Q8ZBJ7 (SPED_YERPE) 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:	YPO3412, y0774, YP_0273

Organism

Yersinia pestis [Reference proteome] [HAMAP]

Taxonomic identifier

632 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

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-Rule MF_00465
Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. HAMAP-Rule MF_00465
Cofactor	Pyruvoyl group By similarity.
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP-Rule 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-Rule 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 Reference 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
Molecule processing
	Chain	1 – 111	111	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_0000030075
	Chain	112 – 264	153	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000030076
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)
	Q8ZBJ7 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: E4C0AEE946FEDC89	FASTA	264	30,293
	10 20 30 40 50 60 MSKLKLHGFN NLTKSLSFCI YDICYAKTAD DRDGYIAYID EQYNANRLTE ILSETCSIIG 70 80 90 100 110 120 ANILNIARQD YDPQGASVTI LVSEEPVDPR DVDTSEHPGP LPSAVVAHLD KSHICVHTYP 130 140 150 160 170 180 ESHPEAGLCT FRADIEVSTC GVISPLKALN YLIHQLESDI VTMDYRVRGF TRDINGVKHF 190 200 210 220 230 240 IDHKINSIQN FMSDDMKSLY HMMDVNVYQE NIFHTKMMLK DFDLKHYLFN AKPEELSAEE 250 260 KEQITRLLYK EMQEIYYGRN VPEV

References

[1]	"Genome sequence of Yersinia pestis, the causative agent of plague." Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CO-92 / Biovar Orientalis.
[2]	"Genome sequence of Yersinia pestis KIM." Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. , Matson J.S., Blattner F.R., Perry R.D. J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KIM10+ / Biovar Mediaevalis.
[3]	"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans." Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R. DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL590842 Genomic DNA. Translation: CAL22001.1. AE009952 Genomic DNA. Translation: AAM84361.1. AE017042 Genomic DNA. Translation: AAS60549.1.
PIR	AF0414.
RefSeq	NP_668110.1. NC_004088.1. NP_991672.1. NC_005810.1. YP_002348304.1. NC_003143.1.
3D structure databases
ProteinModelPortal	Q8ZBJ7.
ModBase	Search...
Protein-protein interaction databases
STRING	214092.YPO3412.
Proteomic databases
PRIDE	Q8ZBJ7.
Protocols and materials databases
DNASU	1145721.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM84361; AAM84361; y0774. AAS60549; AAS60549; YP_0273.
GeneID	1145721. 1176229. 2766455.
KEGG	ype:YPO3412. ypk:y0774. ypm:YP_0273.
Phylogenomic databases
eggNOG	COG1586.
HOGENOM	HOG000116821.
KO	K01611.
OMA	ISTFRAD.
ProtClustDB	PRK05462.
Enzyme and pathway databases
UniPathway	UPA00331; UER00451.
Family and domain databases
Gene3D	3.60.90.10. 1 hit.
HAMAP	MF_00465. AdoMetDC_2.
InterPro	IPR003826. S-AdoMet_decarboxylase-bac/arc. IPR009165. S-AdoMet_deCO2ase_bac. IPR016067. S-AdoMet_deCO2ase_core. [Graphical view]
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_YERPE

Accession

Primary (citable) accession number: Q8ZBJ7
Secondary accession number(s): Q0WBN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program