SPEE_PYRHO
ID SPEE_PYRHO Reviewed; 280 AA.
AC O57950;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=PH0211;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH
RP N1-AMINOPROPYLAGMATINE AND S-METHYL-5'-THIOADENOSINE, ACTIVE SITE, AND
RP SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of spermidine synthase from Pyrococcus horikoshII OT3.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine group
CC from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to
CC putrescine (1,4-diaminobutane) to yield spermidine. {ECO:0000255|HAMAP-
CC Rule:MF_00198}.
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 -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00198}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|Ref.2}.
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; BA000001; BAA29280.1; -; Genomic_DNA.
DR PIR; A71244; A71244.
DR PDB; 2E5W; X-ray; 2.00 A; A/B/C/D=1-280.
DR PDB; 2ZSU; X-ray; 2.20 A; A/B/C/D/E/F=1-280.
DR PDBsum; 2E5W; -.
DR PDBsum; 2ZSU; -.
DR AlphaFoldDB; O57950; -.
DR SMR; O57950; -.
DR STRING; 70601.3256597; -.
DR EnsemblBacteria; BAA29280; BAA29280; BAA29280.
DR KEGG; pho:PH0211; -.
DR eggNOG; arCOG00050; Archaea.
DR OMA; WIPSFGY; -.
DR UniPathway; UPA00248; UER00314.
DR EvolutionaryTrace; O57950; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
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; Polyamine biosynthesis; Spermidine biosynthesis;
KW Transferase.
FT CHAIN 1..280
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156531"
FT DOMAIN 7..240
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 ECO:0000305|Ref.2"
FT BINDING 32
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2E5W"
FT BINDING 63
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000305|Ref.2, ECO:0007744|PDB:2E5W"
FT BINDING 87
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000305|Ref.2, ECO:0007744|PDB:2E5W"
FT BINDING 107
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2E5W"
FT BINDING 144..145
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2E5W"
FT BINDING 161..164
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000305|Ref.2, ECO:0007744|PDB:2E5W"
FT BINDING 168
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000269|Ref.2, ECO:0007744|PDB:2E5W"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 14..28
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2E5W"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:2ZSU"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 185..197
FT /evidence="ECO:0007829|PDB:2E5W"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:2E5W"
FT STRAND 229..242
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:2E5W"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:2E5W"
SQ SEQUENCE 280 AA; 31970 MW; CFBEFAF6FDF6DC7E CRC64;
MRDMEFIEWY PRGYGVAFKV KRKILEEQSE YQKIEVYETE GFGKLLAIDG TVQLVTEGEK
SYHEPLVHPA MLAHPNPRRV LIIGGGDGGA IREVLKHEEV EEVIMVEIDK KVIEISAKYI
GIDGGILEKM LSDKHEKGKL IIGDGVKFIE ENSGFDVIIV DSTDPVGPAE MLFSEEFYKN
AYRALNDPGI YVTQAGSVYL FTDEFLTAYR KMRKVFDKVY YYSFPVIGYA SPWAFLVGVK
GSIDFMKVDA EKGKKLGLEY YDPDKHETLF QMPRYIVQML
