Spermidine synthase (P09158)

Identification
Name:Spermidine synthase
Synonyms:
  • Putrescine aminopropyltransferase
  • PAPT
  • SPDSY
Gene Name:speE
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM), which serves as an aminopropyl donor
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0S-Adenosylmethioninamine + 1.0Putrescine + 1.0Ethylenediamine ↔ 1.05'-Methylthioadenosine + 1.0Hydrogen ion + 1.0Spermidine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Cadaverine + 1.0S-Adenosylmethioninamine → 1.05'-Methylthioadenosine + 1.0Hydrogen ion + 1.0Aminopropylcadaverine
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0S-Adenosylmethioninamine + 1.0Putrescine ↔ 1.05'-Methylthioadenosine + 1.0Spermidine
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0S-Adenosylmethioninamine + 1.0Spermidine ↔ 1.05'-Methylthioadenosine + 1.0Spermine
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0S-Adenosylmethioninamine + 1.0Cadaverine ↔ 1.05'-Methylthioadenosine + 1.0Aminopropylcadaverine
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.05'-S-methyl-5'-thioadenosine
1.0Putrescine + 1.0S-Adenosylmethioninamine → 1.0Spermidine + 1.0Hydrogen ion + 1.05'-S-methyl-5'-thioadenosine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Cadaverine + 1.0Decarboxy-SAM → 1.0Aminopropylcadaverine + 1.05'-Methylthioadenosine + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Decarboxy-SAM + 1.0Putrescine → 1.05'-Methylthioadenosine + 1.0Spermidine + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0S-Adenosylmethioninamine + 1.0Putrescine + 1.0Ethylenediamine ↔ 1.05'-Methylthioadenosine + 1.0Hydrogen ion + 1.0Spermidine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Cadaverine + 1.0S-Adenosylmethioninamine → 1.05'-Methylthioadenosine + 1.0Hydrogen ion + 1.0Aminopropylcadaverine
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0S-Adenosylmethioninamine + 1.0Putrescine ↔ 1.05'-Methylthioadenosine + 1.0Spermidine
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0S-Adenosylmethioninamine + 1.0Putrescine → 1.05'-Methylthioadenosine + 1.0Spermidine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB011735'-MethylthioadenosineMetaboCard
ECMDB12189AminopropylcadaverineMetaboCard
ECMDB02322CadaverineMetaboCard
ECMDB20325Decarboxy-SAMMetaboCard
ECMDB20274EthylenediamineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01414PutrescineMetaboCard
ECMDB00988S-AdenosylmethioninamineMetaboCard
ECMDB01257SpermidineMetaboCard
ECMDB01256SpermineMetaboCard
GO Classification:
Function
catalytic activity
Gene Properties
Blattner:b0121
Gene OrientationCounterclockwise
Centisome Percentage:2.92
Left Sequence End135598
Right Sequence End136464
Gene Sequence:
>867 bp
ATGGCCGAAAAAAAACAGTGGCATGAAACGCTACACGACCAGTTTGGGCAGTACTTTGCG
GTAGATAACGTTCTGTATCATGAAAAGACCGATCACCAGGATCTGATCATTTTTGAGAAC
GCTGCATTTGGTCGCGTAATGGCGCTGGATGGCGTAGTACAAACCACCGAGCGCGACGAG
TTTATCTATCATGAGATGATGACCCATGTTCCGCTACTGGCCCATGGTCACGCGAAACAT
GTGCTGATTATCGGCGGCGGCGACGGTGCCATGCTGCGTGAAGTAACCCGACATAAAAAC
GTTGAGTCAATCACGATGGTGGAAATCGATGCGGGTGTCGTATCGTTCTGCCGTCAGTAT
CTACCCAACCATAACGCCGGTAGCTACGACGATCCGCGCTTTAAGCTGGTGATCGACGAT
GGCGTCAATTTCGTTAATCAAACCAGCCAGACCTTTGATGTCATTATCTCCGACTGCACC
GATCCTATCGGTCCCGGCGAAAGCCTTTTCACTTCGGCATTTTATGAAGGCTGCAAACGT
TGCCTGAATCCTGGCGGTATCTTCGTCGCACAAAACGGCGTCTGCTTTTTACAGCAGGAA
GAAGCCATCGACAGCCATCGCAAACTCAGCCATTACTTCAGCGACGTTGGCTTTTATCAG
GCGGCGATCCCGACCTATTACGGCGGTATCATGACTTTTGCATGGGCGACAGATAACGAC
GCCTTACGCCATCTCTCAACCGAAATTATTCAGGCGCGTTTTCTCGCCTCTGGCCTGAAA
TGCCGTTATTACAATCCGGCAATCCATACGGCAGCTTTTGCCTTACCTCAGTATCTGCAA
GACGCACTGGCTTCACAGCCGTCCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:288
Protein Molecular Weight:32321
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Spermidine synthase
MAEKKQWHETLHDQFGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDE
FIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVTRHKNVESITMVEIDAGVVSFCRQY
LPNHNAGSYDDPRFKLVIDDGVNFVNQTSQTFDVIISDCTDPIGPGESLFTSAFYEGCKR
CLNPGGIFVAQNGVCFLQQEEAIDSHRKLSHYFSDVGFYQAAIPTYYGGIMTFAWATDND
ALRHLSTEIIQARFLASGLKCRYYNPAIHTAAFALPQYLQDALASQPS
References
External Links:
ResourceLink
Uniprot ID:P09158
Uniprot Name:SPEE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21238974
Ecogene ID:EG10963
Ecocyc:EG10963
ColiBase:b0121
Kegg Gene:b0121
EchoBASE ID:EB0956
CCDB:SPEE_ECOLI
BacMap:16128114
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bowman, W. H., Tabor, C. W., Tabor, H. (1973). "Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli." J Biol Chem 248:2480-2486. Pubmed: 4572733
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Tabor, C. W., Tabor, H. (1987). "The speEspeD operon of Escherichia coli. Formation and processing of a proenzyme form of S-adenosylmethionine decarboxylase." J Biol Chem 262:16037-16040. Pubmed: 3316212
  • Tabor, C. W., Tabor, H., Xie, Q. W. (1986). "Spermidine synthase of Escherichia coli: localization of the speE gene." Proc Natl Acad Sci U S A 83:6040-6044. Pubmed: 3526348
  • Xie, Q. W., Tabor, C. W., Tabor, H. (1989). "Spermidine biosynthesis in Escherichia coli: promoter and termination regions of the speED operon." J Bacteriol 171:4457-4465. Pubmed: 2666401