(data stored in ACNUC7421 zone)

SWISSPROT: SPEE_ECODH

ID   SPEE_ECODH              Reviewed;         288 AA.
AC   B1XC96;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   30-AUG-2017, entry version 62.
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};
GN   OrderedLocusNames=ECDH10B_0101;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine
CC       group from the amino donor S-adenosylmethioninamine (decarboxy-
CC       AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
CC       {ECO:0000255|HAMAP-Rule:MF_00198}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine +
CC       putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.
CC       {ECO:0000255|HAMAP-Rule:MF_00198}.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; spermidine
CC       biosynthesis; spermidine from putrescine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00198}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; CP000948; ACB01300.1; -; Genomic_DNA.
DR   RefSeq; WP_000818411.1; NC_010473.1.
DR   ProteinModelPortal; B1XC96; -.
DR   SMR; B1XC96; -.
DR   EnsemblBacteria; ACB01300; ACB01300; ECDH10B_0101.
DR   KEGG; ecd:ECDH10B_0101; -.
DR   eggNOG; ENOG4105CCX; Bacteria.
DR   eggNOG; COG0421; LUCA.
DR   HOGENOM; HOG000256146; -.
DR   KO; K00797; -.
DR   OMA; YPCGHIG; -.
DR   UniPathway; UPA00248; UER00314.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.30.140.10; -; 1.
DR   HAMAP; MF_00198; Spermidine_synth; 1.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR030373; PABS_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR001045; Spermi_synthase.
DR   InterPro; IPR035246; Spermidine_synt_N.
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   3: Inferred from homology;
DR   PRODOM; B1XC96.
DR   SWISS-2DPAGE; B1XC96.
KW   Cytoplasm; Polyamine biosynthesis; Spermidine biosynthesis;
KW   Transferase.
FT   CHAIN         1    288       Polyamine aminopropyltransferase.
FT                                /FTId=PRO_1000099281.
FT   DOMAIN        9    238       PABS. {ECO:0000255|HAMAP-Rule:MF_00198}.
FT   REGION       53     54       Polyamine binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00198}.
FT   REGION      140    141       S-adenosylmethioninamine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00198}.
FT   REGION      159    161       Polyamine binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00198}.
FT   ACT_SITE    158    158       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00198}.
FT   BINDING       9      9       Polyamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00198}.
FT   BINDING      33     33       S-adenosylmethioninamine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00198}.
FT   BINDING      64     64       Polyamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00198}.
FT   BINDING      88     88       Polyamine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00198}.
FT   BINDING     108    108       S-adenosylmethioninamine.
FT                                {ECO:0000255|HAMAP-Rule:MF_00198}.
FT   BINDING     165    165       S-adenosylmethioninamine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00198}.
SQ   SEQUENCE   288 AA;  32321 MW;  31AE026FF6199E9F CRC64;
     MAEKKQWHET LHDQFGQYFA VDNVLYHEKT DHQDLIIFEN AAFGRVMALD GVVQTTERDE
     FIYHEMMTHV PLLAHGHAKH VLIIGGGDGA MLREVTRHKN VESITMVEID AGVVSFCRQY
     LPNHNAGSYD DPRFKLVIDD GVNFVNQTSQ TFDVIISDCT DPIGPGESLF TSAFYEGCKR
     CLNPGGIFVA QNGVCFLQQE EAIDSHRKLS HYFSDVGFYQ AAIPTYYGGI MTFAWATDND
     ALRHLSTEII QARFLASGLK CRYYNPAIHT AAFALPQYLQ DALASQPS
//

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