SPEE2_HYPBU
ID SPEE2_HYPBU Reviewed; 305 AA.
AC A2BJU2;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Polyamine aminopropyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:19822146};
DE AltName: Full=1,3-diaminopropane aminopropyltransferase {ECO:0000305|PubMed:19822146};
DE EC=2.5.1.23 {ECO:0000269|PubMed:19822146};
DE AltName: Full=Sym-norspermidine synthase {ECO:0000305|PubMed:19822146};
GN Name=speE2 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:19822146};
GN OrderedLocusNames=Hbut_0383;
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 1,3-diaminopropane to
CC yield sym-norspermidine (bis(3-aminopropyl)amine). It can also
CC synthesize thermospermine from spermidine with a very low activity.
CC {ECO:0000269|PubMed:19822146}.
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: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; ABM80253.1; -; Genomic_DNA.
DR RefSeq; WP_011821571.1; NC_008818.1.
DR AlphaFoldDB; A2BJU2; -.
DR SMR; A2BJU2; -.
DR STRING; 415426.Hbut_0383; -.
DR EnsemblBacteria; ABM80253; ABM80253; Hbut_0383.
DR GeneID; 4782683; -.
DR KEGG; hbu:Hbut_0383; -.
DR eggNOG; arCOG00050; Archaea.
DR HOGENOM; CLU_048199_0_1_2; -.
DR OMA; YGSDEHE; -.
DR OrthoDB; 77175at2157; -.
DR BioCyc; MetaCyc:MON-21055; -.
DR BRENDA; 2.5.1.23; 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; IPR037163; Spermidine_synt_N_sf.
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..305
FT /note="Polyamine aminopropyltransferase 2"
FT /id="PRO_0000431725"
FT DOMAIN 7..242
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 161
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"
FT BINDING 170
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
SQ SEQUENCE 305 AA; 34437 MW; A04CBE54D469B5EF CRC64;
MAQRLPWRFV AEWTSEGEMV LREVKRIYAA GATRYQEYMI AELAGIGKAL VLDGKVQSSI
LDEHWYHEAL VHPILLAHQC PRKVLVIGGG EGATVREVLR HSCVEHVTMV DIDEELVELA
KKHLAEWHQG AFSSDKLELV IGDGRRYVEN CHRKYDAIIL DLVDPMEGGP AARLYTLEFY
RAVKGCLRPG GAVVTQATSP TLSPRVYAVI RNTLAKVFTI VRPYVSYVRS YNGLWGFVAA
SDTVDPAKLS AKEVDELIAA RIRGQLRFYD GETHEWMFRL PLPVRQVLSE TRDYATDEKP
VYVPV
