Q895G3 (SPEH_CLOTE) 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:	CTC_01312

Organism

Clostridium tetani [Complete proteome] [HAMAP]

Taxonomic identifier

1513 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	126 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_0000030103
	Chain	63 – 126	64	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000030104
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)
	Q895G3 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D8FA2E8D9389F992	FASTA	126	13,996
	10 20 30 40 50 60 MNNLGRHILA EIYGCDELIL NDKEYIERIM VDSALKSGAE VREVAFHKFS PQGVSGVVII 70 80 90 100 110 120 SESHLTIHTW PELGYAAVDV FTCGDRVNPW DACNYMGEKL NAKNITATEV KRGIFEQPVA VKASNE

References

[1]

"The genome sequence of Clostridium tetani, the causative agent of tetanus disease." Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G. Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed: 12552129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Massachusetts / E88.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015927 Genomic DNA. Translation: AAO35877.1.
RefSeq	NP_781940.1. NC_004557.1.
3D structure databases
ProteinModelPortal	Q895G3.
SMR	Q895G3. Positions 3-117.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1059115.
GenomeReviews	Gene locus CTC_01312 in contig AE015927_GR.
KEGG	ctc:CTC01312.
NMPDR	fig|212717.1.peg.1162.
PATRIC	19510589. VBICloTet101274_1342.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG485559.
OMA	ISNKFEP.
ProtClustDB	PRK03124.
Enzyme and pathway databases
BioCyc	CTET212717:CTC_01312-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_CLOTE

Accession

Primary (citable) accession number: Q895G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program