RegulonDB

Gene
Name:	speD
Synonym(s):	ECK0119, EG10962, b0120
Genome position(nucleotides):	134788 <-- 135582 Genome Browser
Strand:	reverse
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	46.16
External database links:

ASAP:	ABE-0000416
CGSC:	158
ECHOBASE:	EB0955
ECOLIHUB:	speD
NCBI-GENE:	947719
OU-MICROARRAY:	b0120
STRING:	511145.b0120
COLOMBOS:	speD

Gene

Name:

speD

Synonym(s):

ECK0119, EG10962, b0120

Genome position(nucleotides):

134788 <-- 135582 Genome Browser

Strand:

reverse

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

46.16

External database links:

ASAP:

CGSC:

ECHOBASE:

ECOLIHUB:

NCBI-GENE:

OU-MICROARRAY:

STRING:

COLOMBOS:

Product

Name:

S-adenosylmethionine decarboxylase proenzyme

Synonym(s):

SpeD

Sequence:

Get amino acid sequence Fasta Format

Cellular location:

cytosol

Molecular weight:

30.385

Isoelectric point:

5.067

Motif(s):

Type	Positions	Sequence
	33 -> 169	DGYIAYIDELYNANRLTEILSETCSIIGANILNIARQDYEPQGASVTILVSEEPVDPKLIDKTEHPGPLPETVVAHLDKSHICVHTYPESHPEGGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTIDYRVRG
	112 -> 264	SHICVHTYPESHPEGGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTIDYRVRGFTRDINGMKHFIDHEINSIQNFMSDDMKALYDMVDVNVYQENIFHTKMLLKEFDLKHYMFHTKPEDLTDSERQEITAALWKEMREIYYGRNMPAV
	1 -> 111	MKKLKLHGFNNLTKSLSFCIYDICYAKTAEERDGYIAYIDELYNANRLTEILSETCSIIGANILNIARQDYEPQGASVTILVSEEPVDPKLIDKTEHPGPLPETVVAHLDK

Classification:

Multifun Terms (GenProtEC)
Multifun Terms (GenProtEC)		1 - metabolism --> 1.7 - central intermediary metabolism --> 1.7.14 - polyamine biosynthesis
Gene Ontology Terms (GO)
	cellular_component	GO:0005829 - cytosol
	molecular_function	GO:0003824 - catalytic activity GO:0016829 - lyase activity GO:0016831 - carboxy-lyase activity GO:0004014 - adenosylmethionine decarboxylase activity GO:0000287 - magnesium ion binding
	biological_process	GO:0008152 - metabolic process GO:0006596 - polyamine biosynthetic process GO:0008295 - spermidine biosynthetic process GO:0006557 - S-adenosylmethioninamine biosynthetic process GO:0097264 - self proteolysis

Note(s):

Note(s): ...[more].

Reference(s):

[1] Allen RR., et al., 1981
[2] Guo J., et al., 1995
[3] Hafner EW., et al., 1979
[4] Igarashi K., et al., 1986
[5] Kashiwagi K., et al., 1988
[6] Markham GD., et al., 1983
[7] Pegg AE. 1983
[8] Pegg AE., et al., 1986
[9] Pegg AE., et al., 1983
[10] Shirahata A., et al., 1985
[11] Weitkamp EL., et al., 1991
[12] Wu YQ., et al., 1993
[13] Xie QW., et al., 1989

External database links:

DIP:

ECOCYC:

ECOLIWIKI:

INTERPRO:

INTERPRO:

INTERPRO:

PANTHER:

PFAM:

PRIDE:

PRODB:

REFSEQ:

UNIPROT:

Reference(s)
[1] Allen RR., Klinman JP., 1981, Stereochemistry and kinetic isotope effects in the decarboxylation of S-adenosylmethionine catalyzed by the pyruvyl enzyme, S-adenosylmethionine decarboxylase., J Biol Chem 256(7):3233-9
[2] Guo J., Wu YQ., Rattendi D., Bacchi CJ., Woster PM., 1995, S-(5'-deoxy-5'-adenosyl)-1-aminoxy-4-(methylsulfonio)-2-cyclopentene (AdoMao): an irreversible inhibitor of S-adenosylmethionine decarboxylase with potent in vitro antitrypanosomal activity., J Med Chem 38(10):1770-7
[3] Hafner EW., Tabor CW., Tabor H., 1979, Mutants of Escherichia coli that do not contain 1,4-diaminobutane (putrescine) or spermidine., J Biol Chem 254(24):12419-26
[4] Igarashi K., Kashiwagi K., Hamasaki H., Miura A., Kakegawa T., Hirose S., Matsuzaki S., 1986, Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines., J Bacteriol 166(1):128-34
[5] Kashiwagi K., Taneja SK., Xie QW., Tabor CW., Tabor H., 1988, S-adenosylmethionine decarboxylase from Escherichia coli and from Saccharomyces cerevisiae: cloning and overexpression of the genes., Adv Exp Med Biol 250:73-9
[6] Markham GD., Tabor CW., Tabor H., 1983, S-adenosylmethionine decarboxylase (Escherichia coli)., Methods Enzymol 94:228-30
[7] Pegg AE., 1983, Inhibitors of S-adenosylmethionine decarboxylase., Methods Enzymol 94:239-47
[8] Pegg AE., Coward JK., Talekar RR., Secrist JA., 1986, Effects of certain 5'-substituted adenosines on polyamine synthesis: selective inhibitors of spermine synthase., Biochemistry 25(14):4091-7
[9] Pegg AE., Jacobs G., 1983, Comparison of inhibitors of S-adenosylmethionine decarboxylase from different species., Biochem J 213(2):495-502
[10] Shirahata A., Christman KL., Pegg AE., 1985, Quantitation of S-adenosylmethionine decarboxylase protein., Biochemistry 24(16):4417-23
[11] Weitkamp EL., Dixon HB., Khomutov AR., Khomutov RM., 1991, Effect of magnesium ions on the inhibition of S-adenosylmethionine decarboxylase from Escherichia coli by [2-(amino-oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulphonium ., Biochem J 277 ( Pt 3):643-5
[12] Wu YQ., Woster PM., 1993, Preparation of the pure diastereomeric forms of S-(5'-deoxy-5'-adenosyl)-1-ammonio-4-methylsulfonio-2-cyclopentene and their evaluation as irreversible inhibitors of S-adenosylmethionine decarboxylase from Escherichia coli., Bioorg Med Chem 1(5):349-60
[13] Xie QW., Tabor CW., Tabor H., 1989, Spermidine biosynthesis in Escherichia coli: promoter and termination regions of the speED operon., J Bacteriol 171(8):4457-65

Reference(s)

[1] Allen RR., Klinman JP., 1981, Stereochemistry and kinetic isotope effects in the decarboxylation of S-adenosylmethionine catalyzed by the pyruvyl enzyme, S-adenosylmethionine decarboxylase., J Biol Chem 256(7):3233-9

[2] Guo J., Wu YQ., Rattendi D., Bacchi CJ., Woster PM., 1995, S-(5'-deoxy-5'-adenosyl)-1-aminoxy-4-(methylsulfonio)-2-cyclopentene (AdoMao): an irreversible inhibitor of S-adenosylmethionine decarboxylase with potent in vitro antitrypanosomal activity., J Med Chem 38(10):1770-7

[3] Hafner EW., Tabor CW., Tabor H., 1979, Mutants of Escherichia coli that do not contain 1,4-diaminobutane (putrescine) or spermidine., J Biol Chem 254(24):12419-26

[4] Igarashi K., Kashiwagi K., Hamasaki H., Miura A., Kakegawa T., Hirose S., Matsuzaki S., 1986, Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines., J Bacteriol 166(1):128-34

[5] Kashiwagi K., Taneja SK., Xie QW., Tabor CW., Tabor H., 1988, S-adenosylmethionine decarboxylase from Escherichia coli and from Saccharomyces cerevisiae: cloning and overexpression of the genes., Adv Exp Med Biol 250:73-9

[6] Markham GD., Tabor CW., Tabor H., 1983, S-adenosylmethionine decarboxylase (Escherichia coli)., Methods Enzymol 94:228-30

[7] Pegg AE., 1983, Inhibitors of S-adenosylmethionine decarboxylase., Methods Enzymol 94:239-47

[8] Pegg AE., Coward JK., Talekar RR., Secrist JA., 1986, Effects of certain 5'-substituted adenosines on polyamine synthesis: selective inhibitors of spermine synthase., Biochemistry 25(14):4091-7

[9] Pegg AE., Jacobs G., 1983, Comparison of inhibitors of S-adenosylmethionine decarboxylase from different species., Biochem J 213(2):495-502

[10] Shirahata A., Christman KL., Pegg AE., 1985, Quantitation of S-adenosylmethionine decarboxylase protein., Biochemistry 24(16):4417-23

[11] Weitkamp EL., Dixon HB., Khomutov AR., Khomutov RM., 1991, Effect of magnesium ions on the inhibition of S-adenosylmethionine decarboxylase from Escherichia coli by [2-(amino-oxy)ethyl](5'-deoxyadenosin-5'-yl)(methyl)sulphonium ., Biochem J 277 ( Pt 3):643-5

[12] Wu YQ., Woster PM., 1993, Preparation of the pure diastereomeric forms of S-(5'-deoxy-5'-adenosyl)-1-ammonio-4-methylsulfonio-2-cyclopentene and their evaluation as irreversible inhibitors of S-adenosylmethionine decarboxylase from Escherichia coli., Bioorg Med Chem 1(5):349-60

[13] Xie QW., Tabor CW., Tabor H., 1989, Spermidine biosynthesis in Escherichia coli: promoter and termination regions of the speED operon., J Bacteriol 171(8):4457-65