A6VCN1 (SPEH_PSEA7) 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:	PSPA7_5494

Organism

Pseudomonas aeruginosa (strain PA7) [Complete proteome] [HAMAP]

Taxonomic identifier

381754 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	160 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 – 72	72	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_1000013681
	Chain	73 – 160	88	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000315030
Sites
	Active site	73	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	78	1	Proton acceptor; for processing activity By similarity
	Active site	93	1	Proton donor; for catalytic activity By similarity
	Site	72 – 73	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	73	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6VCN1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 7D0506A8FAEE07CB	FASTA	160	17,208
	10 20 30 40 50 60 MAIQPLRLDP ITVLGKQLVI ELFDCVDTRF DDIQWIEESM LEAARQANAT IITSAFHKFS 70 80 90 100 110 120 PIGISGVVVI AESHLAIHTW PEYGYAAVDV FTCGDVLDGA QAVRVLSERL GSQRHLISSM 130 140 150 160 DRGLGGHRLG LLSRSLAGNA PVDGDSPTLR WALGQGTGVA

References

[1]	Dodson R.J., Harkins D., Paulsen I.T. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PA7.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000744 Genomic DNA. Translation: ABR82327.1.
RefSeq	YP_001350816.1. NC_009656.1.
3D structure databases
ProteinModelPortal	A6VCN1.
ModBase	Search...
Protein-protein interaction databases
STRING	A6VCN1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5356663.
GenomeReviews	Gene locus PSPA7_5494 in contig CP000744_GR.
KEGG	pap:PSPA7_5494.
PATRIC	19832483. VBIPseAer80442_5220.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1586.
HOGENOM	HBG485559.
OMA	ISNKFEP.
PhylomeDB	A6VCN1.
ProtClustDB	CLSK868886.
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_PSEA7

Accession

Primary (citable) accession number: A6VCN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	August 21, 2007
Last modified:	December 14, 2011
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program