P57304 (SPED_BUCAI) 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:	BU208

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	265 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 Reference 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 – 113	113	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_0000030035
	Chain	114 – 265	152	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000030036
Sites
	Active site	114	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	119	1	Proton acceptor; for processing activity By similarity
	Active site	142	1	Proton donor; for catalytic activity By similarity
	Site	113 – 114	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	114	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P57304 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 1709CCED2B8661CC	FASTA	265	30,919
	10 20 30 40 50 60 MIKLQKLKLY GFNNLTKSLS FCIYDICYAN TNDSRNSYIS YIDEQYNAIR LTKILKKTCS 70 80 90 100 110 120 IIGANVLNIF HQDYEPQGAS VTILVCEEPM SMEKIDALNK NIVSSSVLAH LDKSHICVHT 130 140 150 160 170 180 YPESHPQSGI CTFRADIEVS TCGIISPLNA LNYLIHQLES DIVTIEYRVR GFTRDIHGIK 190 200 210 220 230 240 HFIDHKINSI QNFMSDDIKS MYDMVDVNVY QENIFHTRML LREFNLKNYL FNINLENLEK 250 260 EERSYIKKLL SKEMREIYYG RNISR

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12925.1.
RefSeq	NP_240039.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57304.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000003224; EBBUCP00000003000; EBBUCG00000003224.
GeneID	1109651.
GenomeReviews	Gene locus BU208 in contig BA000003_GR.
KEGG	buc:BU208.
PATRIC	21243936. VBIBucAph127364_0220.
Phylogenomic databases
GeneTree	EBGT00050000008111.
HOGENOM	HBG303125.
OMA	ISTFRAD.
PhylomeDB	P57304.
ProtClustDB	PRK05462.
Enzyme and pathway databases
BioCyc	BSP107806:BU208-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_BUCAI

Accession

Primary (citable) accession number: P57304

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program