SPEE_THET8
ID SPEE_THET8 Reviewed; 314 AA.
AC Q5SK28; P83816;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:15983049};
DE AltName: Full=Agmatine aminopropyltransferase {ECO:0000305|PubMed:15983049};
DE EC=2.5.1.104 {ECO:0000269|PubMed:15983049};
DE AltName: Full=N1-aminopropylagmatine synthase {ECO:0000305|PubMed:15983049};
DE AltName: Full=Norspermidine aminopropyltransferase {ECO:0000305|PubMed:21458463};
DE EC=2.5.1.126 {ECO:0000269|PubMed:21458463};
DE AltName: Full=Spermidine aminopropyltransferase {ECO:0000305|PubMed:21458463};
DE EC=2.5.1.79 {ECO:0000269|PubMed:21458463};
DE AltName: Full=Spermine synthase {ECO:0000305|PubMed:21458463};
DE EC=2.5.1.22 {ECO:0000269|PubMed:21458463};
DE AltName: Full=Thermine synthase {ECO:0000305|PubMed:21458463};
DE AltName: Full=Thermospermine synthase {ECO:0000305|PubMed:21458463};
DE AltName: Full=Triamine/agmatine aminopropyltransferase {ECO:0000303|PubMed:21458463};
DE Short=TAAPT {ECO:0000303|PubMed:21458463};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=TTHA0824;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=15983049; DOI=10.1074/jbc.m413332200;
RA Ohnuma M., Terui Y., Tamakoshi M., Mitome H., Niitsu M., Samejima K.,
RA Kawashima E., Oshima T.;
RT "N1-aminopropylagmatine, a new polyamine produced as a key intermediate in
RT polyamine biosynthesis of an extreme thermophile, Thermus thermophilus.";
RL J. Biol. Chem. 280:30073-30082(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of polyamine aminopropyltransferase from Thermus
RT thermophilus.";
RL Submitted (JUL-2003) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH
RP S-METHYL-5'-THIOADENOSINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=21458463; DOI=10.1016/j.jmb.2011.03.025;
RA Ohnuma M., Ganbe T., Terui Y., Niitsu M., Sato T., Tanaka N., Tamakoshi M.,
RA Samejima K., Kumasaka T., Oshima T.;
RT "Crystal structures and enzymatic properties of a triamine/agmatine
RT aminopropyltransferase from Thermus thermophilus.";
RL J. Mol. Biol. 408:971-986(2011).
CC -!- FUNCTION: Involved in the biosynthesis of polyamines which are thought
CC to support the growth of thermophilic microorganisms under high-
CC temperature conditions. It seems that long-chain and branched-chain of
CC polyamines effectively stabilize DNA and RNA, respectively. Catalyzes
CC the irreversible transfer of a propylamine group from the amino donor
CC S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1-
CC aminopropylagmatine. An efficient aminopropyltransferase activity has
CC been also observed with norspermidine which produces thermine, and
CC spermidine which produces spermine and thermospermine. The aminopropyl
CC activity with homospermidine, mitsubishine, thermine, 1,3-
CC diaminopropane, putrescine (1,4-diaminobutane), spermine and
CC caldopentamine are very low. The reaction involves a nucleophilic
CC attack on the C-3 methylene of the propylamine moiety adjacent to the
CC positively charged sulfur of decarboxy-AdoMet.
CC {ECO:0000269|PubMed:15983049, ECO:0000269|PubMed:21458463}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) +
CC N(1)-aminopropylagmatine + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:36487, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:58145, ChEBI:CHEBI:64335;
CC EC=2.5.1.104; Evidence={ECO:0000269|PubMed:15983049,
CC ECO:0000269|PubMed:21458463};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=norspermidine + S-adenosyl 3-(methylsulfanyl)propylamine =
CC H(+) + norspermine + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:42864,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC ChEBI:CHEBI:57920, ChEBI:CHEBI:58704; EC=2.5.1.126;
CC Evidence={ECO:0000269|PubMed:21458463};
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:21458463};
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:21458463};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.57 uM for norspermidine (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21458463};
CC KM=0.77 uM for agmatine (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:15983049};
CC KM=1.64 uM for S-adenosylmethioninamine (at pH 9 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:21458463};
CC KM=1.73 uM for spermidine (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21458463};
CC KM=38.3 uM for mitsubishine (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:21458463};
CC Note=kcat is 0.73 sec(-1) for aminopropyl transferase activity with
CC S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees
CC Celsius). kcat is 0.65 sec(-1) for aminopropyl transferase activity
CC with spermidine as substrate (at pH 9 and 37 degrees Celsius). kcat
CC is 0.53 sec(-1) for aminopropyl transferase activity with
CC norspermidine as substrate (at pH 9 and 37 degrees Celsius). kcat is
CC 0.37 sec(-1) for aminopropyl transferase activity with agmatine as
CC substrate (at pH 9 and 37 degrees Celsius). kcat is 0.29 sec(-1) for
CC aminopropyl transferase activity with mitsubishine as substrate (at
CC pH 9 and 37 degrees Celsius). {ECO:0000269|PubMed:21458463};
CC pH dependence:
CC Optimum pH is 8.5 at 60 degrees Celsius.
CC {ECO:0000269|PubMed:21458463};
CC Temperature dependence:
CC Optimum temperature is above 80 degrees Celsius.
CC {ECO:0000269|PubMed:21458463};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21458463}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking both speB and speE genes show
CC defective growth at 70 degrees Celsius and significantly defective
CC growth at 78 degrees Celsius. They accumulate agmatine and N1-
CC aminopropylagmatine. {ECO:0000269|PubMed:15983049}.
CC -!- MISCELLANEOUS: In T.thermophilus, the biosynthetic pathways of
CC spermidine operates via N1-aminopropylagmatine without the production
CC of putrescine. {ECO:0000305|PubMed:15983049}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
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DR EMBL; AP008226; BAD70647.1; -; Genomic_DNA.
DR RefSeq; WP_011172918.1; NC_006461.1.
DR RefSeq; YP_144090.1; NC_006461.1.
DR PDB; 1UIR; X-ray; 2.00 A; A/B=1-314.
DR PDB; 3ANX; X-ray; 2.50 A; A/B=1-314.
DR PDBsum; 1UIR; -.
DR PDBsum; 3ANX; -.
DR AlphaFoldDB; Q5SK28; -.
DR SMR; Q5SK28; -.
DR STRING; 300852.55772206; -.
DR EnsemblBacteria; BAD70647; BAD70647; BAD70647.
DR GeneID; 3168303; -.
DR KEGG; ttj:TTHA0824; -.
DR PATRIC; fig|300852.9.peg.818; -.
DR eggNOG; COG0421; Bacteria.
DR HOGENOM; CLU_048199_0_1_0; -.
DR OMA; LWPGQSF; -.
DR PhylomeDB; Q5SK28; -.
DR BioCyc; MetaCyc:MON-16736; -.
DR BRENDA; 2.5.1.104; 2305.
DR SABIO-RK; Q5SK28; -.
DR EvolutionaryTrace; Q5SK28; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043919; F:agmatine aminopropyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043918; F:cadaverine aminopropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016768; F:spermine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010487; F:thermospermine synthase activity; IDA:UniProtKB.
DR GO; GO:0006596; P:polyamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
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 Pfam; PF17284; Spermine_synt_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Polyamine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..314
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_1000012028"
FT DOMAIN 4..241
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 BINDING 33
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|PubMed:21458463, ECO:0007744|PDB:3ANX"
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 ECO:0000269|PubMed:21458463, ECO:0007744|PDB:3ANX"
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 ECO:0000269|PubMed:21458463, ECO:0007744|PDB:3ANX"
FT BINDING 158..161
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 168
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT STRAND 6..20
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1UIR"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1UIR"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3ANX"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 185..198
FT /evidence="ECO:0007829|PDB:1UIR"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:3ANX"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 232..243
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:1UIR"
FT HELIX 280..288
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1UIR"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1UIR"
SQ SEQUENCE 314 AA; 36006 MW; 4B6E438CFE60552A CRC64;
MDYGMYFFEH VTPYETLVRR MERVIASGKT PFQDYFLFES KGFGKVLILD KDVQSTERDE
YIYHETLVHP AMLTHPEPKR VLIVGGGEGA TLREVLKHPT VEKAVMVDID GELVEVAKRH
MPEWHQGAFD DPRAVLVIDD ARAYLERTEE RYDVVIIDLT DPVGEDNPAR LLYTVEFYRL
VKAHLNPGGV MGMQAGMILL THHRVHPVVH RTVREAFRYV RSYKNHIPGF FLNFGFLLAS
DAFDPAAFSE GVIEARIRER NLALRHLTAP YLEAMFVLPK DLLEALEKET MVSTDQNPFY
VTPEGEARQA PYKG
