Q0AZ53 (SPEH_SYNWW) 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:	Swol_0674

Organism

Syntrophomonas wolfei subsp. wolfei (strain Goettingen) [Complete proteome] [HAMAP]

Taxonomic identifier

335541 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Syntrophomonadaceae › Syntrophomonas

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_1000013685
	Chain	63 – 126	64	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000315034
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)
	Q0AZ53 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: E6D302E174B1660D	FASTA	126	14,019
	10 20 30 40 50 60 MQSLGRHVLA EIYGCRFEVL NDVKKVEDIM VNAALEAGAE IREFVFHKFS PQGVSGVVVI 70 80 90 100 110 120 SESHLAIHTW PELGYAALDV FTCGDRVNPW DACNYVAEMF SAGDMKASEV KRGLMEQPEE RLVANM

References

[1]

"Complete sequence of Syntrophomonas wolfei subsp. wolfei str. Goettingen." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Sims D., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R., McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J., Stams A.J.M., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Goettingen.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000448 Genomic DNA. Translation: ABI68001.1.
RefSeq	YP_753372.1. NC_008346.1.
3D structure databases
ProteinModelPortal	Q0AZ53.
SMR	Q0AZ53. Positions 2-116.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0AZ53.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4281195.
GenomeReviews	Gene locus Swol_0674 in contig CP000448_GR.
KEGG	swo:Swol_0674.
PATRIC	23856095. VBISynWol51738_0715.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1586.
HOGENOM	HBG485559.
OMA	SYFFKFS.
ProtClustDB	PRK03124.
Enzyme and pathway databases
BioCyc	SWOL335541:SWOL_0674-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_SYNWW

Accession

Primary (citable) accession number: Q0AZ53

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program