SPEE_ECOLI
ID SPEE_ECOLI Reviewed; 288 AA.
AC P09158;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:4572733};
DE AltName: Full=Cadaverine aminopropyltransferase {ECO:0000305|PubMed:4572733};
DE EC=2.5.1.- {ECO:0000269|PubMed:4572733};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000305|PubMed:4572733};
DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine aminopropyltransferase {ECO:0000305|PubMed:4572733};
DE EC=2.5.1.79 {ECO:0000269|PubMed:4572733};
DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:4572733};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:4572733};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:4572733};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:23001854, ECO:0000269|PubMed:4572733};
DE AltName: Full=Spermine synthase {ECO:0000303|PubMed:4572733};
DE EC=2.5.1.22 {ECO:0000269|PubMed:4572733};
DE AltName: Full=Thermospermine synthase {ECO:0000305|PubMed:4572733};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:3526348};
GN OrderedLocusNames=b0121, JW0117;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3316212; DOI=10.1016/s0021-9258(18)47692-2;
RA Tabor C.W., Tabor H.;
RT "The speEspeD operon of Escherichia coli. Formation and processing of a
RT proenzyme form of S-adenosylmethionine decarboxylase.";
RL J. Biol. Chem. 262:16037-16040(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RX PubMed=2666401; DOI=10.1128/jb.171.8.4457-4465.1989;
RA Xie Q.W., Tabor C.W., Tabor H.;
RT "Spermidine biosynthesis in Escherichia coli: promoter and termination
RT regions of the speED operon.";
RL J. Bacteriol. 171:4457-4465(1989).
RN [6]
RP PROTEIN SEQUENCE OF 2-31.
RX PubMed=3526348; DOI=10.1073/pnas.83.16.6040;
RA Tabor C.W., Tabor H., Xie Q.W.;
RT "Spermidine synthase of Escherichia coli: localization of the speE gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6040-6044(1986).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=4572733; DOI=10.1016/s0021-9258(19)44133-1;
RA Bowman W.H., Tabor C.W., Tabor H.;
RT "Spermidine biosynthesis. Purification and properties of propylamine
RT transferase from Escherichia coli.";
RL J. Biol. Chem. 248:2480-2486(1973).
RN [8]
RP ACTIVITY REGULATION, AND REACTION MECHANISM.
RX PubMed=6993485; DOI=10.1016/s0021-9258(20)79698-5;
RA Zappia V., Cacciapuoti G., Pontoni G., Oliva A.;
RT "Mechanism of propylamine-transfer reactions. Kinetic and inhibition
RT studies on spermidine synthase from Escherichia coli.";
RL J. Biol. Chem. 255:7276-7280(1980).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=6406265; DOI=10.1016/0014-5793(82)80600-5;
RA Pegg A.E., Bitonti A.J., McCann P.P., Coward J.K.;
RT "Inhibition of bacterial aminopropyltransferases by S-adenosyl-1,8-diamino-
RT 3-thiooctane and by dicyclohexylamine.";
RL FEBS Lett. 155:192-196(1983).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=6508744; DOI=10.1042/bj2230823;
RA Mattila T., Honkanen-Buzalski T., Poso H.;
RT "Reversible inhibition of bacterial growth after specific inhibition of
RT spermidine synthase by dicyclohexylamine.";
RL Biochem. J. 223:823-830(1984).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-158; CYS-159; THR-160;
RP ASP-161; PRO-162; ILE-163 AND PRO-165, ACTIVE SITE, BIOPHYSICOCHEMICAL
RP PROPERTIES, MASS SPECTROMETRY, AND REACTION MECHANISM.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23001854; DOI=10.1007/s12033-012-9599-3;
RA Lee M.J., Yang Y.T., Lin V., Huang H.;
RT "Site-directed mutations of the gatekeeping loop region affect the activity
RT of Escherichia coli spermidine synthase.";
RL Mol. Biotechnol. 54:572-580(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=20051267; DOI=10.1016/j.jsb.2009.12.024;
RA Zhou X., Chua T.K., Tkaczuk K.L., Bujnicki J.M., Sivaraman J.;
RT "The crystal structure of Escherichia coli spermidine synthase SpeE reveals
RT a unique substrate-binding pocket.";
RL J. Struct. Biol. 169:277-285(2010).
CC -!- FUNCTION: Involved in the biosynthesis of polyamines which play a
CC significant role in the structural and functional organization in the
CC chromoid of E.coli by compacting DNA and neutralizing negative charges.
CC Catalyzes the irreversible transfer (ping-pong mechanism) of a
CC propylamine group from the amino donor S-adenosylmethioninamine
CC (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield
CC spermidine. Cadaverine (1,5-diaminopentane) and spermidine can also be
CC used as the propylamine acceptor. {ECO:0000269|PubMed:23001854,
CC ECO:0000269|PubMed:4572733}.
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:23001854, ECO:0000269|PubMed:4572733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) +
CC S-methyl-5'-thioadenosine + spermine; Xref=Rhea:RHEA:19973,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:45725,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:57834; EC=2.5.1.22;
CC Evidence={ECO:0000269|PubMed:4572733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cadaverine + S-adenosyl 3-(methylsulfanyl)propylamine =
CC aminopropylcadaverine + H(+) + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:33387, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:58384, ChEBI:CHEBI:64858;
CC Evidence={ECO:0000269|PubMed:4572733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) +
CC S-methyl-5'-thioadenosine + thermospermine; Xref=Rhea:RHEA:30515,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:59903; EC=2.5.1.79;
CC Evidence={ECO:0000269|PubMed:4572733};
CC -!- ACTIVITY REGULATION: The activity is thought to be regulated mainly by
CC the availability of decarboxylated S-adenosylmethionine. Inhibited by
CC dicyclohexylamine, S-adenosyl-1,8-diamino-3-thiooctane (AdoDATO),
CC sulfonium-deaminated analogs of S-adenosyl(5')-3-methylthiopropylamine,
CC p-hydroxymercuribenzoate and N-ethylmaleimide.
CC {ECO:0000269|PubMed:4572733, ECO:0000269|PubMed:6406265,
CC ECO:0000269|PubMed:6508744, ECO:0000269|PubMed:6993485}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 uM for S-adenosylmethionine {ECO:0000269|PubMed:4572733};
CC KM=12 uM for putrescine {ECO:0000269|PubMed:4572733};
CC KM=77.77 uM for putrescine (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:23001854};
CC KM=84.98 uM for S-adenosylmethionine (at pH 7.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:23001854};
CC Vmax=2 umol/min/mg enzyme {ECO:0000269|PubMed:4572733};
CC Vmax=0.560 umol/min/mg enzyme (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:23001854};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:23001854};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:23001854};
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:20051267,
CC ECO:0000269|PubMed:4572733}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- MASS SPECTROMETRY: Mass=33823; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:23001854};
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02804; AAA24643.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73232.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96695.1; -; Genomic_DNA.
DR PIR; A29778; SYECSD.
DR RefSeq; NP_414663.1; NC_000913.3.
DR RefSeq; WP_000818411.1; NZ_STEB01000010.1.
DR PDB; 3O4F; X-ray; 2.90 A; A/B/C/D/E/F/G/H=1-288.
DR PDBsum; 3O4F; -.
DR AlphaFoldDB; P09158; -.
DR SMR; P09158; -.
DR BioGRID; 4262092; 263.
DR BioGRID; 852039; 1.
DR IntAct; P09158; 11.
DR STRING; 511145.b0121; -.
DR SWISS-2DPAGE; P09158; -.
DR jPOST; P09158; -.
DR PaxDb; P09158; -.
DR PRIDE; P09158; -.
DR EnsemblBacteria; AAC73232; AAC73232; b0121.
DR EnsemblBacteria; BAB96695; BAB96695; BAB96695.
DR GeneID; 66671591; -.
DR GeneID; 947726; -.
DR KEGG; ecj:JW0117; -.
DR KEGG; eco:b0121; -.
DR PATRIC; fig|1411691.4.peg.2161; -.
DR EchoBASE; EB0956; -.
DR eggNOG; COG0421; Bacteria.
DR HOGENOM; CLU_048199_0_0_6; -.
DR InParanoid; P09158; -.
DR OMA; LWPGQSF; -.
DR PhylomeDB; P09158; -.
DR BioCyc; EcoCyc:SPERMIDINESYN-MON; -.
DR BioCyc; MetaCyc:SPERMIDINESYN-MON; -.
DR BRENDA; 2.5.1.16; 2026.
DR UniPathway; UPA00248; UER00314.
DR PRO; PR:P09158; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043918; F:cadaverine aminopropyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004766; F:spermidine synthase activity; IDA:EcoCyc.
DR GO; GO:0016768; F:spermine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010487; F:thermospermine synthase activity; IDA:UniProtKB.
DR GO; GO:0008295; P:spermidine biosynthetic process; IMP:EcoCyc.
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; IPR030373; PABS_CS.
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 TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Polyamine biosynthesis;
KW Reference proteome; Spermidine biosynthesis; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3526348"
FT CHAIN 2..288
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156479"
FT DOMAIN 9..238
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000305|PubMed:23001854"
FT BINDING 33
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 64
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 88
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 108
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 140..141
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 158..161
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 165
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT MUTAGEN 158
FT /note="D->A: Completely inactive."
FT /evidence="ECO:0000269|PubMed:23001854"
FT MUTAGEN 159
FT /note="C->A: Reduction of 23% of the aminopropyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:23001854"
FT MUTAGEN 159
FT /note="C->S: No influence on aminopropyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:23001854"
FT MUTAGEN 160
FT /note="T->A: Reduction of aminopropyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23001854"
FT MUTAGEN 161
FT /note="D->A: Completely inactive."
FT /evidence="ECO:0000269|PubMed:23001854"
FT MUTAGEN 162
FT /note="P->A: No influence on aminopropyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:23001854"
FT MUTAGEN 163
FT /note="I->A: No influence on aminopropyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:23001854"
FT MUTAGEN 165
FT /note="P->A: Reduction of aminopropyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23001854"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 11..28
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:3O4F"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3O4F"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:3O4F"
FT TURN 141..145
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 182..197
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3O4F"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:3O4F"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:3O4F"
SQ 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
