Q6KZI1 (SPEH_PICTO) 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:	PTO1286

Organism

Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) [Complete proteome] [HAMAP]

Taxonomic identifier

263820 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Picrophilaceae › Picrophilus

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 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 – 63	63	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_0000030135
	Chain	64 – 130	67	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000030136
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)
	Q6KZI1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: ADA852AD04D33172	FASTA	130	14,599
	10 20 30 40 50 60 MKVAVGVHII ADLYGVDARL ISSSEAISPI MENAIQEGHL TKISSEYYQF RPMGASGIAL 70 80 90 100 110 120 LAESHLSFHT WPEYGLVTLD IYTCGDRSNA DRAFDYIIKV LKPTSVDYRK MERGSQIKED 130 VRITDPQMML

References

[1]

"Genome sequence of Picrophilus torridus and its implications for life around pH 0." Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C., Schepers B., Dock C., Antranikian G., Liebl W. Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004) [PubMed: 15184674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017261 Genomic DNA. Translation: AAT43871.1.
RefSeq	YP_024064.1. NC_005877.1.
3D structure databases
ProteinModelPortal	Q6KZI1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2844387.
GenomeReviews	Gene locus PTO1286 in contig AE017261_GR.
KEGG	pto:PTO1286.
NMPDR	fig|263820.1.peg.1286.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG485559.
OMA	SYFFKFS.
ProtClustDB	PRK01236.
Enzyme and pathway databases
BioCyc	PTOR263820:PTO1286-MONOMER.
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_PICTO

Accession

Primary (citable) accession number: Q6KZI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 5, 2004
Last modified:	November 16, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program