SPEE_PYRAE
ID SPEE_PYRAE Reviewed; 291 AA.
AC Q8ZXM4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:19822146};
DE AltName: Full=Diamine/triamine aminopropyltransferase {ECO:0000303|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 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};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=PAE1203;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
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 and 1,3-
CC diaminopropane to yield norspermine, and to spermidine to yield
CC thermospermine. It can also synthesize thermospermine from putrescine
CC (1,4-diaminobutane) and caldopentamine from norspermine with a very low
CC activity. The biosynthesis of caldohexamine and caldoheptamine from
CC caldopentamine has been also observed. {ECO:0000255|HAMAP-
CC Rule:MF_00198, 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}.
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DR EMBL; AE009441; AAL63322.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZXM4; -.
DR SMR; Q8ZXM4; -.
DR STRING; 178306.PAE1203; -.
DR EnsemblBacteria; AAL63322; AAL63322; PAE1203.
DR KEGG; pai:PAE1203; -.
DR PATRIC; fig|178306.9.peg.890; -.
DR eggNOG; arCOG00050; Archaea.
DR HOGENOM; CLU_048199_0_1_2; -.
DR InParanoid; Q8ZXM4; -.
DR OMA; WIPSFGY; -.
DR BRENDA; 2.5.1.126; 5239.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
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..291
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156529"
FT DOMAIN 5..245
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 36
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 67
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 91
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 111
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 143..144
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 291 AA; 32806 MW; 9320B183DF573C4A CRC64;
MSKVPGPIVL MEPLSGKTSL IIKINAIHVS KRSKYQGILI VDTDDYGRTL VLDDYIQSSY
YDEIYYHESL VHPAVTTHPR PSDVLILGGG EGATLREVLK HNTVKRAVMV DIDGDVVELS
KKYLPQMHQG AFDDPRSEVR IEDGFVYVEN ALKRGEKFDV VIMDLTDPYS SDIAKQLYTP
EFFGKVKRLL REDGIVVTQA GNSFYFPEAY DYVLQGVKGN FPIIAEYSVW IPSFGYAVNF
VLGSLKHDPH SLSAEEVDKR LSERGVRAEF YSGKTHIALM NMPVIKKILR V
