SPEE1_HYPBU
ID SPEE1_HYPBU Reviewed; 292 AA.
AC A2BIX4;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Polyamine aminopropyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:19822146};
DE AltName: Full=Caldopentamine synthase {ECO:0000305|PubMed:19822146};
DE AltName: Full=Norspermidine aminopropyltransferase {ECO:0000305|PubMed:19822146};
DE EC=2.5.1.126 {ECO:0000269|PubMed:19822146};
DE AltName: Full=Norspermine aminopropyltransferase {ECO:0000305|PubMed:19822146};
DE EC=2.5.1.127 {ECO:0000269|PubMed:19822146};
DE AltName: Full=Norspermine synthase {ECO:0000305|PubMed:19822146};
DE AltName: Full=Spermidine aminopropyltransferase {ECO:0000305|PubMed:19822146};
DE EC=2.5.1.79 {ECO:0000269|PubMed:19822146};
DE AltName: Full=Thermospermine synthase {ECO:0000305|PubMed:19822146};
DE AltName: Full=Triamine/tetramine aminopropyltransferase {ECO:0000303|PubMed:19822146};
GN Name=speE1 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:19822146};
GN OrderedLocusNames=Hbut_0057;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=19822146; DOI=10.1016/j.febslet.2009.10.014;
RA Knott J.M.;
RT "Biosynthesis of long-chain polyamines by crenarchaeal polyamine synthases
RT from Hyperthermus butylicus and Pyrobaculum aerophilum.";
RL FEBS Lett. 583:3519-3524(2009).
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 norspermidine,
CC spermidine and norspermine to yield norspermine, thermospermine and
CC caldopentamine, respectively. It can also synthesize sym-norspermidine
CC (bis(3-aminopropyl)amine) from 1,3-diaminopropane with a very low
CC activity. The biosynthesis of caldohexamine and caldoheptamine from
CC caldopentamine has been also observed. {ECO:0000269|PubMed:19822146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=norspermine + S-adenosyl 3-(methylsulfanyl)propylamine =
CC caldopentamine + 2 H(+) + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:42868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:58704, ChEBI:CHEBI:82769;
CC EC=2.5.1.127; Evidence={ECO:0000269|PubMed:19822146};
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:19822146};
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:19822146};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_00198}.
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, ECO:0000255|RuleBase:RU003836}.
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DR EMBL; CP000493; ABM79935.1; -; Genomic_DNA.
DR AlphaFoldDB; A2BIX4; -.
DR SMR; A2BIX4; -.
DR STRING; 415426.Hbut_0057; -.
DR EnsemblBacteria; ABM79935; ABM79935; Hbut_0057.
DR KEGG; hbu:Hbut_0057; -.
DR eggNOG; arCOG00050; Archaea.
DR HOGENOM; CLU_048199_0_1_2; -.
DR OMA; WIPSFGY; -.
DR OrthoDB; 77175at2157; -.
DR BioCyc; MetaCyc:MON-21056; -.
DR BRENDA; 2.5.1.127; 10772.
DR Proteomes; UP000002593; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR11558; PTHR11558; 1.
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; Transferase.
FT CHAIN 1..292
FT /note="Polyamine aminopropyltransferase 1"
FT /id="PRO_0000431724"
FT DOMAIN 1..244
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 35
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 66
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 90
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 110
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 142..143
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 292 AA; 32856 MW; 9C9AC95C44D96550 CRC64;
MELGMFRLNI YQPGGPIGAL YPVEKILYHG RSQYQEIMIL VLRGFGKTLV LDGLIQSTES
DEHIYHETLV HPAMTVHPNP RRVLILGGGE GATLREVLKH NTVEKAVMVD IDGEVVRVAR
EYLPEWHQGA FDDPRAQVVI MDGFEYIKEA ARRGEDFDVI IMDLTDPFGP KIAAKLYTKE
AIGLVKSVLR SDGILVTQAG CAALFPEAFE KVYGSVKSLF AHAEEYGVWV PSFMYVNSFV
FASDKYRLTD LSMEEVDRRL RERGVETRFY SGLRHYTLIG LGGIRLLEGR GS
