Reviewed, UniProtKB/Swiss-Prot Q42679 (DCAM_CATRO)

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

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

Taxonomic identifier

4058 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Vinceae › Catharanthus

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2.
Cofactor	Pyruvoyl group.
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.
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 – 70	70	S-adenosylmethionine decarboxylase beta chain		PRO_0000029997
	Chain	71 – 357	287	S-adenosylmethionine decarboxylase alpha chain		PRO_0000029998
Sites
	Active site	11	1	By similarity
	Active site	14	1	By similarity
	Active site	71	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	85	1	Proton donor; for catalytic activity By similarity
	Active site	234	1	Proton acceptor; for processing activity By similarity
	Active site	247	1	Proton acceptor; for processing activity By similarity
	Site	70 – 71	2	Cleavage (non-hydrolytic); by autolysis
Amino acid modifications
	Modified residue	71	1	Pyruvic acid (Ser); by autocatalysis
Experimental info
	Mutagenesis	71	1	S → A: Loss of activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q42679-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 364918E116388301	FASTA	357	39,714
	10 20 30 40 50 60 MALPASAIGF EGYEKRLEIS FFESSFFADP DGKGLRALNK SQIDEILEPA ECTIVDSLSN 70 80 90 100 110 120 QYLDSYVLSE SSLFVYPYKI IIKTCGTTKL LLSIPAILKL AESLSLSVRN VKYTRGSFIF 130 140 150 160 170 180 PGAQSFPHRS FSEEVELLDN YFGKLGLESN AFIMGNPDQP QKWHVYSASV GSEQSSDPTY 190 200 210 220 230 240 TLEMCMTGLD REKASVFYKS ESSSAALMTT RSGIRKILPD SEICDFEFDP CGYSMNSIEE 250 260 270 280 290 300 AAISTIHVTP EDGFSYASFE AAGYDLKAQN LGMMIERVLA CFQPSEFSVA VHCDVTCKSL 310 320 330 340 350 EQICSLELKE YSLDEKINEE LGLGGSIIYK KFLRIDACGS PRSILKCCWK EDESEEE

References

[1]

"cDNAs for S-adenosyl-L-methionine decarboxylase from Catharanthus roseus, heterologous expression, identification of the proenzyme-processing site, evidence for the presence of both subunits in the active enzyme, and a conserved region in the 5' mRNA leader." Schroeder G., Schroeder J. Eur. J. Biochem. 228:74-78(1995) [PubMed: 7883014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PYRUVATE FORMATION AT SER-71, MUTAGENESIS OF SER-71.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U12573 mRNA. Translation: AAC48989.1.
PIR	S68990.
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. 20471.
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_CATRO

Accession

Primary (citable) accession number: Q42679

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)