S-adenosylmethionine decarboxylase proenzyme (P0A7F6)

Identification
Name:S-adenosylmethionine decarboxylase proenzyme
Synonyms:
  • AdoMetDC
  • SAMDC
  • S-adenosylmethionine decarboxylase beta chain
  • S-adenosylmethionine decarboxylase alpha chain
Gene Name:speD
Enzyme Class:
Biological Properties
General Function:Involved in adenosylmethionine decarboxylase activity
Specific Function:Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0S-Adenosylmethionine + 1.0Hydrogen ion ↔ 1.0S-Adenosylmethioninamine + 1.0Carbon dioxide
ReactionCard
SMPDB Reactions:
1.0S-adenosyl-L-methionine+1.0Thumb → 1.0Thumb+1.0Thumb
1.0S-adenosyl-L-methionine + 1.0Hydrogen ion → 1.0Carbon dioxide + 1.0S-Adenosylmethioninamine
ReactionCard
1.0S-adenosyl-L-methionine+1.0Thumb → 1.0Thumb+1.0Thumb
1.0S-adenosyl-L-methionine + 1.0Hydrogen ion → 1.0Decarboxy-SAM + 1.0Carbon dioxide
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0S-Adenosylmethionine + 1.0Hydrogen ion ↔ 1.0S-Adenosylmethioninamine + 1.0Carbon dioxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB04030Carbon dioxideMetaboCard
ECMDB20325Decarboxy-SAMMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00988S-AdenosylmethioninamineMetaboCard
ECMDB01185S-AdenosylmethionineMetaboCard
GO Classification:
Function
adenosylmethionine decarboxylase activity
carbon-carbon lyase activity
carboxy-lyase activity
catalytic activity
lyase activity
Process
cellular amino acid and derivative metabolic process
cellular amino acid derivative metabolic process
cellular biogenic amine metabolic process
cellular metabolic process
metabolic process
polyamine biosynthetic process
polyamine metabolic process
spermidine biosynthetic process
Gene Properties
Blattner:b0120
Gene OrientationCounterclockwise
Centisome Percentage:2.91
Left Sequence End134788
Right Sequence End135582
Gene Sequence:
>795 bp
TTGAAAAAACTGAAACTGCATGGCTTTAATAATCTGACCAAAAGTCTGAGTTTTTGTATT
TACGATATCTGCTACGCCAAAACTGCCGAAGAGCGCGACGGTTATATTGCTTATATCGAT
GAACTCTATAATGCCAACCGTCTGACCGAAATCCTGTCAGAAACCTGTTCCATTATCGGG
GCTAATATTCTTAACATCGCCCGCCAGGATTACGAACCACAGGGTGCCAGCGTCACTATT
CTGGTGAGTGAAGAACCGGTTGACCCGAAACTCATCGACAAAACAGAACACCCCGGCCCA
CTGCCAGAAACGGTCGTTGCCCATCTTGATAAAAGTCATATTTGCGTACATACCTACCCG
GAAAGTCATCCTGAAGGCGGTTTATGTACCTTCCGCGCCGATATTGAAGTCTCTACCTGC
GGCGTGATTTCTCCGCTGAAGGCGCTGAATTACCTGATCCACCAGCTTGAGTCCGATATC
GTAACCATTGATTATCGCGTGCGCGGTTTTACCCGCGACATTAACGGTATGAAGCACTTT
ATCGACCATGAGATTAATTCGATTCAGAACTTTATGTCTGACGATATGAAGGCGCTGTAT
GACATGGTGGATGTGAACGTCTATCAGGAAAATATCTTCCATACCAAGATGTTGCTTAAA
GAGTTCGACCTTAAGCACTACATGTTCCACACCAAACCGGAAGACTTAACCGACAGCGAG
CGCCAGGAAATTACCGCTGCGCTGTGGAAAGAAATGCGCGAGATTTATTACGGGCGCAAT
ATGCCAGCTGTTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:264
Protein Molecular Weight:30384
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>S-adenosylmethionine decarboxylase proenzyme
MKKLKLHGFNNLTKSLSFCIYDICYAKTAEERDGYIAYIDELYNANRLTEILSETCSIIG
ANILNIARQDYEPQGASVTILVSEEPVDPKLIDKTEHPGPLPETVVAHLDKSHICVHTYP
ESHPEGGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTIDYRVRGFTRDINGMKHF
IDHEINSIQNFMSDDMKALYDMVDVNVYQENIFHTKMLLKEFDLKHYMFHTKPEDLTDSE
RQEITAALWKEMREIYYGRNMPAV
References
External Links:
ResourceLink
Uniprot ID:P0A7F6
Uniprot Name:SPED_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21238973
Ecogene ID:EG10962
Ecocyc:EG10962
ColiBase:b0120
Kegg Gene:b0120
EchoBASE ID:EB0955
CCDB:SPED_ECOLI
BacMap:16128113
General Reference:
  • Anton, D. L., Kutny, R. (1987). "Escherichia coli S-adenosylmethionine decarboxylase. Subunit structure, reductive amination, and NH2-terminal sequences." J Biol Chem 262:2817-2822. Pubmed: 3546296
  • 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
  • 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
  • Lu, Z. J., Markham, G. D. (2007). "Metal ion activation of S-adenosylmethionine decarboxylase reflects cation charge density." Biochemistry 46:8172-8180. Pubmed: 17567041
  • Markham, G. D., Tabor, C. W., Tabor, H. (1982). "S-adenosylmethionine decarboxylase of Escherichia coli. Studies on the covalently linked pyruvate required for activity." J Biol Chem 257:12063-12068. Pubmed: 6749853
  • Minton, K. W., Tabor, H., Tabor, C. W. (1990). "Paraquat toxicity is increased in Escherichia coli defective in the synthesis of polyamines." Proc Natl Acad Sci U S A 87:2851-2855. Pubmed: 2181453
  • 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