SPEE_HELPY
ID SPEE_HELPY Reviewed; 262 AA.
AC O25503;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:16009566};
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:16009566};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:16009566};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:16009566};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:16009566};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=HP_0832;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP CRYSTALLIZATION, AND SUBUNIT.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=15502329; DOI=10.1107/s0907444904021985;
RA Lu P.-K., Chien S.-Y., Tsai J.-Y., Fong C.-T., Lee M.-J., Huang H.,
RA Sun Y.-J.;
RT "Crystallization and preliminary X-ray diffraction analysis of spermidine
RT synthase from Helicobacter pylori.";
RL Acta Crystallogr. D 60:2067-2069(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, ACTIVITY REGULATION,
RP SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=16009566; DOI=10.1016/j.pep.2005.04.017;
RA Lee M.-J., Huang C.-Y., Sun Y.-J., Huang H.;
RT "Cloning and characterization of spermidine synthase and its implication in
RT polyamine biosynthesis in Helicobacter pylori strain 26695.";
RL Protein Expr. Purif. 43:140-148(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=17357156; DOI=10.1002/prot.21315;
RA Lu P.K., Tsai J.Y., Chien H.Y., Huang H., Chu C.H., Sun Y.J.;
RT "Crystal structure of Helicobacter pylori spermidine synthase: a Rossmann-
RT like fold with a distinct active site.";
RL Proteins 67:743-754(2007).
CC -!- FUNCTION: Involved in the cell growth and proliferation. Catalyzes the
CC irreversible transfer of a propylamine group from the amino donor S-
CC adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-
CC diaminobutane) to yield spermidine. Spermidine cannot be used as an
CC aminopropyl acceptor. {ECO:0000269|PubMed:16009566}.
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:16009566};
CC -!- ACTIVITY REGULATION: Inhibited by methylglyoxal
CC bis(cyclopentylamidinohydrazone)(MGBCP). {ECO:0000269|PubMed:16009566}.
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. {ECO:0000269|PubMed:15502329,
CC ECO:0000269|PubMed:16009566, ECO:0000269|PubMed:17357156}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- MASS SPECTROMETRY: Mass=31945; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16009566};
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
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DR EMBL; AE000511; AAD07882.1; -; Genomic_DNA.
DR PIR; H64623; H64623.
DR RefSeq; NP_207625.1; NC_000915.1.
DR RefSeq; WP_000265099.1; NC_018939.1.
DR PDB; 2CMG; X-ray; 2.00 A; A/B=1-262.
DR PDB; 2CMH; X-ray; 2.30 A; A/B/C=1-262.
DR PDB; 5X0Z; X-ray; 2.70 A; A/B/C/D=1-262.
DR PDBsum; 2CMG; -.
DR PDBsum; 2CMH; -.
DR PDBsum; 5X0Z; -.
DR AlphaFoldDB; O25503; -.
DR SMR; O25503; -.
DR STRING; 85962.C694_04265; -.
DR PaxDb; O25503; -.
DR EnsemblBacteria; AAD07882; AAD07882; HP_0832.
DR KEGG; hpy:HP_0832; -.
DR PATRIC; fig|85962.47.peg.887; -.
DR eggNOG; COG0421; Bacteria.
DR OMA; EYTIEAK; -.
DR PhylomeDB; O25503; -.
DR BRENDA; 2.5.1.16; 2604.
DR UniPathway; UPA00248; UER00314.
DR EvolutionaryTrace; O25503; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004766; F:spermidine synthase activity; IBA:GO_Central.
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; 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 PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Polyamine biosynthesis; Reference proteome;
KW Spermidine biosynthesis; Transferase.
FT CHAIN 1..262
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156483"
FT DOMAIN 1..249
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 29
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 83
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:2CMG"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2CMG"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 161..172
FT /evidence="ECO:0007829|PDB:2CMG"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:2CMG"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:2CMG"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:2CMG"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2CMG"
SQ 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
