B6YV04 (SPEH_THEON) 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:	speH
Ordered Locus Names:	TON_1742

Organism

Thermococcus onnurineus (strain NA1) [Complete proteome] [HAMAP]

Taxonomic identifier

523850 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

Protein attributes

Sequence length	141 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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 By similarity. HAMAP MF_00464
Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. HAMAP MF_00464
Cofactor	Pyruvoyl group By similarity. HAMAP MF_00464
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP MF_00464
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers By similarity.
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 By similarity. HAMAP MF_00464
Sequence similarities	Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Ontologies

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 62	62	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_1000125467
	Chain	63 – 141	79	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_1000125468
Sites
	Active site	63	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	68	1	Proton acceptor; for processing activity By similarity
	Active site	83	1	Proton donor; for catalytic activity By similarity
	Site	62 – 63	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	63	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	B6YV04 [UniParc]. Last modified January 20, 2009. Version 1. Checksum: 02A169AA600AA184	FASTA	141	15,789
	10 20 30 40 50 60 METIGFHYVV EAAGCDPEIL GNADKIRQIF LEAAKVGKME VKASYFFKFS PTGVSGVVIV 70 80 90 100 110 120 AESHISIHTW PEKGYAALDV YTCGTTADPE KAVDYILDKI KAQYAHVSEI KRGIEEDDET 130 140 FTHMILTWEE KLERKNGDEK S

References

[1]

"The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism." Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H., Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J., Colwell R.R., Kim S.-J., Lee J.-H. J. Bacteriol. 190:7491-7499(2008) [PubMed: 18790866] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000855 Genomic DNA. Translation: ACJ17232.1.
RefSeq	YP_002308129.1. NC_011529.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B6YV04.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7017411.
GenomeReviews	Gene locus TON_1742 in contig CP000855_GR.
KEGG	ton:TON_1742.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG485559.
OMA	SYFFKFS.
ProtClustDB	PRK04025.
Family and domain databases
HAMAP	MF_00464. AdoMetDC_1. [Tree]
InterPro	IPR003826. S-AdoMet_decarboxylase-bac/arc. IPR016067. S-AdoMet_deCO2ase_core. IPR017716. S-AdoMet_deCOase_pro-enz. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
KO	K01611.
Pfam	PF02675. AdoMet_dc. 1 hit. [Graphical view]
SUPFAM	SSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMs	TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SPEH_THEON

Accession

Primary (citable) accession number: B6YV04

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	January 20, 2009
Last modified:	November 16, 2011
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program