SPEE_SACS2
ID SPEE_SACS2 Reviewed; 301 AA.
AC Q9UXE4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:3096734};
DE AltName: Full=1,3-diaminopropane aminopropyltransferase {ECO:0000305|PubMed:3096734};
DE EC=2.5.1.23 {ECO:0000269|PubMed:3096734};
DE AltName: Full=Norspermidine aminopropyltransferase {ECO:0000305|PubMed:3096734};
DE EC=2.5.1.126 {ECO:0000269|PubMed:3096734};
DE AltName: Full=Norspermine synthase {ECO:0000305|PubMed:3096734};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000305|PubMed:3096734};
DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:3096734};
DE AltName: Full=Spermidine aminopropyltransferase {ECO:0000305|PubMed:3096734};
DE EC=2.5.1.79 {ECO:0000269|PubMed:3096734};
DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000305|PubMed:3096734};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Sym-norspermidine synthase {ECO:0000305|PubMed:3096734};
DE AltName: Full=Thermospermine synthase {ECO:0000305|PubMed:3096734};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=SSO0757;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=3096734; DOI=10.1111/j.1432-1033.1986.tb10442.x;
RA Cacciapuoti G., Porcelli M., Carteni-Farina M., Gambacorta A., Zappia V.;
RT "Purification and characterization of propylamine transferase from
RT Sulfolobus solfataricus, an extreme thermophilic archaebacterium.";
RL Eur. J. Biochem. 161:263-271(1986).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=1541263; DOI=10.1111/j.1432-1033.1992.tb16657.x;
RA Facchiano F., Ragone R., Porcelli M., Cacciapuoti G., Colonna G.;
RT "Effect of temperature on the propylamine transferase from Sulfolobus
RT solfataricus, an extreme thermophilic archaebacterium. 1. Conformational
RT behavior of the oligomeric enzyme in solution.";
RL Eur. J. Biochem. 204:473-482(1992).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1541264; DOI=10.1111/j.1432-1033.1992.tb16658.x;
RA Ragone R., Facchiano F., Cacciapuoti G., Porcelli M., Colonna G.;
RT "Effect of temperature on the propylamine transferase from Sulfolobus
RT solfataricus, an extreme thermophilic archaebacterium. 2. Denaturation and
RT structural stability.";
RL Eur. J. Biochem. 204:483-490(1992).
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 various amine acceptors
CC such as putrescine (1,4-diaminobutane), 1,3-diaminopropane, sym-
CC norspermidine and spermidine. The biosynthesis of caldopentamine from
CC norspermine has been also observed, but with a very low activity. The
CC reaction involves a nucleophilic attack on the C-3 methylene of the
CC propylamine moiety adjacent to the positively charged sulfur of
CC decarboxy-AdoMet. S-adenosylmethioninamine is the only amino donor.
CC {ECO:0000269|PubMed:3096734}.
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:3096734};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=propane-1,3-diamine + S-adenosyl 3-(methylsulfanyl)propylamine
CC = H(+) + norspermidine + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:23244, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:57484, ChEBI:CHEBI:57920; EC=2.5.1.23;
CC Evidence={ECO:0000269|PubMed:3096734};
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:3096734};
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:3096734};
CC -!- ACTIVITY REGULATION: Competitively inhibited by 5-methylthioadenosine,
CC 5-methylthiotubercidin, S-adenosyl(5)-3-thiopropylamine and S-adenosyl-
CC 3-thio-l,8-diaminooctane. {ECO:0000269|PubMed:3096734}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.9 uM for S-adenosylmethioninamine (at 78 degrees Celsius and at
CC pH 7.5) {ECO:0000269|PubMed:3096734};
CC KM=954 uM for sym-nor-spermidine (at 78 degrees Celsius and at pH
CC 7.5) {ECO:0000269|PubMed:3096734};
CC KM=1539 uM for spermidine (at 78 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:1541263, ECO:0000269|PubMed:1541264,
CC ECO:0000269|PubMed:3096734};
CC KM=1675 uM for 1,3-diaminopropane (at 78 degrees Celsius and at pH
CC 7.5) {ECO:0000269|PubMed:3096734};
CC KM=3850 uM for putrescine (at 78 degrees Celsius and at pH 7.5)
CC {ECO:0000269|PubMed:3096734};
CC Vmax=1980 nmol/min/mg enzyme with 1,3-diaminopropane as substrate (at
CC 78 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:3096734};
CC Vmax=662 nmol/min/mg enzyme with putrescine as substrate (at 78
CC degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:3096734};
CC Vmax=316 nmol/min/mg enzyme with sym-nor-spermidine as substrate (at
CC 78 degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:3096734};
CC Vmax=124 nmol/min/mg enzyme with spermidine as substrate (at 78
CC degrees Celsius and at pH 7.5) {ECO:0000269|PubMed:3096734};
CC pH dependence:
CC Optimum pH is 7.5 with one-half of the maximal activity at pH 6 and
CC 9.5. {ECO:0000269|PubMed:3096734};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. No loss of activity is
CC observable even after exposure of the purified enzyme to 100 degrees
CC Celsius for 1 hour. At 60 and 110 degrees Celsius the reaction rate
CC is one-half of the maximal value, and a residual 20% activity is
CC still observable at 120 degrees Celsius.
CC {ECO:0000269|PubMed:3096734};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00198}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:1541263,
CC ECO:0000269|PubMed:3096734}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
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DR EMBL; Y18930; CAB57546.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41051.1; -; Genomic_DNA.
DR PIR; D90224; D90224.
DR RefSeq; WP_009991336.1; NC_002754.1.
DR AlphaFoldDB; Q9UXE4; -.
DR SMR; Q9UXE4; -.
DR STRING; 273057.SSO0757; -.
DR EnsemblBacteria; AAK41051; AAK41051; SSO0757.
DR GeneID; 44129755; -.
DR KEGG; sso:SSO0757; -.
DR PATRIC; fig|273057.12.peg.753; -.
DR eggNOG; arCOG00050; Archaea.
DR HOGENOM; CLU_048199_0_1_2; -.
DR InParanoid; Q9UXE4; -.
DR OMA; LWPGQSF; -.
DR PhylomeDB; Q9UXE4; -.
DR UniPathway; UPA00248; UER00314.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004766; F:spermidine synthase activity; IDA:UniProtKB.
DR GO; GO:0050314; F:sym-norspermidine synthase activity; IDA:UniProtKB.
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 Cytoplasm; Polyamine biosynthesis; Reference proteome;
KW Spermidine biosynthesis; Transferase.
FT CHAIN 1..301
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156534"
FT DOMAIN 4..240
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 159
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 BINDING 64
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 89
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 109
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 141..142
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 301 AA; 34854 MW; 2A6A1897C71E773D CRC64;
MFGWHWLLEW QTPYEFHGHL IEKVLAEEKT PYQHVTLVEF TRFGKGLIID GKVQSTLYDE
HIYHELLVHP LLLSLTKPPK SVLILGGGEG ATLREVLKYK SVEKAVMVDI DEKVIEFAKK
YLYEWHQGAF EDKRTNLVIT DGLKFIKETK EKYDAIILDL TDPIKNSTSY MLYTKEFYEK
LREILNERGG IVTQATSPSF SLEVYVTIYN TIKEVFKEAS ASYTYMASFD GLWGFVYGGV
RPDLLSEDEV DSKINERIDG QLRFYDGYSH KISFSLPKNI KSEFQKITKI STEKDPIYVP
A
