Reviewed, UniProtKB/Swiss-Prot Q43820 (DCAM_PEA)

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- Recommended name:
            S-adenosylmethionine decarboxylase alpha chain
    2- Recommended name:
            S-adenosylmethionine decarboxylase beta chain

Gene names

Name:

SAMDC

Organism

Pisum sativum (Garden pea)

Taxonomic identifier

3888 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2.
Cofactor	Pyruvoyl group By similarity.
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
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.
Sequence similarities	Belongs to the eukaryotic AdoMetDC family.

Ontologies

Keywords
Biological process	Polyamine biosynthesis Spermidine biosynthesis
Ligand	Pyruvate S-adenosyl-L-methionine Schiff base
Molecular function	Decarboxylase Lyase
PTM	Autocatalytic cleavage Zymogen
Gene Ontology (GO)
Biological process	spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW spermine biosynthetic process Inferred from electronic annotation. Source: InterPro
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 – 68	68	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_0000030019
	Chain	69 – 353	285	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000030020
Sites
	Active site	9	1	By similarity
	Active site	12	1	By similarity
	Active site	69	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	83	1	Proton donor; for catalytic activity By similarity
	Active site	232	1	Proton acceptor; for processing activity By similarity
	Active site	245	1	Proton acceptor; for processing activity By similarity
	Site	68 – 69	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	69	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q43820-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 51FACD264FEBD30B	FASTA	353	38,683
	10 20 30 40 50 60 MAVSAIGFEG FEKRLEISFS DPGLFSDPQG RGLRSLTKSQ LDEILAPAEC TIVSSLANED 70 80 90 100 110 120 VDSYVLSESS LFVYAYKLII KTCGTTKLLL SIPPILKLAD SISLNVRSVR YTRGSFIFPG 130 140 150 160 170 180 AQSFPHRHFS EEVAVLDGFF GKLGSGSMAY ILGGSDEAQN WHIYCASSDS VSPEGSVYTL 190 200 210 220 230 240 EMCMTGLDRE KASVFFKEQT GSAAEMTVNS GIRKILRNSE ICDFDFEPCG YSMNSVEGSA 250 260 270 280 290 300 VSTIHITPED GFSYASFETA GYDLKAINLN EMVMRVLACF QPTEFSVAVH VDNASKSFEQ 310 320 330 340 350 GCLLDVKGYC CEEKSHQGLG MSGSVVYQKF LKTSYCGSPR STLKCWKDED EEE

References

[1]	"Expression of the pea S-adenosylmethionine decarboxylase gene is involved in developmental and environmental responses." Marco F., Carrasco P. Planta 214:641-647(2002) [PubMed: 11925048] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Alaska.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U60592 mRNA. Translation: AAB03865.1.
PIR	T06515.
3D structure databases
HSSP	HSSP built from PDB template 1JEN based on UniProtKB P17707.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.1.50. 287.
Family and domain databases
InterPro	IPR001985. S-AdoMet_decarboxylase. IPR018167. S-AdoMet_decarboxylase_sg. IPR016067. S-AdoMet_deCO2ase_core. IPR018166. S-AdoMet_deCO2ase_CS. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
PANTHER	PTHR11570. SAM_decarbox. 1 hit.
Pfam	PF01536. SAM_decarbox. 1 hit. [Graphical view]
PIRSF	PIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
ProDom	PD002379. SAM_decarbox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00535. SAM_DCase. 1 hit.
PROSITE	PS01336. ADOMETDC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCAM_PEA

Accession

Primary (citable) accession number: Q43820

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)