Q97BP8 (SPEH_THEVO) 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:	TV0407
ORF Names:	TVG0395474

Organism

Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) [Complete proteome] [HAMAP]

Taxonomic identifier

273116 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma › Thermoplasma volcanium

Protein attributes

Sequence length	130 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-Rule MF_00464
Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. HAMAP-Rule MF_00464
Cofactor	Pyruvoyl group By similarity.
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP-Rule 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-Rule 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	S-adenosylmethioninamine biosynthetic process Inferred from electronic annotation. Source: HAMAP spermidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	adenosylmethionine decarboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 63	63	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_0000030159
	Chain	64 – 130	67	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000030160
Sites
	Active site	64	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	69	1	Proton acceptor; for processing activity By similarity
	Active site	84	1	Proton donor; for catalytic activity By similarity
	Site	63 – 64	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	64	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97BP8 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 92E6060AF363D3C3	FASTA	130	14,561
	10 20 30 40 50 60 MKVGVGIHII ADFYGVDSKL ISTTERMYPI IEGAVKYGRL TKISSDYYQF RPQGASGVVL 70 80 90 100 110 120 LAESHLSFHT WPEYGLVTLD IYTCGDPKTA DDAFEYLTRE LKPTSVTTRK IVRGDLVGEE 130 GLNEMQVEIH

References

[1]

"Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium." Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M. Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000011 Genomic DNA. Translation: BAB59549.1.
RefSeq	NP_110924.1. NC_002689.2.
3D structure databases
ProteinModelPortal	Q97BP8.
SMR	Q97BP8. Positions 4-121.
ModBase	Search...
Protein-protein interaction databases
STRING	273116.TVN0405.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB59549; BAB59549; BAB59549.
GeneID	1440921.
KEGG	tvo:TVN0405.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1586.
KO	K01611.
OMA	GNLYGCN.
ProtClustDB	PRK01236.
Enzyme and pathway databases
UniPathway	UPA00331; UER00451.
Family and domain databases
Gene3D	3.60.90.10. 1 hit.
HAMAP	MF_00464. AdoMetDC_1.
InterPro	IPR003826. S-AdoMet_decarboxylase-bac/arc. IPR016067. S-AdoMet_deCO2ase_core. IPR017716. S-AdoMet_deCOase_pro-enz. [Graphical view]
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_THEVO

Accession

Primary (citable) accession number: Q97BP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 24, 2001
Last sequence update:	October 1, 2001
Last modified:	May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program