Q0T880 (SPED_SHIF8) 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:	speD
Ordered Locus Names:	SFV_0111

Organism

Shigella flexneri serotype 5b (strain 8401) [Complete proteome] [HAMAP]

Taxonomic identifier

373384 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	264 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_00465
Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. HAMAP MF_00465
Cofactor	Pyruvoyl group By similarity. HAMAP MF_00465
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP MF_00465
Subunit structure	Heterooctamer of four alpha and four beta chains arranged as a tetramer 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_00465
Sequence similarities	Belongs to the prokaryotic AdoMetDC family. Type 2 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 – 111	111	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_1000013692
	Chain	112 – 264	153	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000315018
Sites
	Active site	112	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	117	1	Proton acceptor; for processing activity By similarity
	Active site	140	1	Proton donor; for catalytic activity By similarity
	Site	111 – 112	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	112	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0T880 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: E228BCF8EBDD0325	FASTA	264	30,385
	10 20 30 40 50 60 MKKLKLHGFN NLTKSLSFCI YDICYAKTAE ERDGYIAYID ELYNANRLTE ILSETCSIIG 70 80 90 100 110 120 ANILNIARQD YEPQGASVTI LVSEEPVDPK LIDKTEHPGP LPETVVAHLD KSHICVHTYP 130 140 150 160 170 180 ESHPEGGLCT FRADIEVSTC GVISPLKALN YLIHQLESDI VTIDYRVRGF TRDINGMKHF 190 200 210 220 230 240 IDHEINSIQN FMSDDMKALY DMVDVNVYQE NIFHTKMLLK EFDLKHYMFH TKPEDLTDSE 250 260 RQEITAALWK EMREIYYGRN MPAV

References

[1]

"Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a." Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q. BMC Genomics 7:173-173(2006) [PubMed: 16822325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 8401.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000266 Genomic DNA. Translation: ABF02396.1.
RefSeq	YP_687701.1. NC_008258.1.
3D structure databases
ProteinModelPortal	Q0T880.
SMR	Q0T880. Positions 43-174.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0T880.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000095423; EBESCP00000091619; EBESCG00000094467.
GeneID	4210133.
GenomeReviews	Gene locus SFV_0111 in contig CP000266_GR.
KEGG	sfv:SFV_0111.
PATRIC	18723144. VBIShiFle33408_0129.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1586.
GeneTree	EBGT00050000009049.
HOGENOM	HBG303125.
OMA	ISTFRAD.
ProtClustDB	PRK05462.
Enzyme and pathway databases
BioCyc	SFLE373384:SFV_0111-MONOMER.
Family and domain databases
HAMAP	MF_00465. AdoMetDC_2. [Tree]
InterPro	IPR003826. S-AdoMet_decarboxylase-bac/arc. IPR009165. S-AdoMet_deCO2ase_bac. IPR016067. S-AdoMet_deCO2ase_core. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
KO	K01611.
Pfam	PF02675. AdoMet_dc. 1 hit. [Graphical view]
PIRSF	PIRSF001356. SAM_decarboxylas. 1 hit.
SUPFAM	SSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMs	TIGR03331. SAM_DCase_Eco. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SPED_SHIF8

Accession

Primary (citable) accession number: Q0T880

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program