SPEE_THEMA
ID SPEE_THEMA Reviewed; 296 AA.
AC Q9WZC2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:11731804};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:11731804};
DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:11731804};
DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:17585781};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:17585781};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000303|PubMed:17585781};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:11731804, ECO:0000269|PubMed:17585781};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=TM_0654;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP ACTIVITY REGULATION.
RX PubMed=7641073; DOI=10.1016/1357-2725(95)00007-c;
RA Pegg A.E., Poulin R., Coward J.K.;
RT "Use of aminopropyltransferase inhibitors and of non-metabolizable analogs
RT to study polyamine regulation and function.";
RL Int. J. Biochem. Cell Biol. 27:425-442(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-76; ASP-101; ASP-170 AND
RP ASP-173, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX PubMed=17585781; DOI=10.1021/bi602498k;
RA Wu H., Min J., Ikeguchi Y., Zeng H., Dong A., Loppnau P., Pegg A.E.,
RA Plotnikov A.N.;
RT "Structure and mechanism of spermidine synthases.";
RL Biochemistry 46:8331-8339(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF APOENZYME AND COMPLEX WITH
RP SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=11731804; DOI=10.1038/nsb737;
RA Korolev S., Ikeguchi Y., Skarina T., Beasley S., Arrowsmith C., Edwards A.,
RA Joachimiak A., Pegg A.E., Savchenko A.;
RT "The crystal structure of spermidine synthase with a multisubstrate adduct
RT inhibitor.";
RL Nat. Struct. Biol. 9:27-31(2002).
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. It has lower
CC affinity and lower activity towards 1,3-diaminopropane, cadaverine
CC (1,5-diaminopentane), agmatine, norspermidine and spermidine (in
CC vitro). {ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:11731804,
CC ECO:0000269|PubMed:17585781}.
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:11731804, ECO:0000269|PubMed:17585781};
CC -!- ACTIVITY REGULATION: Strongly inhibited by S-adenosyl-1,8-diamino-3-
CC thiooctane. {ECO:0000269|PubMed:7641073}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.75 uM for S-adenosylmethioninamine (at pH 7.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:17585781};
CC KM=19 uM for putrescine (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:17585781};
CC Note=kcat is 0.77 sec(-1) for aminopropyltransferase activity with
CC putrescine as substrate (at pH 7.5 and 37 degrees Celsius). kcat is
CC 22.7 sec(-1) for aminopropyltransferase activity with putrescine as
CC substrate (at pH 7.5 and 80 degrees Celsius).
CC {ECO:0000269|PubMed:17585781};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11731804};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius.
CC {ECO:0000269|PubMed:11731804};
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:0000269|PubMed:11731804}.
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; AE000512; AAD35738.1; -; Genomic_DNA.
DR PIR; C72348; C72348.
DR RefSeq; NP_228463.1; NC_000853.1.
DR PDB; 1INL; X-ray; 1.50 A; A/B/C/D=1-296.
DR PDB; 1JQ3; X-ray; 1.80 A; A/B/C/D=1-296.
DR PDBsum; 1INL; -.
DR PDBsum; 1JQ3; -.
DR AlphaFoldDB; Q9WZC2; -.
DR SMR; Q9WZC2; -.
DR STRING; 243274.THEMA_01395; -.
DR DrugBank; DB02844; S-Adenosyl-1,8-Diamino-3-Thiooctane.
DR PRIDE; Q9WZC2; -.
DR EnsemblBacteria; AAD35738; AAD35738; TM_0654.
DR KEGG; tma:TM0654; -.
DR PATRIC; fig|243274.18.peg.273; -.
DR eggNOG; COG0421; Bacteria.
DR InParanoid; Q9WZC2; -.
DR OMA; LWPGQSF; -.
DR BRENDA; 2.5.1.16; 6331.
DR SABIO-RK; Q9WZC2; -.
DR UniPathway; UPA00248; UER00314.
DR EvolutionaryTrace; Q9WZC2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
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; Reference proteome;
KW Spermidine biosynthesis; Transferase.
FT CHAIN 1..296
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156513"
FT DOMAIN 16..251
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198,
FT ECO:0000305|PubMed:11731804"
FT BINDING 46
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000269|PubMed:11731804"
FT BINDING 77
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:11731804"
FT BINDING 101
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:11731804"
FT BINDING 121
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000269|PubMed:11731804"
FT BINDING 152..153
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000269|PubMed:11731804"
FT BINDING 170..173
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:11731804"
FT MUTAGEN 76
FT /note="Y->F: Reduces enzyme activity about 1000-fold."
FT /evidence="ECO:0000269|PubMed:17585781"
FT MUTAGEN 101
FT /note="D->I: Reduces enzyme activity over 10000-fold."
FT /evidence="ECO:0000269|PubMed:17585781"
FT MUTAGEN 170
FT /note="D->A: Reduces enzyme activity over 10000-fold."
FT /evidence="ECO:0000269|PubMed:17585781"
FT MUTAGEN 173
FT /note="D->A: Reduces enzyme activity about 500-fold."
FT /evidence="ECO:0000269|PubMed:17585781"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1INL"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1INL"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1JQ3"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:1INL"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:1INL"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:1INL"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:1INL"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:1INL"
SQ SEQUENCE 296 AA; 34142 MW; 9298A156B7481945 CRC64;
MRTLKELERE LQPRQHLWYF EYYTGNNVGL FMKMNRVIYS GQSDIQRIDI FENPDLGVVF
ALDGITMTTE KDEFMYHEML AHVPMFLHPN PKKVLIIGGG DGGTLREVLK HDSVEKAILC
EVDGLVIEAA RKYLKQTSCG FDDPRAEIVI ANGAEYVRKF KNEFDVIIID STDPTAGQGG
HLFTEEFYQA CYDALKEDGV FSAETEDPFY DIGWFKLAYR RISKVFPITR VYLGFMTTYP
SGMWSYTFAS KGIDPIKDFD PEKVRKFNKE LKYYNEEVHV ASFALPNFVK KELGLM
