2CMG}.
STRAND 161 172 {ECO:0000244|PDB:2CMG}.
TURN 174 176 {ECO:0000244|PDB:2CMG}.
HELIX 178 189 {ECO:0000244|PDB:2CMG}.
STRAND 193 198 {ECO:0000244|PDB:2CMG}.
STRAND 208 216 {ECO:0000244|PDB:2CMG}.
TURN 219 222 {ECO:0000244|PDB:2CMG}.
HELIX 225 228 {ECO:0000244|PDB:2CMG}.
HELIX 239 244 {ECO:0000244|PDB:2CMG}.
HELIX 250 255 {ECO:0000244|PDB:2CMG}.
HELIX 256 258 {ECO:0000244|PDB:2CMG}.
SEQUENCE 262 AA; 30539 MW; FC368C83B7749C36 CRC64;
MWITQEITPY LRKEYTIEAK LLDVRSEHNI LEIFKSKDFG EIAMLNRQLL FKNFLHIESE
LLAHMGGCTK KELKEVLIVD GFDLELAHQL FKYDTHIDFV QADEKILDSF ISFFPHFHEV
KNNKNFTHAK QLLDLDIKKY DLIFCLQEPD IHRIDGLKRM LKEDGVFISV AKHPLLEHVS
MQNALKNMGG VFSVAMPFVA PLRILSNKGY IYASFKTHPL KDLMTPKIEA LTSVRYYNED
IHRAAFALPK NLQEVFKDNI KS


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