SPEE_PYRFU
ID SPEE_PYRFU Reviewed; 281 AA.
AC Q8U4G1;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:17545282};
DE AltName: Full=1,3-diaminopropane aminopropyltransferase {ECO:0000305|PubMed:17545282};
DE EC=2.5.1.23 {ECO:0000269|PubMed:17545282};
DE AltName: Full=Agmatine aminopropyltransferase {ECO:0000305|PubMed:17545282};
DE AltName: Full=Agmatine/cadaverine aminopropyltransferase {ECO:0000303|PubMed:17545282};
DE AltName: Full=Cadaverine aminopropyltransferase {ECO:0000305|PubMed:17545282};
DE EC=2.5.1.- {ECO:0000269|PubMed:17545282};
DE AltName: Full=N(1)-aminopropylagmatine synthase {ECO:0000305|PubMed:17545282};
DE EC=2.5.1.104 {ECO:0000269|PubMed:17545282};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000305|PubMed:17545282};
DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:17545282};
DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000305|PubMed:17545282};
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:17545282};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=PF0127;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-281, PROTEIN SEQUENCE,
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=17545282; DOI=10.1128/jb.00151-07;
RA Cacciapuoti G., Porcelli M., Moretti M.A., Sorrentino F., Concilio L.,
RA Zappia V., Liu Z.J., Tempel W., Schubot F., Rose J.P., Wang B.C.,
RA Brereton P.S., Jenney F.E., Adams M.W.;
RT "The first agmatine/cadaverine aminopropyl transferase: biochemical and
RT structural characterization of an enzyme involved in polyamine biosynthesis
RT in the hyperthermophilic archaeon Pyrococcus furiosus.";
RL J. Bacteriol. 189:6057-6067(2007).
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 agmatine, cadaverine (1,5-diaminopentane), putrescine (1,4-
CC diaminobutane) and 1,3-diaminopropane. The biosynthesis of norspermine
CC and thermospermine from sym-norspermidine and spermidine has been also
CC observed, but with a very low activity. The reaction involves a
CC nucleophilic attack on the C-3 methylene of the propylamine moiety
CC adjacent to the positively charged sulfur of decarboxy-AdoMet.
CC {ECO:0000269|PubMed:17545282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cadaverine + S-adenosyl 3-(methylsulfanyl)propylamine =
CC aminopropylcadaverine + H(+) + S-methyl-5'-thioadenosine;
CC Xref=Rhea:RHEA:33387, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:58384, ChEBI:CHEBI:64858;
CC Evidence={ECO:0000269|PubMed:17545282};
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:17545282};
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:17545282};
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:17545282};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 uM for agmatine {ECO:0000269|PubMed:17545282};
CC KM=1877 uM for 1,3-diaminopropane {ECO:0000269|PubMed:17545282};
CC KM=3767 uM for cadaverine {ECO:0000269|PubMed:17545282};
CC KM=7703 uM for putrescine {ECO:0000269|PubMed:17545282};
CC Note=kcat is 2.09 sec(-1) for aminopropyl transferase activity with
CC cadaverine as amine acceptor. kcat is 0.18 sec(-1) for aminopropyl
CC transferase activity with putrescine as amine acceptor. kcat is 0.1
CC sec(-1) for aminopropyl transferase activity with agmatine as amine
CC acceptor. kcat is 0.06 sec(-1) for aminopropyl transferase activity
CC with 1,3-diaminopropane as amine acceptor.
CC {ECO:0000269|PubMed:17545282};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. The enzyme is highly
CC thermophilic. 50% activity is still observable at 103 degrees
CC Celsius. {ECO:0000269|PubMed:17545282};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00198}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17545282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- INDUCTION: At temperatures higher than 95 degrees Celsius or by
CC oxidative shock. {ECO:0000269|PubMed:17545282}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
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DR EMBL; AE009950; AAL80251.1; -; Genomic_DNA.
DR RefSeq; WP_011011239.1; NZ_CP023154.1.
DR PDB; 1MJF; X-ray; 1.80 A; A/B=1-281.
DR PDBsum; 1MJF; -.
DR AlphaFoldDB; Q8U4G1; -.
DR SMR; Q8U4G1; -.
DR STRING; 186497.PF0127; -.
DR EnsemblBacteria; AAL80251; AAL80251; PF0127.
DR GeneID; 41711914; -.
DR KEGG; pfu:PF0127; -.
DR PATRIC; fig|186497.12.peg.132; -.
DR eggNOG; arCOG00050; Archaea.
DR HOGENOM; CLU_048199_0_1_2; -.
DR OMA; LWPGQSF; -.
DR OrthoDB; 77175at2157; -.
DR PhylomeDB; Q8U4G1; -.
DR BRENDA; 2.5.1.104; 5243.
DR SABIO-RK; Q8U4G1; -.
DR UniPathway; UPA00248; UER00314.
DR EvolutionaryTrace; Q8U4G1; -.
DR Proteomes; UP000001013; 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; IDA:UniProtKB.
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 PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Polyamine biosynthesis;
KW Reference proteome; Spermidine biosynthesis; Transferase.
FT CHAIN 1..281
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156530"
FT DOMAIN 6..238
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 31
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 62
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 86
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 105
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"
FT BINDING 159..162
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 166
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1MJF"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:1MJF"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 183..195
FT /evidence="ECO:0007829|PDB:1MJF"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:1MJF"
FT STRAND 227..240
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:1MJF"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:1MJF"
SQ SEQUENCE 281 AA; 32334 MW; 72C97AE45BE1C487 CRC64;
MERAFIEWYP RGYGVAFKIK KKIYEKLSKY QKIEVYETEG FGRLLALDGT VQLVTLGERS
YHEPLVHPAM LAHPKPKRVL VIGGGDGGTV REVLQHDVDE VIMVEIDEDV IMVSKDLIKI
DNGLLEAMLN GKHEKAKLTI GDGFEFIKNN RGFDVIIADS TDPVGPAKVL FSEEFYRYVY
DALNNPGIYV TQAGSVYLFT DELISAYKEM KKVFDRVYYY SFPVIGYASP WAFLVGVKGD
IDFTKIDRER AKKLQLEYYD PLMHETLFQM PKYIRETLQR L
