P0A7F6 (SPED_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine decarboxylase proenzyme
Short name=AdoMetDC
Short name=SAMDC
EC=4.1.1.50

Cleaved into the following 2 chains:

1. S-adenosylmethionine decarboxylase beta chain
2. S-adenosylmethionine decarboxylase alpha chain

Gene names

Name:	speD
Ordered Locus Names:	b0120, JW0116

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. HAMAP MF_00465
Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. Ref.6
Cofactor	Pyruvoyl group. Ref.1 Ref.5 Ref.6
Enzyme regulation	Allosterically activated by metal cations, which are absolutely required for activity. The presumed physiological activator is Mg2+, but can also be activated in vitro by other divalent cations such as Mn2+, Fe2+ and Ca2+, by the monovalent cation Li+, and by trivalent cations such as Eu3+, Tb3+ and Gd3+. Competitively inhibited by methylglyoxal bis-guanylhydrazone. Also inhibited by Zn2+, inhibition may be due to interaction with the active site cysteine. Inactivated by treatment with the imine reductant NaCNBH3 only in the presence of substrate. Ref.5 Ref.6 Ref.8
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP MF_00465
Subunit structure	Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers. Ref.5
Post-translational modification	Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain. HAMAP MF_00465
Miscellaneous	Spermidine-deficient mutants show a small decrease in growth rate and increased sensibility to superoxide toxicity. HAMAP MF_00465
Sequence similarities	Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=60 µM for S-adenosyl-L-methionine (at 25 degrees Celsius in the presence of 0.01 M MgCl2) Ref.6 Vmax=3.8 µmol/min/mg enzyme (at 25 degrees Celsius in the presence of 0.01M MgCl2) Vmax=6.8 µmol/min/mg enzyme (at 37 degrees Celsius in the presence of 0.1M MgCl2) pH dependence: Optimum pH is 7.4. Active from pH 6.7 to 8.5.

Ontologies

Keywords
Biological process	Polyamine biosynthesis Spermidine biosynthesis
Ligand	Magnesium Pyruvate S-adenosyl-L-methionine Schiff base
Molecular function	Decarboxylase Lyase
PTM	Autocatalytic cleavage Zymogen
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	adenosylmethionine decarboxylase activity Inferred from mutant phenotype. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 111	111	S-adenosylmethionine decarboxylase beta chain HAMAP MF_00465		PRO_0000030043
	Chain	112 – 264	153	S-adenosylmethionine decarboxylase alpha chain HAMAP MF_00465		PRO_0000030044
Sites
	Active site	112	1	Schiff-base intermediate with substrate; via pyruvic acid
	Active site	117	1	Proton acceptor; for processing activity By similarity
	Active site	140	1	Proton donor; for catalytic activity By similarity
	Site	111 – 112	2	Cleavage (non-hydrolytic); by autolysis
Amino acid modifications
	Modified residue	112	1	Pyruvic acid (Ser); by autocatalysis HAMAP MF_00465

Sequences

	Sequence		Length	Mass (Da)
	P0A7F6 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: E228BCF8EBDD0325	FASTA	264	30,385
	10 20 30 40 50 60 MKKLKLHGFN NLTKSLSFCI YDICYAKTAE ERDGYIAYID ELYNANRLTE ILSETCSIIG 70 80 90 100 110 120 ANILNIARQD YEPQGASVTI LVSEEPVDPK LIDKTEHPGP LPETVVAHLD KSHICVHTYP 130 140 150 160 170 180 ESHPEGGLCT FRADIEVSTC GVISPLKALN YLIHQLESDI VTIDYRVRGF TRDINGMKHF 190 200 210 220 230 240 IDHEINSIQN FMSDDMKALY DMVDVNVYQE NIFHTKMLLK EFDLKHYMFH TKPEDLTDSE 250 260 RQEITAALWK EMREIYYGRN MPAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The speEspeD operon of Escherichia coli. Formation and processing of a proenzyme form of S-adenosylmethionine decarboxylase." Tabor C.W., Tabor H. J. Biol. Chem. 262:16037-16040(1987) [PubMed: 3316212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SELF-PROCESSING, CLEAVAGE SITE, COFACTOR.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Escherichia coli S-adenosylmethionine decarboxylase. Subunit structure, reductive amination, and NH2-terminal sequences." Anton D.L., Kutny R. J. Biol. Chem. 262:2817-2822(1987) [PubMed: 3546296] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21 AND 112-143, SELF-PROCESSING, CLEAVAGE SITE, COFACTOR, ENZYME REGULATION, SUBUNIT.
[6]	"S-adenosylmethionine decarboxylase of Escherichia coli. Studies on the covalently linked pyruvate required for activity." Markham G.D., Tabor C.W., Tabor H. J. Biol. Chem. 257:12063-12068(1982) [PubMed: 6749853] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SCHIFF BASE FORMATION. Strain: K12.
[7]	"Paraquat toxicity is increased in Escherichia coli defective in the synthesis of polyamines." Minton K.W., Tabor H., Tabor C.W. Proc. Natl. Acad. Sci. U.S.A. 87:2851-2855(1990) [PubMed: 2181453] [Abstract] Cited for: SENSITIVITY OF MUTANTS.
[8]	"Metal ion activation of S-adenosylmethionine decarboxylase reflects cation charge density." Lu Z.J., Markham G.D. Biochemistry 46:8172-8180(2007) [PubMed: 17567041] [Abstract] Cited for: ALLOSTERIC METAL ION ACTIVATION, ENZYME REGULATION, PH DEPENDENCE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02804 Genomic DNA. Translation: AAA24644.1. U00096 Genomic DNA. Translation: AAC73231.1. AP009048 Genomic DNA. Translation: BAB96694.1.
PIR	DCECDM. B29778.
RefSeq	NP_414662.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A7F6.
SMR	P0A7F6. Positions 43-174.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47936N.
IntAct	P0A7F6. 4 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000405; EBESCP00000000405; EBESCG00000000335. EBESCT00000016578; EBESCP00000015869; EBESCG00000015637.
GeneID	947719.
GenomeReviews	Gene locus JW0116 in contig AP009048_GR. Gene locus b0120 in contig U00096_GR.
KEGG	ecj:JW0116. eco:b0120.
PATRIC	32115341. VBIEscCol129921_0122.
Organism-specific databases
EchoBASE	EB0955.
EcoGene	EG10962. speD.
Phylogenomic databases
eggNOG	COG1586.
GeneTree	EBGT00050000009049.
HOGENOM	HBG303125.
OMA	ISTFRAD.
ProtClustDB	PRK05462.
Enzyme and pathway databases
BioCyc	EcoCyc:SPED-MONOMER. MetaCyc:SPED-MONOMER.
Gene expression databases
Genevestigator	P0A7F6.
Family and domain databases
HAMAP	MF_00465. AdoMetDC_2. [Tree]
InterPro	IPR003826. S-AdoMet_decarboxylase-bac/arc. IPR009165. S-AdoMet_deCO2ase_bac. IPR016067. S-AdoMet_deCO2ase_core. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
KO	K01611.
Pfam	PF02675. AdoMet_dc. 1 hit. [Graphical view]
PIRSF	PIRSF001356. SAM_decarboxylas. 1 hit.
SUPFAM	SSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMs	TIGR03331. SAM_DCase_Eco. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SPED_ECOLI

Accession

Primary (citable) accession number: P0A7F6
Secondary accession number(s): P09159

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program