C1EZJ4 (C1EZJ4_BACC3) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
S-adenosylmethionine decarboxylase proenzyme HAMAP-Rule MF_00464
Short name=AdoMetDC HAMAP-Rule MF_00464
Short name=SAMDC HAMAP-Rule MF_00464
EC=4.1.1.50 HAMAP-Rule MF_00464

Gene names

Name:	speD2 EMBL ACO29170.1
Synonyms:	speH HAMAP-Rule MF_00464
Ordered Locus Names:	BCA_5342 EMBL ACO29170.1

Organism

Bacillus cereus (strain 03BB102) [Complete proteome] [HAMAP] EMBL ACO29170.1

Taxonomic identifier

572264 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus cereus

Protein attributes

Sequence length	123 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_00464
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. HAMAP-Rule MF_00464
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. HAMAP-Rule MF_00464

Ontologies

Keywords
Biological process	Polyamine biosynthesis HAMAP-Rule MF_00464 Spermidine biosynthesis HAMAP-Rule MF_00464
Ligand	Pyruvate HAMAP-Rule MF_00464 S-adenosyl-L-methionine HAMAP-Rule MF_00464 Schiff base HAMAP-Rule MF_00464
Molecular function	Decarboxylase HAMAP-Rule MF_00464 Lyase
PTM	Autocatalytic cleavage HAMAP-Rule MF_00464 Zymogen HAMAP-Rule MF_00464
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
Sites
	Active site	65	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP-Rule MF_00464
	Active site	70	1	Proton acceptor; for processing activity By similarity HAMAP-Rule MF_00464
	Active site	85	1	Proton donor; for catalytic activity By similarity HAMAP-Rule MF_00464
	Site	64 – 65	2	Cleavage (non-hydrolytic); by autolysis By similarity HAMAP-Rule MF_00464
Amino acid modifications
	Modified residue	65	1	Pyruvic acid (Ser); by autocatalysis By similarity HAMAP-Rule MF_00464

Sequences

	Sequence		Length	Mass (Da)
	C1EZJ4 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: 3AD4589D240EE3A3	FASTA	123	13,815
	10 20 30 40 50 60 MEYSTFGKHI IVDLWGVDFS LLDDMYFLEH HLVHAAALSG AHVLNVSTKE FHPHGVTVLV 70 80 90 100 110 120 LLSESHLSIH TYPEKNFAAI DCYTCGTTVE PQIAIDYIVS ILEPNEMHIK RLIRGIGEIV NTD

References

[1]	"Genome sequence of Bacillus cereus 03BB102." Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C., Sutton G., Sims D. Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 03BB102 EMBL ACO29170.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001407 Genomic DNA. Translation: ACO29170.1.
RefSeq	YP_002752553.1. NC_012472.1.
3D structure databases
ProteinModelPortal	C1EZJ4.
ModBase	Search...
Protein-protein interaction databases
STRING	572264.BCA_5342.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACO29170; ACO29170; BCA_5342.
GeneID	7691600.
KEGG	bcx:BCA_5342.
PATRIC	18823849. VBIBacCer84800_5212.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1586.
HOGENOM	HOG000216579.
KO	K01611.
OMA	EYSTFGR.
ProtClustDB	PRK01706.
Enzyme and pathway databases
BioCyc	BCER572264:GH22-3531-MONOMER.
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

C1EZJ4_BACC3

Accession

Primary (citable) accession number: C1EZJ4

Entry history

Integrated into UniProtKB/TrEMBL:	May 26, 2009
Last sequence update:	May 26, 2009
Last modified:	May 1, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)