(data stored in SCRATCH zone)

SWISSPROT: C8U1J1_ECO10

ID   C8U1J1_ECO10            Unreviewed;       288 AA.
AC   C8U1J1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Polyamine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
DE   AltName: Full=Putrescine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
DE            Short=PAPT {ECO:0000256|HAMAP-Rule:MF_00198};
DE   AltName: Full=Spermidine synthase {ECO:0000256|HAMAP-Rule:MF_00198};
DE            Short=SPDS {ECO:0000256|HAMAP-Rule:MF_00198};
DE            Short=SPDSY {ECO:0000256|HAMAP-Rule:MF_00198};
DE            EC=2.5.1.16 {ECO:0000256|HAMAP-Rule:MF_00198};
GN   Name=speE {ECO:0000256|HAMAP-Rule:MF_00198,
GN   ECO:0000313|EMBL:BAI28999.1};
GN   OrderedLocusNames=ECO103_0121 {ECO:0000313|EMBL:BAI28999.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28999.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28999.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|HAMAP-Rule:MF_00198}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine =
CC         H(+) + S-methyl-5'-thioadenosine + spermidine;
CC         Xref=Rhea:RHEA:12721, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC         ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:326268;
CC         EC=2.5.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00198,
CC         ECO:0000256|RuleBase:RU003837};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; spermidine
CC       biosynthesis; spermidine from putrescine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00198}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00198}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS01095326}.
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00198, ECO:0000256|RuleBase:RU003836}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00198}.
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DR   EMBL; AP010958; BAI28999.1; -; Genomic_DNA.
DR   RefSeq; WP_000818411.1; NC_013353.1.
DR   SMR; C8U1J1; -.
DR   EnsemblBacteria; BAI28999; BAI28999; ECO103_0121.
DR   KEGG; eoh:ECO103_0121; -.
DR   HOGENOM; HOG000256146; -.
DR   KO; K00797; -.
DR   OMA; LWPGQSF; -.
DR   BioCyc; ECOL585395:ECO103_RS00620-MONOMER; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000000959; 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   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   InterPro; IPR037163; Spermidine_synt_N_sf.
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; C8U1J1.
DR   SWISS-2DPAGE; C8U1J1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS01095314};
KW   Polyamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198,
KW   ECO:0000256|PROSITE-ProRule:PRU00354};
KW   Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198,
KW   ECO:0000256|RuleBase:RU003837};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00198, ECO:0000256|PROSITE-
KW   ProRule:PRU00354, ECO:0000256|RuleBase:RU003836}.
FT   DOMAIN        9    238       PABS. {ECO:0000259|PROSITE:PS51006}.
FT   REGION       53     54       Polyamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00198}.
FT   REGION      140    141       S-adenosylmethioninamine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   REGION      159    161       Polyamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00198}.
FT   ACT_SITE    158    158       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198, ECO:0000256|PROSITE-ProRule:
FT                                PRU00354}.
FT   BINDING      33     33       S-adenosylmethioninamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   BINDING      64     64       Polyamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   BINDING      88     88       Polyamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   BINDING     108    108       S-adenosylmethioninamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   BINDING     165    165       S-adenosylmethioninamine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                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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