RegulonDB RegulonDB 10.9: Gene Form
   

speD gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

speE speD yacL speDp speDp

Gene      
Name: speD    Texpresso search in the literature
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


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)  
  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:
DIP-47936N
ECOCYC:
SPED-MONOMER
ECOLIWIKI:
b0120
INTERPRO:
IPR009165
INTERPRO:
IPR016067
INTERPRO:
IPR003826
PANTHER:
PTHR33866
PFAM:
PF02675
PRIDE:
P0A7F6
PRODB:
PRO_000023974
REFSEQ:
NP_414662
UNIPROT:
P0A7F6


Operon      
Name: yacC-speED         
Operon arrangement:
Transcription unit        Promoter
speD
speE
yacC-speED


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References


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


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